|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1-1293 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 2309.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1 MTTRLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFG 80
Cdd:PRK10252 4 MSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 81 EPSIIDLRTAPDPHRAATERMQADLAQDLRVDGGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAW 160
Cdd:PRK10252 84 LPEIIDLRTQPDPHAAAQALMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 161 QRGEATPESPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRLA 240
Cdd:PRK10252 164 LRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 241 GHAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKKM 320
Cdd:PRK10252 244 AQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 321 RRHQRYDAEQIVRDSGKAAGDEPLFGPVLNVKVFDYQLDIDGVQAVTHTLATGPVNDLELALFPDETGGLSLEILANKAR 400
Cdd:PRK10252 324 RRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELALFPDEHGGLSIEILANPQR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 401 YDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARLAAVNDTVVPLPATTLSALVADQARKTPDAPALADARWQ 480
Cdd:PRK10252 404 YDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 DQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVA 640
Cdd:PRK10252 564 DQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 641 QKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADS-VAACRTLRRVF 719
Cdd:PRK10252 644 QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGaRQSCASLRQVF 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTGSSVPIGWPVWNTGLRILDAAMRPVPPGVAG 799
Cdd:PRK10252 724 CSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAG 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 800 DLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLP 879
Cdd:PRK10252 804 DLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALP 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 880 DVAQAVSHACVFNQAAATGGDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPL 959
Cdd:PRK10252 884 DVEQAVTHACVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 960 PTLGGERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQLSRQLARQVTPGQVMVASTVGKLSA 1039
Cdd:PRK10252 964 PELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLAT 1043
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1040 LLAADlSDEQArRLGLDTLLPLRESDGPTLFCFHPASGFAWQFSVLARYLSPRWSITGIQSPRPQGPMASAASLDEVCEH 1119
Cdd:PRK10252 1044 LLDAE-EDESR-RLGFGTILPLREGDGPTLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEA 1121
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1120 HLRTLLAQQPHGPYYLFGYSLGGTLAQGIAARLRQRGEAVAFLGLLDTWPPETQNWAEKEANGLDPEVLAEIDREREAFL 1199
Cdd:PRK10252 1122 HLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPETQNWREKEANGLDPEVLAEIDREREAFL 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1200 AAQQGQASGELFSAIEGNYADAVRLLTTAHSAKFDGKATLFVAEKTRQAGMDPQVVWGPWVAELEVFSQNCAHVDIISPQ 1279
Cdd:PRK10252 1202 AAQQGSLSTELFTTIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEGMSPEQAWSPWIAELDVYRQDCAHVDIISPE 1281
|
1290
....*....|....
gi 635952396 1280 AFEAIGPVVREILG 1293
Cdd:PRK10252 1282 AFEKIGPILRATLN 1295
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-1268 |
0e+00 |
|
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: 744.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 3 TRLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFGEP 82
Cdd:COG1020 16 APLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 83 SIIDLRTAPDPHRAATERMQADLAQDLRVDGGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQR 162
Cdd:COG1020 96 VVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 163 GEATPESP-FTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRLAG 241
Cdd:COG1020 176 GAPLPLPPlPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 242 HAPQCQ--PADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKK 319
Cdd:COG1020 256 LARRHGvtLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 320 MRRHQRYDAEQIVRDSG--KAAGDEPLFGPVLNVKVFDY-QLDIDGVQAVTHTLATGPVN-DLELALFPDEtGGLSLEIL 395
Cdd:COG1020 336 AYAHQDLPFERLVEELQpeRDLSRNPLFQVMFVLQNAPAdELELPGLTLEPLELDSGTAKfDLTLTVVETG-DGLRLTLE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 396 ANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELAR-LAAVNDTVVPLPA-TTLSALVADQARKTPDAPA 473
Cdd:COG1020 415 YNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQlLAEWNATAAPYPAdATLHELFEAQAARTPDAVA 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 474 LADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARP 553
Cdd:COG1020 495 VVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGA 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 554 SLLITSEDQLARFSDiPGLESLCYQQPLAAG--DDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRY 631
Cdd:COG1020 575 RLVLTQSALAARLPE-LGVPVLALDALALAAepATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 632 PLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLdadsVAA 711
Cdd:COG1020 654 GLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAA----PEA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 712 CRTLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPACGPELaavTGSSVPIGWPVWNTGLRILDAAM 790
Cdd:COG1020 730 LPSLRLVLVGGEALPPELVRRWrARLPGARLVNLYGPTETTVDSTYYEVTPPDA---DGGSVPIGRPIANTRVYVLDAHL 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 791 RPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELG 869
Cdd:COG1020 807 QPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELG 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 870 EIDRVMSGLPDVAQAVSHacvfnqAAATGGDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSAN 949
Cdd:COG1020 887 EIEAALLQHPGVREAVVV------AREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 950 GKLDRKALPLPTLGGERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQLSRQLARQVTPGQVM 1029
Cdd:COG1020 961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLF 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1030 VASTvgklsALLAADLSDEQARRLGLDTLLPLRESDGPTLFCFHPASGFAWQFSVLARYLSPRWSITGIQSPRPQGPMAS 1109
Cdd:COG1020 1041 LAAA-----AAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLL 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1110 AASLDEVCEHHLRTLLAQQPHGPYYLFGYSLGGTLAQGIAARLRQRGEAVAFLGLLDTWPPetqnwaekEANGLDPEVLA 1189
Cdd:COG1020 1116 ALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLL--------LALLLLALLLL 1187
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 1190 EIDREREAFLAAQQGQASGELFSAIEGNYADAVRLLTTAHSAKFDGKATLFVAEKTRQAGMDPQVVWGPWVAELEVFSQ 1268
Cdd:COG1020 1188 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALAL 1266
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
459-957 |
0e+00 |
|
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: 685.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 459 ALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTG 538
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 539 YPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 619 AIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLA 698
Cdd:cd17646 162 GIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 699 AFVASLDADsvaACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPElaavTGSSVPIGWPV 778
Cdd:cd17646 242 VFLAEPAAG---SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPA----ETPSVPIGRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 779 WNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQ 858
Cdd:cd17646 315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 859 LKIRGQRIELGEIDRVMSGLPdvaqAVSHACVFNQAAATGGdaRQLVGYLVSDSG-LPLDTAALKARLAEQLPPHMVPVV 937
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHP----AVTHAVVVARAAPAGA--ARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPAA 468
|
490 500
....*....|....*....|
gi 635952396 938 LMQLAELPLSANGKLDRKAL 957
Cdd:cd17646 469 FVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
469-957 |
0e+00 |
|
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: 597.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSedqlarfsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd05930 81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFvasLDADS 708
Cdd:cd05930 127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL---LQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 709 VAACRTLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPaCGPElaAVTGSSVPIGWPVWNTGLRILD 787
Cdd:cd05930 204 LAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATYYR-VPPD--DEEDGRVPIGRPIPNTRVYVLD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 788 AAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIE 867
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 868 LGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLS 947
Cdd:cd05930 361 LGEIEAALLAHPGVREAA----VVAREDGDGEK--RLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
490
....*....|
gi 635952396 948 ANGKLDRKAL 957
Cdd:cd05930 435 PNGKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-1170 |
7.07e-172 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 568.25 E-value: 7.07e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 83 SIIDLRTAPDPHRAATERMQADLAQDLRVdGGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRawqr 162
Cdd:PRK12467 2725 SRLDWRDRADLEQALDALAAADRQQGFDL-LSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF---- 2799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 163 GEATPESpftpfAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAplggraagsdiwrmkleMNADAFRRLAGH 242
Cdd:PRK12467 2800 GQPPPAR-----EGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARA-----------------LYPAPAEAVAGH 2857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 243 APQCQPADLALALTTLWLGR----LCNRMDYAAGFIFMRR---MGSAALTST---------------GPVLNVLPLAVHI 300
Cdd:PRK12467 2858 GAHYLHLDATQTRQLIEFARrhrvTLNTLVQGAWLLLLQRftgQDTVCFGATvagrpaqlrgaeqqlGLFINTLPVIASP 2937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 301 DAQETLADLAMRLAAQLKKMRRHQRYDAEQIVRDSGKaaGDEPLFGPVLnvkVFD-YQLDIDGVQAVTHTLATGPVNDLE 379
Cdd:PRK12467 2938 RAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQ--GGEALFDSIL---VFEnYPISEALKQGAPSGLRFGAVSSRE 3012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 380 -------LALFPDETggLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARLAAVNDTVVPL 452
Cdd:PRK12467 3013 qtnypltLAVGLGDT--LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAA 3090
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 453 PATTLSA--LVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGA 530
Cdd:PRK12467 3091 YPSERLVhqLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGG 3170
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 531 AWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQ--PLAAGDDAPLALSKPDHTAYIIFTSGSTG 608
Cdd:PRK12467 3171 AYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRldLNGYSENNPSTRVMGENLAYVIYTSGSTG 3250
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 609 RPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAePEAHRDPQAMQQFFARYGVT 688
Cdd:PRK12467 3251 KPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVR-DNDLWDPEELWQAIHAHRIS 3329
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 689 TTHFVPSMLAAFVAslDADsVAACRTLRRVFCSGEALPTELCREWER-LTGAPLHNLYGPTEAAVDVSWYpACGPElAAV 767
Cdd:PRK12467 3330 IACFPPAYLQQFAE--DAG-GADCASLDIYVFGGEAVPPAAFEQVKRkLKPRGLTNGYGPTEAVVTVTLW-KCGGD-AVC 3404
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 768 TGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLTN 846
Cdd:PRK12467 3405 EAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRAD 3484
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 847 GAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGgdaRQLVGYLVSDSGLPLDTAALKARLA 926
Cdd:PRK12467 3485 GVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAV----VLARDGAGG---KQLVAYVVPADPQGDWRETLRDHLA 3557
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 927 EQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPTLGGERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSL 1006
Cdd:PRK12467 3558 ASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSL 3637
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1007 LAMRLAAQLSRQLARQVTPGQVMVASTVGKLSALLaadlsdeQARRLGLDTLLPL--RESDGPTLFCFHPASGFAWQFSV 1084
Cdd:PRK12467 3638 LALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS-------PLGDVPVNLLLDLnrLETGFPALFCRHEGLGTVFDYEP 3710
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1085 LARYLSPRWSITGIQSPRPQGPMASAASLDEVCEHHLRTLLAQQPHGPYYLFGYSLGGTLAQGIAARLRQRGEAVAFLGL 1164
Cdd:PRK12467 3711 LAVILEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGL 3790
|
....*.
gi 635952396 1165 LDTWPP 1170
Cdd:PRK12467 3791 FDNTLP 3796
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-1235 |
1.77e-168 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 558.03 E-value: 1.77e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFgEPS 83
Cdd:PRK12316 49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPL-EVE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 IIDLRTAPDPHRAATERMQADLAQDLRVDGGN-PLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQR 162
Cdd:PRK12316 128 FEDCSGLPEAEQEARLRDEAQRESLQPFDLCEgPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 163 GeATPESPFTPFaevvdEYQRYAgseAWQR----------DKAFWQAQ---------------RQALPSPASLSAAPLGG 217
Cdd:PRK12316 208 G-AEPGLPALPI-----QYADYA---LWQRswleageqerQLEYWRAQlgeehpvlelptdhpRPAVPSYRGSRYEFSID 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 218 RAAGSDIWRMKLEMNADAFRRLAGhapqcqpadlalaLTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLA 297
Cdd:PRK12316 279 PALAEALRGTARRQGLTLFMLLLG-------------AFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 298 VHIDAQETLADLAMRLAAQLKKMRRHQRYDAEQIVR--DSGKAAGDEPLFGPVLNVKvfDYQLDIDGVQAVThTLATGPV 375
Cdd:PRK12316 346 SVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEalKVERSLSHSPLFQVMYNHQ--PLVADIEALDTVA-GLEFGQL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 376 N--------DLELALFpDETGGLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARLA-AVN 446
Cdd:PRK12316 423 EwksrttqfDLTLDTY-EKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVeGWN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 447 DT--VVPLPATTLSaLVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHG 524
Cdd:PRK12316 502 ATaaEYPLQRGVHR-LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLA 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 525 IVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLItSEDQLARFSDIP-GLESLCYQQPL----AAGDDAPLALSKPDHTAY 599
Cdd:PRK12316 581 ILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL-SQSHLGRKLPLAaGVQVLDLDRPAawleGYSEENPGTELNPENLAY 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 IIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQ 679
Cdd:PRK12316 660 VIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLV 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 680 QFFARYGVTTTHFVPSMLAAFvasLDADSVAACRTLRRVFCSGEALPTELCRE-WERLTGAPLHNLYGPTEAAVDVSwYP 758
Cdd:PRK12316 740 ELINREGVDTLHFVPSMLQAF---LQDEDVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVT-HW 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 759 ACGPElaavTGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTG 838
Cdd:PRK12316 816 TCVEE----GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTG 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 839 DVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHACvfnqaaatggDARQLVGYLVSDSGLPLDT 918
Cdd:PRK12316 892 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGKQLVGYVVLESEGGDWR 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 919 AALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPTLGGERSGR-PPEPGMETLVATAFSQLLGCEVNDIDAD 997
Cdd:PRK12316 962 EALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYvAPRNALERTLAAIWQDVLGVERVGLDDN 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 998 FFALGGHSLLAMRLAAQlSRQLARQVTPGQVMVASTVGKLS--ALLAADLSDEQARRLGLDTLLPLRESdgptLFCFHPA 1075
Cdd:PRK12316 1042 FFELGGDSIVSIQVVSR-ARQAGIQLSPRDLFQHQTIRSLAlvAKAGQATAADQGPASGEVALAPVQRW----FFEQAIP 1116
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1076 SGFAWQFSVLaryLSPRwsitgiqspRPQGPMASAASLDEVCEHHlrtllaqqphgpyylfgyslggtlaqgIAARLRQR 1155
Cdd:PRK12316 1117 QRQHWNQSLL---LQAR---------QPLDPDRLGRALERLVAHH---------------------------DALRLRFR 1157
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1156 GEAvaflglldtwppetQNWAEKEANGLDPEVLAEIDREREAFLAA--QQGQAS-----GELFSAIEGNYADAV-RLLTT 1227
Cdd:PRK12316 1158 EED--------------GGWQQAYAAPQAGEVLWQRQAASEEELLAlcEEAQRSldleqGPLLRALLVDMADGSqRLLLV 1223
|
....*...
gi 635952396 1228 AHSAKFDG 1235
Cdd:PRK12316 1224 IHHLVVDG 1231
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-1131 |
2.25e-167 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 554.77 E-value: 2.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 5 LPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWV--AADRTFGEP 82
Cdd:PRK12467 1117 LPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIhpVGSLTLEEP 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 83 sIIDLRTAPDPHRAAteRMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQR 162
Cdd:PRK12467 1197 -LLLAADKDEAQLKV--YVEAEARQPFDLEQG-PLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQ 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 163 GEaTPESPFTPFaevvdEYQRYAgseAWQRDK----------AFWQAQ---RQAL-------PSPASLSAaplggRAAgs 222
Cdd:PRK12467 1273 GQ-SLQLPALPI-----QYADYA---VWQRQWmdagerarqlAYWKAQlggEQPVlelptdrPRPAVQSH-----RGA-- 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 223 diwRMKLEMN---ADAFRRLAgHAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVH 299
Cdd:PRK12467 1337 ---RLAFELPpalAEGLRALA-RREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAE 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 300 IDAQETLADLAMR-----LAAQLkkmrrHQRYDAEQIVR--DSGKAAGDEPLFGpvlnvKVFDYQLDIDGVQAVTHTLAT 372
Cdd:PRK12467 1413 VDGQASFQQLLQQvkqaaLEAQA-----HQDLPFEQLVEalQPERSLSHSPLFQ-----VMFNHQRDDHQAQAQLPGLSV 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 373 GPVN--------DLELALFpDETGGLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANE-LARLA 443
Cdd:PRK12467 1483 ESLSwesqtaqfDLTLDTY-ESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAErRQILE 1561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 444 AVNDTVVPLP-ATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLAL 522
Cdd:PRK12467 1562 GWNATHTGYPlARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGL 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 523 HGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQP---LAAGDDAPLALS-KPDHTA 598
Cdd:PRK12467 1642 LAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEddwLEGYSDSNPAVNlAPQNLA 1721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 599 YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAM 678
Cdd:PRK12467 1722 YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQL 1801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 679 QQFFARYGVTTTHFVPSMLAAFVASldADSVAACRTLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWY 757
Cdd:PRK12467 1802 IQLIERQQVTTLHFVPSMLQQLLQM--DEQVEHPLSLRRVVCGGEALEVEALRPWlERLPDTGLFNLYGPTETAVDVTHW 1879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 758 PACGPELAAvtGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYR 836
Cdd:PRK12467 1880 TCRRKDLEG--RDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGtVGSRLYR 1957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 837 TGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHACvfnqaaaTGGDARQLVGYLV-SDSGLP 915
Cdd:PRK12467 1958 TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-------DGANGKQLVAYVVpTDPGLV 2030
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 916 LDT-------AALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPTLGGERSG-RPPEPGMETLVATAFSQLL 987
Cdd:PRK12467 2031 DDDeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAyVAPQSELEQRLAAIWQDVL 2110
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 988 GCEVNDIDADFFALGGHSLLAMRLAAQlSRQLARQVTPGQVMVASTVGKLSALLA---ADLSDEQARRLGLDTLLPLRES 1064
Cdd:PRK12467 2111 GLEQVGLHDNFFELGGDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQegdGTVSIDQGPVTGDLPLLPIQQM 2189
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 1065 dgptLFCFHPASGFAWQFSVLaryLSPRWSItgiqsprpQGPMASAAsLDEVCEHH--LRTLLAQQPHG 1131
Cdd:PRK12467 2190 ----FFADDIPERHHWNQSVL---LEPREAL--------DAELLEAA-LQALLVHHdaLRLGFVQEDGG 2242
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-1018 |
4.04e-165 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 548.23 E-value: 4.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 5 LPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFgEPSI 84
Cdd:PRK05691 676 LPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEF-ALQR 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 85 IDLRTAPDPHRAATERM----QADLAQDLRVdggNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAW 160
Cdd:PRK05691 755 IDLSDLPEAEREARAAQireeEARQPFDLEK---GPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAA 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 161 QRGEATPESPFTPFAEVVDEYQR--YAGSEAwQRDKAFWQAQ-RQALPSPASLSAAPLGGRAAGSDIwRMKLEMNA---D 234
Cdd:PRK05691 832 CQGQTAELAPLPLGYADYGAWQRqwLAQGEA-ARQLAYWKAQlGDEQPVLELATDHPRSARQAHSAA-RYSLRVDAslsE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 235 AFRRLAgHAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLA 314
Cdd:PRK05691 910 ALRGLA-QAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVR 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 315 AQLKKMRRHQRYDAEQIVRDSGKAaGDEPLFGPVLNVKvfdyQLDIDGVQAVTHTLATG-PVN------DLELALFPDET 387
Cdd:PRK05691 989 QATLGAQAHQDLPFEQLVEALPQA-REQGLFQVMFNHQ----QRDLSALRRLPGLLAEElPWHsreakfDLQLHSEEDRN 1063
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 388 GGLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARLAAVNDTVVPLPATTLSALVADQARK 467
Cdd:PRK05691 1064 GRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQ 1143
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 468 TPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMM 547
Cdd:PRK05691 1144 TPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM 1223
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 548 LEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAG--DDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 625
Cdd:PRK05691 1224 LADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSwpSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ 1303
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 626 WMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVaslD 705
Cdd:PRK05691 1304 WMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI---D 1380
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 706 ADSVAACRTLRRVFCSGEALPTELC-REWERLTGAPLHNLYGPTEAAVDVSWYpacgpELAAVTGSSVPIGWPVWNTGLR 784
Cdd:PRK05691 1381 EPLAAACTSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTETAINVTHW-----QCQAEDGERSPIGRPLGNVLCR 1455
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 785 ILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:PRK05691 1456 VLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRG 1535
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 864 QRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAE 943
Cdd:PRK05691 1536 FRVEPEEIQARLLAQPGVAQAA----VLVREGAAGA---QLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQ 1608
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 944 LPLSANGKLDRKALPLPTLgGERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQlSRQ 1018
Cdd:PRK05691 1609 MPLGPSGKLDRRALPEPVW-QQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSR-TRQ 1681
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1044 |
4.81e-160 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 533.20 E-value: 4.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 3 TRLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFGEP 82
Cdd:PRK12467 48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 83 siIDLRTAPDPHRAAT---ERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRA 159
Cdd:PRK12467 128 --LDDLANEQGRARESqieAYINEEVARPFDLANG-PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 160 WQRGEaTPESPFTPFaevvdEYQRYAgseAWQR----------DKAFWQAQRQ------ALPSPASLSAAPlGGRAAGSD 223
Cdd:PRK12467 205 YSQGR-EPSLPALPI-----QYADYA---IWQRswleagererQLAYWQEQLGgehtvlELPTDRPRPAVP-SYRGARLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 224 IwRMKLEMnADAFRRLAgHAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQ 303
Cdd:PRK12467 275 V-DLPQAL-SAGLKALA-QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 304 ETLADLAMRLAAQLKKMRRHQRYDAEQIVR--DSGKAAGDEPLFGPVLN-------VKVFDYQ----LDIDGVQAVTHTl 370
Cdd:PRK12467 352 ASFLELLQQVKRTALGAQAHQDLPFEQLVEalQPERSLSHSPLFQVMFNhqntatgGRDREGAqlpgLTVEELSWARHT- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 371 atgpvNDLELAL-FPDETGGLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELAR-LAAVNDT 448
Cdd:PRK12467 431 -----AQFDLALdTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERAReLVRWNAP 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 449 VVPLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEA 528
Cdd:PRK12467 506 ATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 529 GAAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLA-----AGDDAPLALSkPDHTAYIIFT 603
Cdd:PRK12467 586 GGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPADllcgySGHNPEVALD-PDNLAYVIYT 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 604 SGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFA 683
Cdd:PRK12467 665 SGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMA 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 684 RYGVTTTHFVPSMLAAFvasLDADSVAACRTLRRVFCSGEALPTELCREWERLT-GAPLHNLYGPTEAAVDVSWYPaCGp 762
Cdd:PRK12467 745 DQGVTVLKIVPSHLQAL---LQASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYE-LS- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 763 eLAAVTGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVA 841
Cdd:PRK12467 820 -DEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLA 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 842 RWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVShacvfnqAAATGGDARQLVGYLVSDsgLPLDTA-- 919
Cdd:PRK12467 899 RYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV-------LAQPGDAGLQLVAYLVPA--AVADGAeh 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 920 -----ALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPTLGGERSG-RPPEPGMETLVATAFSQLLGCEVND 993
Cdd:PRK12467 970 qatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATfVAPQTELEKRLAAIWADVLKVERVG 1049
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 635952396 994 IDADFFALGGHSLLAMRLAAQLSRQLARQVTPGQVMVASTVGKLSALLAAD 1044
Cdd:PRK12467 1050 LTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ 1100
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-1123 |
4.17e-155 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 518.74 E-value: 4.17e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 5 LPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQwVAADRTFGEPSI 84
Cdd:PRK12316 2603 LPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQ-VILPNMSLRIVL 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 85 IDLRTAPDPhrAATERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGE 164
Cdd:PRK12316 2682 EDCAGVADA--AIRQRVAEEIQRPFDLARG-PLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGE 2758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 165 ATPESPFTPFAEVVDEYQR-YAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRLAGHA 243
Cdd:PRK12316 2759 QPTLPPLPLQYADYAAWQRaWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALA 2838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 244 --PQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKKMR 321
Cdd:PRK12316 2839 rrEGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQ 2918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 322 RHQRYDAEQIVR--DSGKAAGDEPLFGPVLNvkvFDYQLDIDGVQAVTHTLATGPVNDLELALFPDETG----GLSLEIL 395
Cdd:PRK12316 2919 AHQDLPFEQLVEalQPERSLSHSPLFQVMYN---HQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWesaeGLGASLT 2995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 396 ANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELAR-LAAVNDTVVPLP-ATTLSALVADQARKTPDAPA 473
Cdd:PRK12316 2996 YATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQlLEAWNATAAEYPlERGVHRLFEEQVERTPDAVA 3075
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 474 LADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARP 553
Cdd:PRK12316 3076 LAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGA 3155
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 554 SLLITSEDqlARFSDIPGLESLCYQ-QPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYP 632
Cdd:PRK12316 3156 QLLLSQSH--LRLPLAQGVQVLDLDrGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG 3233
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 633 LSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvaaC 712
Cdd:PRK12316 3234 LGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHR---C 3310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 713 RTLRRVFCSGEALPTELCREWerLTGAPLHNLYGPTEAAVDVSWYpacgpELAAVTGSSVPIGWPVWNTGLRILDAAMRP 792
Cdd:PRK12316 3311 TSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHW-----QCVEEGKDAVPIGRPIANRACYILDGSLEP 3383
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 793 VPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEID 872
Cdd:PRK12316 3384 VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE 3463
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 873 RVMSGLPDVAQAVSHACvfnqaaatggDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:PRK12316 3464 ARLLEHPWVREAVVLAV----------DGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 953 DRKALPLPTLGGERSGR-PPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQlSRQLARQVTPGQVMVA 1031
Cdd:PRK12316 3534 DRKALPRPDAALLQQDYvAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSR-ARQAGIRFTPKDLFQH 3612
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1032 STVGKLS--ALLAADLSDEQARRLGLDTLLPLRESdgptLFCFHPASGFAWQFSVLaryLSPRwsitgiqspRPQGPMAS 1109
Cdd:PRK12316 3613 QTIQGLArvARVGGGVAVDQGPVSGETLLLPIQQQ----FFEEPVPERHHWNQSLL---LKPR---------EALDAAAL 3676
|
1130
....*....|....*.
gi 635952396 1110 AASLDEVCEHH--LRT 1123
Cdd:PRK12316 3677 EAALQALVEHHdaLRL 3692
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-1059 |
9.32e-152 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 508.73 E-value: 9.32e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 6 PLVAAQPGIWMAERLSTLPGAWSVAHYVELRGaLDPTLLGKAIVAGLQQADTLSLRF-EEEEGEVWQWVAADRTFGEPSI 84
Cdd:PRK12316 4104 PLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRPLQVVHKQVSLPFAE 4182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 85 IDLRTAPDPHRAATERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAwqrge 164
Cdd:PRK12316 4183 LDWRGRADLQAALDALAAAERERGFDLQRA-PLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSG----- 4256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 165 ATPESPFTPFAEVVDEYQRYAGSEAwqrdKAFWQAQRQALPSPASLSAA-PLGGRAAGSDIWRMKLEMNADAFRRLAGHA 243
Cdd:PRK12316 4257 RPPAQPGGRYRDYIAWLQRQDAAAS----EAFWREQLAALDEPTRLAQAiARADLRSANGYGEHVRELDATATARLREFA 4332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 244 PQCQPA--DLALALTTLWLGRLCNRMDYAAGFIFMRRmgSAALTST----GPVLNVLPLAVHIDAQETLADLAMRLAAQL 317
Cdd:PRK12316 4333 RTQRVTlnTLVQAAWLLLLQRYTGQDTVAFGATVAGR--PAELPGIegqiGLFINTLPVIATPRAQQSVVEWLQQVQRQN 4410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 318 KKMRRHQRYDAEQIVRDSGKaaGDEPLFGPVLNVKVFDY-----QLDIDGVQAVTHTLATGPVNDLELALFPDETggLSL 392
Cdd:PRK12316 4411 LALREHEHTPLYEIQRWAGQ--GGEALFDSLLVFENYPVsealqQGAPGGLRFGEVTNHEQTNYPLTLAVGLGET--LSL 4486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 393 EILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARLAAV-NDTVVPLPAT-TLSALVADQARKTPD 470
Cdd:PRK12316 4487 QFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALwNRTDAGYPATrCVHQLVAERARMTPD 4566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 471 APALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLED 550
Cdd:PRK12316 4567 AVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMED 4646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 551 ARPSLLITSEDQLARFSDIPGLESLCYQQP---LAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 627
Cdd:PRK12316 4647 SGAALLLTQSHLLQRLPIPDGLASLALDRDedwEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT 4726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 628 QDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHrDPQAMQQFFARYGVTTTHFVPSMLAAFVAslDAD 707
Cdd:PRK12316 4727 GERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAE--HAE 4803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 708 SVAACRTLRRVFCSGEALPTELCRE-WERLTGAPLHNLYGPTEAAVDVS-W----YPACGPElaavtgsSVPIGWPVWNT 781
Cdd:PRK12316 4804 RDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLlWkardGDACGAA-------YMPIGTPLGNR 4876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 782 GLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLK 860
Cdd:PRK12316 4877 SGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVK 4956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 861 IRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGgdaRQLVGYLVSDSGLPLDTAA--------LKARLAEQLPPH 932
Cdd:PRK12316 4957 IRGFRIELGEIEARLREHPAVREAV----VIAQEGAVG---KQLVGYVVPQDPALADADEaqaelrdeLKAALRERLPEY 5029
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 933 MVPVVLMQLAELPLSANGKLDRKALPLPTLG-GERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRL 1011
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASlLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 635952396 1012 AAQLSRQLARQVTPGQVMVASTVGKLSALLAADLSDEQARRLGLDTLL 1059
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELL 5157
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
469-957 |
1.61e-150 |
|
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: 462.53 E-value: 1.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSEDQLARFSDIPGLESLCYQQPlAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA-AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVAS--LDA 706
Cdd:cd12116 160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 707 DSVaacrtlrRVFCSGEALPTELCREWERLTGApLHNLYGPTEAAVdvsWYPACGPELAAvtgSSVPIGWPVWNTGLRIL 786
Cdd:cd12116 240 AGL-------TALCGGEALPPDLAARLLSRVGS-LWNLYGPTETTI---WSTAARVTAAA---GPIPIGRPLANTQVYVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 787 DAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQR 865
Cdd:cd12116 306 DAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 866 IELGEIDRVMSGLPDVAQAVshACVFnqaaaTGGDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELP 945
Cdd:cd12116 386 IELGEIEAALAAHPGVAQAA--VVVR-----EDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALP 458
|
490
....*....|..
gi 635952396 946 LSANGKLDRKAL 957
Cdd:cd12116 459 LTANGKLDRKAL 470
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
459-957 |
1.14e-149 |
|
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: 460.51 E-value: 1.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 459 ALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTG 538
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 539 YPDDRLRMMLEDARPSLLITSEdQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDR-SLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 619 AIVnRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTThFVPSMLA 698
Cdd:cd12117 160 GVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 699 AFVASLDADSVAacrTLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPAcgPELAAVTGSsVPIGWP 777
Cdd:cd12117 238 NQLADEDPECFA---GLRELLTGGEVVSPPHVRRVlAACPGLRLVNGYGPTENTTFTTSHVV--TELDEVAGS-IPIGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 778 VWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDD 857
Cdd:cd12117 312 IANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 858 QLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdaRQLVGYLVSDsgLPLDTAALKARLAEQLPPHMVPVV 937
Cdd:cd12117 392 QVKIRGFRIELGEIEAALRAHPGVREAV----VVVREDAGGD--KRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAA 463
|
490 500
....*....|....*....|
gi 635952396 938 LMQLAELPLSANGKLDRKAL 957
Cdd:cd12117 464 FVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
482-885 |
3.53e-148 |
|
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: 453.65 E-value: 3.53e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 DQLARFSDIPGLESLCYQQPLAAGDDAPL-----ALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSA 635
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAppppdAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 636 QDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFF-ARYGVTTTHFVPSMLAAfvasLDADSVAACRT 714
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLAL----LAAALPPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 715 LRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPACGPELAavTGSSVPIGWPVWNTGLRILDAAMRPV 793
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWrARGPGARLINLYGPTETTVWSTATLVDPDDAP--RESPVPIGRPLANTRLYVLDDDLRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 794 PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP--GERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEI 871
Cdd:TIGR01733 315 PVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEI 394
|
410
....*....|....
gi 635952396 872 DRVMSGLPDVAQAV 885
Cdd:TIGR01733 395 EAALLRHPGVREAV 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-1055 |
3.88e-147 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 495.25 E-value: 3.88e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 86 DLRTAPDPHRAATErmqadLAQDLRVDGGN----PLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAwq 161
Cdd:PRK12316 1638 DWRGREDLGQALDA-----LAQAERQKGFDltraPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-- 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 162 rgeatpespfTPFAEVVDEYQRYAgseAW--QRDK----AFWQAQRQALPSPASL--SAAPLGGRAAGSDIWRmklEMNA 233
Cdd:PRK12316 1711 ----------QPVAAPGGRYRDYI---AWlqRQDAaaseAFWKEQLAALEEPTRLaqAARTEDGQVGYGDHQQ---LLDP 1774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 234 DAFRRLAGHAPQCQPA--DLALALTTLWLGRLCNRMDYAAGFIFMRRmgSAALT----STGPVLNVLPLAVHIDAQETLA 307
Cdd:PRK12316 1775 AQTRALAEFARAQKVTlnTLVQAAWLLLLQRYTGQETVAFGATVAGR--PAELPgieqQIGLFINTLPVIAAPRPDQSVA 1852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 308 DLAMRLAAQLKKMRRHQRYDAEQIVRDSGKaaGDEPLFGPVLnvkVFD-YQLDIDGVQAVTHTLATGPVNDLELALFPDE 386
Cdd:PRK12316 1853 DWLQEVQALNLALREHEHTPLYDIQRWAGQ--GGEALFDSLL---VFEnYPVAEALKQGAPAGLVFGRVSNHEQTNYPLT 1927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 387 TG-----GLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELAR-LAAVNDTVVPLPATTL-SA 459
Cdd:PRK12316 1928 LAvtlgeTLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRiLADWDRTPEAYPRGPGvHQ 2007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 460 LVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGD---DAPLALSKPDHTAYIIFTSGSTGRPKGVMVG 616
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAEWADypdTAPAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 617 QTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMaEPEAHRDPQAMQQFFARYGVTTTHFVPSM 696
Cdd:PRK12316 2168 HGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI-RDDELWDPEQLYDEMERHGVTILDFPPVY 2246
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 697 LAAFVASLDADsvaACR-TLRRVFCSGEALPTELCRE-WERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTGssVPI 774
Cdd:PRK12316 2247 LQQLAEHAERD---GRPpAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAY--VPI 2321
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 775 GWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLG 853
Cdd:PRK12316 2322 GRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLG 2401
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 854 RSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGgdaRQLVGYLVSDSGLPLDTAALKARLAEQLPPHM 933
Cdd:PRK12316 2402 RIDHQVKIRGFRIELGEIEARLQAHPAVREAV----VVAQDGASG---KQLVAYVVPDDAAEDLLAELRAWLAARLPAYM 2474
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 934 VPVVLMQLAELPLSANGKLDRKALPLPTLGG-ERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLA 1012
Cdd:PRK12316 2475 VPAHWVVLERLPLNPNGKLDRKALPKPDVSQlRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVV 2554
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 635952396 1013 AQLSRQLARQVTPGQVMVASTvgkLSALLAADLSDEQARRLGL 1055
Cdd:PRK12316 2555 SRVRQDLGLEVPLRILFERPT---LAAFAASLESGQTSRAPVL 2594
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
460-960 |
1.60e-146 |
|
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: 452.55 E-value: 1.60e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 460 LVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITSEDQLARFSDIpGLESLCYQQPLAAGDDAPLA-LSKPDHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFI-GLIDLLDEDTIYHEESENLEpVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 619 AIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLA 698
Cdd:cd17655 161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 699 AFVASLDADSVaacrTLRRVFCSGEALPTELCREWERL--TGAPLHNLYGPTEAAVDVSWYPAcgpELAAVTGSSVPIGW 776
Cdd:cd17655 241 LLDAADDSEGL----SLKHLIVGGEALSTELAKKIIELfgTNPTITNAYGPTETTVDASIYQY---EPETDQQVSVPIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 777 PVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSD 856
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 857 DQLKIRGQRIELGEIDRVMSGLPDVAQAVshacvfnqAAATGGDARQ--LVGYLVSDSglPLDTAALKARLAEQLPPHMV 934
Cdd:cd17655 394 HQVKIRGYRIELGEIEARLLQHPDIKEAV--------VIARKDEQGQnyLCAYIVSEK--ELPVAQLREFLARELPDYMI 463
|
490 500
....*....|....*....|....*.
gi 635952396 935 PVVLMQLAELPLSANGKLDRKALPLP 960
Cdd:cd17655 464 PSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
461-958 |
2.58e-146 |
|
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: 452.18 E-value: 2.58e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 461 VADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYP 540
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 541 DDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALSK-PDHTAYIIFTSGSTGRPKGVMVGQTA 619
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALdADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 620 IVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTThFVPsmlAA 699
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRV-FLP---TV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 700 FVASLDADSVAACRT---LRRVFCSGEALP-TELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPacgPELAAVTGSSVPI 774
Cdd:cd17651 237 ALRALAEHGRPLGVRlaaLRYLLTGGEQLVlTEDLREFcAGLPGLRLHNHYGPTETHVVTALSL---PGDPAAWPAPPPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 775 GWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGR 854
Cdd:cd17651 314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 855 SDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdaRQLVGYLVSDSGLPLDTAALKARLAEQLPPHMV 934
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAV----VLAREDRPGE--KRLVAYVVGDPEAPVDAAELRAALATHLPEYMV 467
|
490 500
....*....|....*....|....
gi 635952396 935 PVVLMQLAELPLSANGKLDRKALP 958
Cdd:cd17651 468 PSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
469-957 |
7.37e-144 |
|
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: 444.06 E-value: 7.37e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITsedqlarfsdipgleslcyqqplaagddaplalsKPDHTAYIIFTSGSTGRPKGVMVGQtAIVNRLLWMQ 628
Cdd:cd17643 81 ADSGPSLLLT----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSH-ANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DR-YPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDAD 707
Cdd:cd17643 126 QRwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 708 SVAACRtLRRVFCSGEALPTELCREW---ERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTGSsvPIGWPVWNTGLR 784
Cdd:cd17643 206 GRDPLA-LRYVIFGGEALEAAMLRPWagrFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAAS--PIGRPLPGLRVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 785 ILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:cd17643 283 VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 864 QRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAE 943
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAA----VIVREDEPGDT--RLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDA 436
|
490
....*....|....
gi 635952396 944 LPLSANGKLDRKAL 957
Cdd:cd17643 437 LPLTVNGKLDRAAL 450
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
4-424 |
3.62e-143 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 441.04 E-value: 3.62e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFgEPS 83
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPV-PIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 IIDLRTAPDPHRAATERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRG 163
Cdd:cd19533 80 HIDLSGDPDPEGAAQQWMQEDLRKPLPLDND-PLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 164 EATPESPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSdiwRMKLEMNADAFRRL--AG 241
Cdd:cd19533 159 RPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFL---RRTAELPPELTRTLleAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 242 HAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKKMR 321
Cdd:cd19533 236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 322 RHQRYDAEQIVRDSGKAAGDEPLFGPVLNVKVFDYQLDIDGVQAVTHTLATGPVNDLELALFP-DETGGLSLEILANKAR 400
Cdd:cd19533 316 RHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYDrDDESGLRIDFDANPAL 395
|
410 420
....*....|....*....|....
gi 635952396 401 YDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19533 396 YSGEDLARHQERLLRLLEEAAADP 419
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
469-958 |
2.87e-135 |
|
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: 420.89 E-value: 2.87e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSedqlarfsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd17652 81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAfvasLDADS 708
Cdd:cd17652 127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA----LPPDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 709 VAACRTLrrvFCSGEALPTELCREWERltGAPLHNLYGPTEAAVDVSWYPaCGPelaavTGSSVPIGWPVWNTGLRILDA 788
Cdd:cd17652 203 LPDLRTL---VVAGEACPAELVDRWAP--GRRMINAYGPTETTVCATMAG-PLP-----GGGVPPIGRPVPGTRVYVLDA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 789 AMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIE 867
Cdd:cd17652 272 RLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 868 LGEIDRVMSGLPDVAQAVshacVFNQAAATGGdaRQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLS 947
Cdd:cd17652 352 LGEVEAALTEHPGVAEAV----VVVRDDRPGD--KRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLT 425
|
490
....*....|.
gi 635952396 948 ANGKLDRKALP 958
Cdd:cd17652 426 PNGKLDRRALP 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
460-957 |
3.71e-127 |
|
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: 399.77 E-value: 3.71e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 460 LVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITsedqlarfsdipgleslcyqqplaagddaplalsKPDHTAYIIFTSGSTGRPKGVMVGQTA 619
Cdd:cd12115 84 PPERLRFILEDAQARLVLT----------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 620 IVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEpeahrDPQAMQQFFARYGVTTTHFVPSMLAA 699
Cdd:cd12115 130 AAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAAAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 700 FvasLDADSVAAcrTLRRVFCSGEALPTELCRE-WERLTGAPLHNLYGPTEAAVdvswYpACGPELAAVTGSSVPIGWPV 778
Cdd:cd12115 205 L---LRHDALPA--SVRVVNLAGEPLPRDLVQRlYARLQVERVVNLYGPSEDTT----Y-STVAPVPPGASGEVSIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 779 WNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQ 858
Cdd:cd12115 275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 859 LKIRGQRIELGEIDRVMSGLPDVAQAVshacvfnqAAATGGDA--RQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPV 936
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAV--------VVAIGDAAgeRRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPS 426
|
490 500
....*....|....*....|.
gi 635952396 937 VLMQLAELPLSANGKLDRKAL 957
Cdd:cd12115 427 RFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
469-958 |
3.51e-125 |
|
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: 394.43 E-value: 3.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSEdqlarfsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd17649 81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADS 708
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 709 VAACRTLRRVFCSGEALPTELCREWeRLTGAPLHNLYGPTEAAVDVSWYPAcgPELAAVTGSSVPIGWPVWNTGLRILDA 788
Cdd:cd17649 208 DGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVTPLVWKC--EAGAARAGASMPIGRPLGGRSAYILDA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 789 AMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIE 867
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 868 LGEIDRVMSGLPdvaqAVSHACVFNQAAATGGdarQLVGYLVS--DSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELP 945
Cdd:cd17649 365 LGEIEAALLEHP----GVREAAVVALDGAGGK---QLVAYVVLraAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLP 437
|
490
....*....|...
gi 635952396 946 LSANGKLDRKALP 958
Cdd:cd17649 438 LTPNGKLDRKALP 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
456-958 |
9.49e-122 |
|
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: 386.02 E-value: 9.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL 535
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLITsedqlarfsdipgleslcyqqplaagddaplalsKPDHTAYIIFTSGSTGRPKGVMV 615
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT----------------------------------QPENLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 616 GQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPS 695
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 696 MLAAFVASLDADSVAACRTLRRVFCSGEALPTELCREWERLTG--APLHNLYGPTEAAVDVSWYPACGPELAAVTgsSVP 773
Cdd:cd17644 207 YWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNIT--SVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 774 IGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA--PGERMYRTGDVARWLTNGAVEY 851
Cdd:cd17644 285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 852 LGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQavshACVFNQAAATGGdaRQLVGYLVSDSGLPLDTAALKARLAEQLPP 931
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT----AVVIVREDQPGN--KRLVAYIVPHYEESPSTVELRQFLKAKLPD 438
|
490 500
....*....|....*....|....*..
gi 635952396 932 HMVPVVLMQLAELPLSANGKLDRKALP 958
Cdd:cd17644 439 YMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
469-957 |
6.32e-119 |
|
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: 378.54 E-value: 6.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSEDQlARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd12114 81 ADAGARLVLTDGPD-AQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPS---MLAAFVASLD 705
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 706 ADSvaacRTLRRVFCSGEALPTELCREWERLT-GAPLHNLYGPTEAAVDVSWYPAcGPELAAVtgSSVPIGWPVWNTGLR 784
Cdd:cd12114 240 ALL----PSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSIYHPI-DEVPPDW--RSIPYGRPLANQRYR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 785 ILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPfaPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQ 864
Cdd:cd12114 313 VLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 865 RIELGEIDRVMSGLPDVAQAVShacvfnqAAATGGDARQLVGYLVSDSGL-PLDTAALKARLAEQLPPHMVPVVLMQLAE 943
Cdd:cd12114 391 RIELGEIEAALQAHPGVARAVV-------VVLGDPGGKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 635952396 944 LPLSANGKLDRKAL 957
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-1062 |
2.22e-113 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 394.15 E-value: 2.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRtfgeps 83
Cdd:PRK05691 1728 PVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS------ 1801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 iiDLRT-----APDPHRAATERMQAdLA-----QDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQI 153
Cdd:PRK05691 1802 --GLRMdwqdfSALPADARQQRLQQ-LAdseahQPFDLERG-PLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFAREL 1877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 154 AAIYRAWQRGEatpESPFTPFAEVVDEY----QRYAGSEAWQRDKAFWQAQ----RQALPSPASLSAAPLggRAAGSDIW 225
Cdd:PRK05691 1878 GALYEAFLDDR---ESPLEPLPVQYLDYsvwqRQWLESGERQRQLDYWKAQlgneHPLLELPADRPRPPV--QSHRGELY 1952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 226 RmkLEMNADAFRRLagHAPQCQPADLALALTTLWLGRLCNRM----DYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHID 301
Cdd:PRK05691 1953 R--FDLSPELAARV--RAFNAQRGLTLFMTMTATLAALLYRYsgqrDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLD 2028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 302 AQETLADLAMRLAAQLKKMRRHQRYDAEQIVR--DSGKAAGDEPLFGPVLNVKVFDYQLdidgvqavTHTLAtgpvndle 379
Cdd:PRK05691 2029 GQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEalQPPRSAAYNPLFQVMCNVQRWEFQQ--------SRQLA-------- 2092
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 380 lalfpdetgGLSLEILANKAR---------------------------YDEAELRRHVARLTALLAQFAADPALRCGEAE 432
Cdd:PRK05691 2093 ---------GMTVEYLVNDARatkfdlnlevtdldgrlgccltysrdlFDEPRIARMAEHWQNLLEALLGDPQQRLAELP 2163
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 433 MLSANELARLAAV--NDTVVPLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAV 510
Cdd:PRK05691 2164 LLAAAEQQQLLDSlaGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGL 2243
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 511 ALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIP-GLESLCYQQ---PLAAGDD 586
Cdd:PRK05691 2244 ALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPaGVARWCLEDdaaALAAYSD 2323
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 587 APLA-LSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLV 665
Cdd:PRK05691 2324 APLPfLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVV 2403
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 666 MaEPEAHRDPQAMQQFFARYGVTTTHFVP---SMLAAFVASLDADSvaacrTLRRVFCSGEALPTElcrEWERLTGA--- 739
Cdd:PRK05691 2404 L-RAQGQWGAEEICQLIREQQVSILGFTPsygSQLAQWLAGQGEQL-----PVRMCITGGEALTGE---HLQRIRQAfap 2474
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 740 -PLHNLYGPTEAAVdvswYP-AC-GPELAAVTGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRP 816
Cdd:PRK05691 2475 qLFFNAYGPTETVV----MPlAClAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRP 2550
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 817 DLTASRFIADPFAP-GERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHAcvfnqAA 895
Cdd:PRK05691 2551 GLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA-----LD 2625
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 896 ATGGdaRQLVGYLVSDSGLPLDTA------ALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPTLGGERSG- 968
Cdd:PRK05691 2626 TPSG--KQLAGYLVSAVAGQDDEAqaalreALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAy 2703
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 969 RPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQlSRQLARQVTPGQVMVASTVGKLSALLAAD--LS 1046
Cdd:PRK05691 2704 QAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVATHSeaAQ 2782
|
1130
....*....|....*.
gi 635952396 1047 DEQARRLGLDTLLPLR 1062
Cdd:PRK05691 2783 AEQGPLQGASGLTPIQ 2798
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
465-957 |
5.45e-112 |
|
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: 358.87 E-value: 5.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRL 544
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 545 RMMLEDARPSLLItsedqlarfsdipgleslcyqqplAAGDDaplalskpdhTAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:cd05945 81 REILDAAKPALLI------------------------ADGDD----------NAYIIFTSGSTGRPKGVQISHDNLVSFT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 625 LWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSmLAAFVASL 704
Cdd:cd05945 127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS-FAAMCLLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 705 DADSVAACRTLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTgsSVPIGWPVWNTGL 783
Cdd:cd05945 206 PTFTPESLPSLRHFLFCGEVLPHKTARALqQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYD--RLPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 784 RILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 864 QRIELGEIDRVMSGLPDVAQAVShacvfnQAAATGGDARQLVGYLVSDSGLP-LDTAALKARLAEQLPPHMVPVVLMQLA 942
Cdd:cd05945 361 YRIELEEIEAALRQVPGVKEAVV------VPKYKGEKVTELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLD 434
|
490
....*....|....*
gi 635952396 943 ELPLSANGKLDRKAL 957
Cdd:cd05945 435 ELPLNANGKIDRKAL 449
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
5-424 |
1.39e-111 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 357.10 E-value: 1.39e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 5 LPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFGEPSI 84
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 85 IDLRTAPDPHRAATERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGE 164
Cdd:cd19066 82 IDLRNLADPEARLLELIDQIQQTIYDLERG-PLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 165 ATPESPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRL--AGH 242
Cdd:cd19066 161 PTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLreVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 243 APQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKKMRR 322
Cdd:cd19066 241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 323 HQRYDAEQIVRDSGKA--AGDEPLFGPVLNVKVFDYQLDIDGVQA---VTHTLATGPVNDLELALFPDETGGLSLEILAN 397
Cdd:cd19066 321 HQRVPFIELVRHLGVVpeAPKHPLFEPVFTFKNNQQQLGKTGGFIfttPVYTSSEGTVFDLDLEASEDPDGDLLLRLEYS 400
|
410 420
....*....|....*....|....*..
gi 635952396 398 KARYDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19066 401 RGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
461-862 |
1.24e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 354.31 E-value: 1.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 461 VADQARKTPDAPALADARWQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITSEDQLA-------------------RFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYI 600
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLeellealgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 601 IFTSGSTGRPKGVMVGQTAIVNRLLWM----QDRYPLSAQDVVAQKTPCSFDVSV-WEFWWPFIAGAQLVMAEPEAHRDP 675
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 676 QAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVS 755
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALL-SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WYPAcGPELAAVTGSsvpIGWPVWNTGLRILDAA-MRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgeRM 834
Cdd:pfam00501 320 TPLP-LDEDLRSLGS---VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GW 389
|
410 420
....*....|....*....|....*...
gi 635952396 835 YRTGDVARWLTNGAVEYLGRSDDQLKIR 862
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
469-957 |
1.22e-109 |
|
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: 352.54 E-value: 1.22e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDArpsllitsedqlarfsdipgleslcyqqplaagdDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd17650 81 EDS----------------------------------GAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVA-QKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDAD 707
Cdd:cd17650 127 REYELDSFPVRLlQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 708 SVAAcRTLRRVFCSGEALPTELCREWERLTGAPLH--NLYGPTEAAVDVSWYpacgpELAAV---TGSSVPIGWPVWNTG 782
Cdd:cd17650 207 GLDL-SAMRLLIVGSDGCKAQDFKTLAARFGQGMRiiNSYGVTEATIDSTYY-----EEGRDplgDSANVPIGRPLPNTA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 783 LRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIR 862
Cdd:cd17650 281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 863 GQRIELGEIDRVMSGLPDVAQAVshacvfnqaAATGGDARQ---LVGYLVSDSglPLDTAALKARLAEQLPPHMVPVVLM 939
Cdd:cd17650 361 GFRIELGEIESQLARHPAIDEAV---------VAVREDKGGearLCAYVVAAA--TLNTAELRAFLAKELPSYMIPSYYV 429
|
490
....*....|....*...
gi 635952396 940 QLAELPLSANGKLDRKAL 957
Cdd:cd17650 430 QLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
463-957 |
1.89e-108 |
|
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: 348.92 E-value: 1.89e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 463 DQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDD 542
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 543 RLRMMLEDARPSLLITsedqlarfsdipgleslcyqqplaagddaplaLSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVN 622
Cdd:cd17653 85 RIQAILRTSGATLLLT--------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 623 RLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEahrDPQAMqqfFARyGVTTTHFVPSMLaafvA 702
Cdd:cd17653 133 YVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPS---DPFAH---VAR-TVDALMSTPSIL----S 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 703 SLDADSVAacrTLRRVFCSGEALPTELCREWerLTGAPLHNLYGPTEAAVDVSwYPACGPelaavtGSSVPIGWPVWNTG 782
Cdd:cd17653 202 TLSPQDFP---NLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISST-MTELLP------GQPVTIGKPIPNST 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 783 LRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIR 862
Cdd:cd17653 270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 863 GQRIELGEIDRVMSGLPDVAQAVShACVFNQaaatggdarQLVGYLVSDSglpLDTAALKARLAEQLPPHMVPVVLMQLA 942
Cdd:cd17653 350 GFRINLEEIEEVVLQSQPEVTQAA-AIVVNG---------RLVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALD 416
|
490
....*....|....*
gi 635952396 943 ELPLSANGKLDRKAL 957
Cdd:cd17653 417 SFPLTANGKVDRKAL 431
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
468-958 |
7.08e-107 |
|
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: 346.38 E-value: 7.08e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 468 TPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMM 547
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 548 LEDARPSLLITSEDQLARFSDiPGLESLCYQQPLAAGDDAPLALS-KPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW 626
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSF-NKSTILLEDPSISQEDTSNIDYInNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 627 MQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTThFVPSMLAAFVASLD- 705
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSERe 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 706 -ADSVAACrtLRRVFCSGEALP-TELCREWERLTGAPLHNLYGPTEAAVdVSWYP----ACGPELAavtgssvPIGWPVW 779
Cdd:cd17656 239 fINRFPTC--VKHIITAGEQLViTNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTinpeAEIPELP-------PIGKPIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 780 NTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQL 859
Cdd:cd17656 309 NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 860 KIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdaRQLVGYLVSDSGLPldTAALKARLAEQLPPHMVPVVLM 939
Cdd:cd17656 389 KIRGYRIELGEIEAQLLNHPGVSEAV----VLDKADDKGE--KYLCAYFVMEQELN--ISQLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*....
gi 635952396 940 QLAELPLSANGKLDRKALP 958
Cdd:cd17656 461 PLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
460-957 |
1.20e-106 |
|
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: 345.68 E-value: 1.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 460 LVADQARKTPDAPALADarW--QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDT 537
Cdd:cd05918 4 LIEERARSQPDAPAVCA--WdgSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 538 GYPDDRLRMMLEDARPSLLITSedqlarfsdipgleslcyqqplaagddaplalsKPDHTAYIIFTSGSTGRPKGVMVGQ 617
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLTS---------------------------------SPSDAAYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 618 TAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAePEAHRdPQAMQQFFARYGVTTTHFVPSml 697
Cdd:cd05918 129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIP-SEEDR-LNDLAGFINRLRVTWAFLTPS-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 698 aaFVASLDADSVAacrTLRRVFCSGEALPTELCREWErlTGAPLHNLYGPTEAAVdvswYPACGPELAAVTGSSvpIGWP 777
Cdd:cd05918 205 --VARLLDPEDVP---SLRTLVLGGEALTQSDVDTWA--DRVRLINAYGPAECTI----AATVSPVVPSTDPRN--IGRP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 778 VwNTGLRILDAA--MRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP-------FAPGERMYRTGDVARWLTNGA 848
Cdd:cd05918 272 L-GATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGS 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 849 VEYLGRSDDQLKIRGQRIELGEI-DRVMSGLPDVAQAVSHACVFnqaaATGGDARQLVGYLVSDSG-------------- 913
Cdd:cd05918 351 LEYVGRKDTQVKIRGQRVELGEIeHHLRQSLPGAKEVVVEVVKP----KDGSSSPQLVAFVVLDGSssgsgdgdslflep 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 635952396 914 ---LPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05918 427 sdeFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
460-958 |
1.73e-105 |
|
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: 341.07 E-value: 1.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 460 LVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITSEDQLArfsdipgleslcyqqplaagddaplalskpdhtaYIIFTSGSTGRPKGVMVGQTA 619
Cdd:cd17645 83 PGERIAYMLADSSAKILLTNPDDLA----------------------------------YVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 620 IVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTThFVPSMLAA 699
Cdd:cd17645 129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIS-FLPTGAAE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 700 FVASLDADSvaacrtLRRVFCSGEALptelcREWERlTGAPLHNLYGPTEAAVDVSWYPACGPElaavtgSSVPIGWPVW 779
Cdd:cd17645 208 QFMQLDNQS------LRVLLTGGDKL-----KKIER-KGYKLVNNYGPTENTVVATSFEIDKPY------ANIPIGKPID 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 780 NTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQL 859
Cdd:cd17645 270 NTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 860 KIRGQRIELGEIDRVMSGLPDVAQAVShacvfnQAAATGGDARQLVGYLVSDSGLPLDtaALKARLAEQLPPHMVPVVLM 939
Cdd:cd17645 350 KIRGYRIEPGEIEPFLMNHPLIELAAV------LAKEDADGRKYLVAYVTAPEEIPHE--ELREWLKNDLPDYMIPTYFV 421
|
490
....*....|....*....
gi 635952396 940 QLAELPLSANGKLDRKALP 958
Cdd:cd17645 422 HLKALPLTANGKVDRKALP 440
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
457-957 |
2.50e-104 |
|
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: 338.32 E-value: 2.50e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 457 LSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLD 536
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 537 TGYPDDRLRMMLEDARPSLLITsedqlarfsdipgleslcyqqplaagddaplalskpdhtAYIIFTSGSTGRPKGVMVG 616
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 617 QTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWW-PFIAGAQLVMAEpeaHRDPQAMQQFFARYGVTTTHFVPS 695
Cdd:COG0318 122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 696 MLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTgssvpIG 775
Cdd:COG0318 199 MLARLLRHPEFARYDL-SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGS-----VG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 776 WPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiADPFapgermYRTGDVARWLTNGAVEYLGRS 855
Cdd:COG0318 273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 856 DDQLKIRGQRIELGEIDRVMSGLPDVAQavshACVFNQAAATGGDArqLVGYLVSDSGLPLDTAALKARLAEQLPPHMVP 935
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAE----AAVVGVPDEKWGER--VVAFVVLRPGAELDAEELRAFLRERLARYKVP 419
|
490 500
....*....|....*....|..
gi 635952396 936 VVLMQLAELPLSANGKLDRKAL 957
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRAL 441
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
469-958 |
3.63e-102 |
|
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: 332.44 E-value: 3.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRG-VKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMM 547
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 548 LEDARPSLLITSEDQLArfsdipgleslcyqqplaagddaplalskpdhtaYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 627
Cdd:cd17648 81 LEDTGARVVITNSTDLA----------------------------------YAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 628 QDRYPLSAQD--VVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFvasld 705
Cdd:cd17648 127 SERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 706 adSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTgssvpIGWPVWNTGLRI 785
Cdd:cd17648 202 --DLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDKS-----LGRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 786 LDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGE-------RMYRTGDVARWLTNGAVEYLGRSDD 857
Cdd:cd17648 275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQtEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 858 QLKIRGQRIELGEIDRVMSGLPDVAQAVSHACVFNQAAATGGDaRQLVGYLVSDSGlPLDTAALKARLAEQLPPHMVPVV 937
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQ-KYLVGYYLPEPG-HVPESDLLSFLRAKLPRYMVPAR 432
|
490 500
....*....|....*....|.
gi 635952396 938 LMQLAELPLSANGKLDRKALP 958
Cdd:cd17648 433 LVRLEGIPVTINGKLDVRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
480-1053 |
8.30e-100 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 352.93 E-value: 8.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS 559
Cdd:PRK05691 3745 QWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 EDQLARFSDIpgLESL-CYQQP-------LAAGDDA---PLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:PRK05691 3825 AACREQARAL--LDELgCANRPrllvweeVQAGEVAshnPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKV 3902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPS----MLAAFVASL 704
Cdd:PRK05691 3903 PYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSliqgMLAEDRQAL 3982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 705 DAdsvaacrtLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPAcgpELAAVTGSSVPIGWPVWNTGL 783
Cdd:PRK05691 3983 DG--------LRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSDDVAFFRV---DLASTRGSYLPIGSPTDNNRL 4051
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 784 RILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLKIR 862
Cdd:PRK05691 4052 YLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIR 4131
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 863 GQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGgdaRQLVGYLVSDSGLPLDTAAL---KARLAEQLPPHMVPVVLM 939
Cdd:PRK05691 4132 GYRIELGEIEARLHEQAEVREAA----VAVQEGVNG---KHLVGYLVPHQTVLAQGALLeriKQRLRAELPDYMVPLHWL 4204
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 940 QLAELPLSANGKLDRKALPLPTLGGERSG--RPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQLSR 1017
Cdd:PRK05691 4205 WLDRLPLNANGKLDRKALPALDIGQLQSQayLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQK 4284
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 635952396 1018 QLARQVTPGQVMVASTVGKLSA----LLAADLSDEQARRL 1053
Cdd:PRK05691 4285 ALQRNVPLRAMFECSTVEELAEyiegLAGSAIDEQKVDRL 4324
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
6-442 |
2.34e-88 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 294.24 E-value: 2.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 6 PLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEE-GEVWQWVAADRTFgEPSI 84
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEnGEPVQVILEERPF-ELEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 85 IDLR--TAPDPHRAATERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQR 162
Cdd:pfam00668 85 IDISdlSESEEEEAIEAFIQRDLQSPFDLEKG-PLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 163 GEATPESPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASL---SAAPLGGRAAGSDIwRMKLEMNADAFRRL 239
Cdd:pfam00668 164 GEPLPLPPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLpkdYARPADRSFKGDRL-SFTLDEDTEELLRK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 240 AGHAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKK 319
Cdd:pfam00668 243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 320 MRRHQRYDAEQIVRDSG--KAAGDEPLFGPVLNVKVFDYQLdidgVQAVTHTLATGPVN-----------DLELALFPDE 386
Cdd:pfam00668 323 AEPHQGYPFGDLVNDLRlpRDLSRHPLFDPMFSFQNYLGQD----SQEEEFQLSELDLSvssvieeeakyDLSLTASERG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 387 tGGLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARL 442
Cdd:pfam00668 399 -GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
596-953 |
2.07e-70 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 239.49 E-value: 2.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 596 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPeahRDP 675
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 676 QAMQQFFARYGVTTTHFVPSMLAAFVAsLDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVS 755
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLK-APESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WYPacGPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiadpfapGERMY 835
Cdd:cd04433 157 TGP--PDDDARKPGS---VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 836 RTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQavshACVFNQAAATGGDArqLVGYLVSDSGLP 915
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE----AAVVGVPDPEWGER--VVAVVVLRPGAD 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 635952396 916 LDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLD 953
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
292-1034 |
1.58e-66 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 247.67 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 292 NVLPLAVHIDAQETLADLAMRLAAQLKKMRRHQRYDAEQIVRDSGKAAGDEPLfgPVLnvkvfdYQLDIDGVQAVTHT-L 370
Cdd:TIGR03443 80 RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERT--PPL------FRLAFQDAPDNQQTtY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 371 ATGPVNDLELALFPdETGGLSLEILANKARYDEAELRRHVARLTALLAQFAADPALRCGEAEMLSANELARLaavndtvv 450
Cdd:TIGR03443 152 STGSTTDLTVFLTP-SSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLL-------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 451 PLPATTLS---------ALVADQARKTPD---------APALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVAL 512
Cdd:TIGR03443 223 PDPTKDLDwsgfrgaihDIFADNAEKHPDrtcvvetpsFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 513 PRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE-----DQLAR---------FSDIPGLE----- 573
Cdd:TIGR03443 303 YRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEkagtlDQLVRdyidkelelRTEIPALAlqddg 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 574 SL-----------CYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQK 642
Cdd:TIGR03443 383 SLvggsleggetdVLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTML 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 643 TPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSM--LaafvasLDADSVAACRTLRRVFC 720
Cdd:TIGR03443 463 SGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMgqL------LSAQATTPIPSLHHAFF 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 721 SGEALPTELCREWERLtgAP---LHNLYGPTEAAVDVSWYpacgpELAAVTGSS---------VPIGWPVWNTGLRILDA 788
Cdd:TIGR03443 537 VGDILTKRDCLRLQTL--AEnvcIVNMYGTTETQRAVSYF-----EIPSRSSDStflknlkdvMPAGKGMKNVQLLVVNR 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 789 AMRPVPPGVA--GDLYLTGIQLAQGYLGRPDLTASRFI----ADP------------------FAPGERMYRTGDVARWL 844
Cdd:TIGR03443 610 NDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVnnwfVDPshwidldkennkperefwLGPRDRLYRTGDLGRYL 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 845 TNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAV--------------SHACVFNQAAATGG---------DA 901
Cdd:TIGR03443 690 PDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlvrrdkdeeptlvSYIVPQDKSDELEEfksevddeeSS 769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 902 RQLVGYLVSDSGLPLDtaaLKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPT---LGGERSGRPPEPGMETL 978
Cdd:TIGR03443 770 DPVVKGLIKYRKLIKD---IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaqLAAVAKNRSASAADEEF 846
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 979 VATAFsqllgcEVNDI--------------DADFFALGGHSLLAMRLAAQLSRQLARQVTPGQVMVASTV 1034
Cdd:TIGR03443 847 TETER------EIRDLwlellpnrpatispDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTI 910
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
465-957 |
2.58e-65 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 230.42 E-value: 2.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRL 544
Cdd:TIGR01734 10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 545 RMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDdaPLALSKP---DHTAYIIFTSGSTGRPKGVMVGQTAIV 621
Cdd:TIGR01734 90 EMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGG--PVSFDHAvkgDDNYYIIYTSGSTGNPKGVQISHDNLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 622 NRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEfWWPFIA-GAQLVMAEPEAHRDPqamQQFFARYG-------VTTTHFV 693
Cdd:TIGR01734 168 SFTNWMLADFPLSEGKQFLNQAPFSFDLSVMD-LYPCLAsGGTLHCLDKDITNNF---KLLFEELPktglnvwVSTPSFV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 694 PsmLAAFVASLDADSVAacRTLRRVFCsGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYpACGPELAAvTGSSV 772
Cdd:TIGR01734 244 D--MCLLDPNFNQENYP--HLTHFLFC-GEELPVKTAKALlERFPKATIYNTYGPTEATVAVTSV-KITQEILD-QYPRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 773 PIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpFAPGERMYRTGDVARwLTNGAVEYL 852
Cdd:TIGR01734 317 PIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 853 GRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHACVFNQAAATggdarQLVGYLVS-----DSGLPLdTAALKARLAE 927
Cdd:TIGR01734 393 GRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKVE-----YLIAAIVPetedfEKEFQL-TKAIKKELKK 466
|
490 500 510
....*....|....*....|....*....|
gi 635952396 928 QLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:TIGR01734 467 SLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
465-957 |
1.06e-62 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 222.85 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRL 544
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 545 RMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALS-KPDHTAYIIFTSGSTGRPKGVMVGQTAIVNR 623
Cdd:PRK04813 92 EMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAvKGDDNYYIIFTSGTTGKPKGVQISHDNLVSF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 624 LLWMQDRYPLSAQDVVAQKTPCSFDVSVWEfWWPFIA-GAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPS------M 696
Cdd:PRK04813 172 TNWMLEDFALPEGPQFLNQAPYSFDLSVMD-LYPTLAsGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSfadmclL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 697 LAAFVASLDADsvaacrtLRR-VFCsGEALPTELCRE-WERLTGAPLHNLYGPTEAAVDVSWYpACGPELAAvTGSSVPI 774
Cdd:PRK04813 251 DPSFNEEHLPN-------LTHfLFC-GEELPHKTAKKlLERFPSATIYNTYGPTEATVAVTSI-EITDEMLD-QYKRLPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 775 GWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARwLTNGAVEYLGR 854
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF---DGQPAYHTGDAGY-LEDGLLFYQGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 855 SDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshACVFNQaaatGGDARQLVGYLVSDSG-----LPLdTAALKARLAEQL 929
Cdd:PRK04813 397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAV--VVPYNK----DHKVQYLIAYVVPKEEdfereFEL-TKAIKKELKERL 469
|
490 500
....*....|....*....|....*...
gi 635952396 930 PPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK04813 470 MEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
459-1293 |
1.46e-62 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 230.75 E-value: 1.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 459 ALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTG 538
Cdd:COG3319 5 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 539 YPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:COG3319 85 ALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 619 AIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLA 698
Cdd:COG3319 165 VLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 699 AFVASLDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTGSSVPIGWPV 778
Cdd:COG3319 245 AALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 779 WNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQ 858
Cdd:COG3319 325 LVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 859 LKIRGQRIELGEIDRVMSGLPDVAQAVshacvfnQAAATGGDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVL 938
Cdd:COG3319 405 RLRRGLREELEEAEAALAEAAAVAAAV-------AAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 939 MQLAELPLSANGKLDRKALPLPTLGGERSGRPPEPGMETLVATAFSQLLGCEVNDIDADFFALGGHSLLAMRLAAQLSRQ 1018
Cdd:COG3319 478 LLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLAL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1019 LARQVTPGQVMVASTVgklsALLAADLSDEQARRLGLDTLLPLRESDGPTLFCFHPASGFAWQFSVLARYLSPRWSITGI 1098
Cdd:COG3319 558 LLRLLLLLALLLAPTL----AALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGL 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1099 QSPRPQGPMASAASLDEVCEHHLRTLLAQQPHGPYYLFGYSLGGTLAQGIAARLRQRGEAVAFLGLLDTWPPET------ 1172
Cdd:COG3319 634 QAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGAlarlde 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1173 ----QNWAEKEANGLDPEVLAEIDRE-----------REAFLAAQQGQASGELFSAIEGNYADAVRLLTTAHSAKFDGKA 1237
Cdd:COG3319 714 aellAALLRDLARGVDLPLDAEELRAldpeerlarllERLREAGLPAGLDAERLRRLLRVFRANLRALRRYRPRPYDGPV 793
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 1238 TLFVAEKTRQAG-MDPQVVWGPWVA-ELEVFSQNCAHVDIISPQAFEAIGPVVREILG 1293
Cdd:COG3319 794 LLFRAEEDPPGRaDDPALGWRPLVAgGLEVHDVPGDHFSMLREPHVAELAAALRAALA 851
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
465-957 |
3.21e-60 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 217.29 E-value: 3.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALadaRW--------QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLD 536
Cdd:COG0365 19 AEGRGDKVAL---IWegedgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 537 TGY-PDDrLRMMLEDARPSLLITSEDQLARFSDI-------------PGLESLCYQQPLAAGDDAPLALS---------- 592
Cdd:COG0365 96 PGFgAEA-LADRIEDAEAKVLITADGGLRGGKVIdlkekvdealeelPSLEHVIVVGRTGADVPMEGDLDwdellaaasa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 593 -------KPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW-MQDRYPLSAQDVVAQKTPCSFDVSVWefWW---PFIAG 661
Cdd:COG0365 175 efepeptDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVFWCTADIGWATGHS--YIvygPLLNG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 662 AQLVMAE-PEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASlDADSVAACR--TLRRVFCSGEALPTELCREWERLTG 738
Cdd:COG0365 253 ATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKA-GDEPLKKYDlsSLRLLGSAGEPLNPEVWEWWYEAVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 739 APLHNLYGPTEAavdVSWYPACGPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTG--IQLAQGYLGRP 816
Cdd:COG0365 332 VPIVDGWGQTET---GGIFISNLPGLPVKPGS---MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 817 DLTASRFiadpFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAA 896
Cdd:COG0365 406 ERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA----VVGVPDE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635952396 897 TGGDArqLVGYLVSDSGLPLD---TAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:COG0365 478 IRGQV--VKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
481-960 |
3.37e-59 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 213.15 E-value: 3.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:cd17647 21 FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVIR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 dqlarfsdipgleslcyqqplAAGddaplALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVA 640
Cdd:cd17647 101 ---------------------AAG-----VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 641 QKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAfvasLDADSVAACRTLRRVFC 720
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQL----LTAQATTPFPKLHHAFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 721 SGEALPTELCREWERLT-GAPLHNLYGPTEAAVDVSWY--PACG--PELAAVTGSSVPIGWPVWNTGLRILDAAMRPVPP 795
Cdd:cd17647 231 VGDILTKRDCLRLQTLAeNVRIVNMYGTTETQRAVSYFevPSRSsdPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQIC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 796 GVA--GDLYLTGIQLAQGYLGRPDLTASRFI----ADP------------------FAPGERMYRTGDVARWLTNGAVEY 851
Cdd:cd17647 311 GIGevGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfwLGPRDRLYRTGDLGRYLPNGDCEC 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 852 LGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVShaCVFNQAaatgGDARQLVGYLVSDSGLPLDTAA----------- 920
Cdd:cd17647 391 CGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT--LVRRDK----DEEPTLVSYIVPRFDKPDDESFaqedvpkevst 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 921 ----------------LKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLP 960
Cdd:cd17647 465 dpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
457-957 |
6.92e-58 |
|
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: 207.80 E-value: 6.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 457 LSALVADQARKTPDAPALA-DARWQfSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL 535
Cdd:cd05936 1 LADLLEEAARRFPDKTALIfMGRKL-TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLITSEDqlarFSDIpgLESlcyqqplAAGDDAPLALSKPDhTAYIIFTSGSTGRPKGVMV 615
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVS----FTDL--LAA-------GAPLGERVALTPED-VAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 616 GQTAIVNRLL----WMQDryPLSAQDVV----------AQkTPCSFdvsvwefwWPFIAGAQLVMaEPEAhRDPQAMQQF 681
Cdd:cd05936 146 THRNLVANALqikaWLED--LLEGDDVVlaalplfhvfGL-TVALL--------LPLALGATIVL-IPRF-RPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 682 fARYGVTTTHFVPSMLAAFVAsLDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAavdvSWYPACG 761
Cdd:cd05936 213 -RKHRVTIFPGVPTMYIALLN-APEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTET----SPVVAVN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 762 PelaaVTGSSVP--IGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGD 839
Cdd:cd05936 287 P----LDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 840 VARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDArqLVGYLVSDSGLPLDTA 919
Cdd:cd05936 356 IGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAA----VVGVPDPYSGEA--VKAFVVLKEGASLTEE 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 635952396 920 ALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05936 430 EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1067-1277 |
2.59e-49 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 174.50 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1067 PTLFCFHPASGFAWQFSVLARYLSPRWSITGIQSPRPQGPMASAASLDEVCEHHLRTLLAQQPHGPYYLFGYSLGGTLAQ 1146
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1147 GIAARLRQRGEAVAFLGLLDTWPPETqNWAEKEANGLDPEVLAEIDREREaflAAQQGQASGELFSAIEGNYADAVRLLT 1226
Cdd:pfam00975 81 EVARRLERQGEAVRSLFLSDASAPHT-VRYEASRAPDDDEVVAEFTDEGG---TPEELLEDEELLSMLLPALRADYRALE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 635952396 1227 TAHSAKFDG-KATLFVAEKTRQAGMD--PQVVWGPWVAELEVFSQNCAHVDIIS 1277
Cdd:pfam00975 157 SYSCPPLDAqSATLFYGSDDPLHDADdlAEWVRDHTPGEFDVHVFDGDHFYLIE 210
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
480-952 |
1.99e-48 |
|
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: 180.49 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS 559
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 EDQLARFSDI-----------------PGLESLC-YQQPLAAGDDAPLALSK---PDHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd05911 90 PDGLEKVKEAakelgpkdkiivlddkpDGVLSIEdLLSPTLGEEDEDLPPPLkdgKDDTAAILYSSGTTGLPKGVCLSHR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 619 AIVNRLLWMQDRYPLSAQDVVAQKTPCSFdvsvweFWwpfIAGAQLVMAEPeAHRDPQ-AMQQFF--------ARYGVTT 689
Cdd:cd05911 170 NLIANLSQVQTFLYGNDGSNDVILGFLPL------YH---IYGLFTTLASL-LNGATViIMPKFDselfldliEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 690 THFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYpacgPELAAVT 768
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDK-YDLSSLRVILSGGAPLSKELQELLaKRFPNATIKQGYGMTETGGILTVN----PDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 769 GSSvpiGWPVWNTGLRILDAA-MRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNG 847
Cdd:cd05911 315 GSV---GRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 848 AVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAqavsHACVFNQAAATGGDARqlVGYLVSDSGLPLDTAALKARLAE 927
Cdd:cd05911 386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVA----DAAVIGIPDEVSGELP--RAYVVRKPGEKLTEKEVKDYVAK 459
|
490 500
....*....|....*....|....*...
gi 635952396 928 QLPPH---MVPVVLMQlaELPLSANGKL 952
Cdd:cd05911 460 KVASYkqlRGGVVFVD--EIPKSASGKI 485
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
469-957 |
1.29e-47 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 177.28 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQ----FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRL 544
Cdd:cd17654 1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 545 RMMLEDARPSLLITSEDQLARFSdipgleslcYQQPLAAGDDAPLALSkpdhTAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELDNAPL---------SFTPEHRHFNIRTDEC----LAYVIHTSGTTGTPKIVAVPHKCILPNI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 625 LWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQ-FFARYGVTTTHFVPSMLAAFVAS 703
Cdd:cd17654 148 QHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFGSQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 704 LDADSV-AACRTLRRVFCSGEALPTELCREWERLTGAPLH--NLYGPTEAAVDVSWYPAcgPELAavtgSSVPIGWPVWN 780
Cdd:cd17654 228 SIKSTVlSATSSLRVLALGGEPFPSLVILSSWRGKGNRTRifNIYGITEVSCWALAYKV--PEED----SPVQLGSPLLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 781 TGLRILDAAMRPvppgVAGDLYLTGIQLA---QGYLGRPDLTasrfiadpfapgerMYRTGDVARwLTNGAVEYLGRSDD 857
Cdd:cd17654 302 TVIEVRDQNGSE----GTGQVFLGGLNRVcilDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 858 QLKIRGQRIELGEIDRVMSGLPDVAQavSHACVFNQaaatggdaRQLVGYLVsdsGLPLDTAALKARLAEQLPPHMVPVV 937
Cdd:cd17654 363 QIKRRGKRINLDLIQQVIESCLGVES--CAVTLSDQ--------QRLIAFIV---GESSSSRIHKELQLTLLSSHAIPDT 429
|
490 500
....*....|....*....|
gi 635952396 938 LMQLAELPLSANGKLDRKAL 957
Cdd:cd17654 430 FVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
456-957 |
2.34e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 178.46 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRS-VFLTlALHGIVEAGAAWLP 534
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNShEYLE-AYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 LDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPGL--------------------ESLCYQQPLAAG-DDAPLALSK 593
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlptvrtvivegdgpaaplapEVGEYEELLAAAsDTFDFPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHTAYIIFTSGSTGRPKGVM------VGQTAIVNRllWMQdrypLSAQDVVAQKTPCsFDVSVWefWWPFIA---GAQL 664
Cdd:PRK06187 166 ENDAAAMLYTSGTTGHPKGVVlshrnlFLHSLAVCA--WLK----LSRDDVYLVIVPM-FHVHAW--GLPYLAlmaGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 665 VMaepeAHR-DPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRtLRRVFCSGEALPTELCREWERLTGAPLHN 743
Cdd:PRK06187 237 VI----PRRfDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSS-LRLVIYGGAALPPALLREFKEKFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 744 LYGPTEAA--VDVSWYPACGPELAAVTGSSvpiGWPVWNTGLRILDAAMRPVPP--GVAGDLYLTGIQLAQGYLGRPDLT 819
Cdd:PRK06187 312 GYGMTETSpvVSVLPPEDQLPGQWTKRRSA---GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEAT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 820 ASRFIADpfapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQavshACVFNQAAATGG 899
Cdd:PRK06187 389 AETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAE----VAVIGVPDEKWG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 900 DArqLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK06187 458 ER--PVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
480-958 |
4.97e-47 |
|
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: 174.79 E-value: 4.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS 559
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 edqlarfsdipgleslcyqqplaagddaplalskpdhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVV 639
Cdd:cd05934 83 -------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 640 AQKTPCSF-DVSVWEFWWPFIAGAQLVMAEPEAHRdpqamqQFFA---RYGVTTTHFVPSMLAAFVASLDADSVAACRtL 715
Cdd:cd05934 126 LTVLPLFHiNAQAVSVLAALSVGATLVLLPRFSAS------RFWSdvrRYGATVTNYLGAMLSYLLAQPPSPDDRAHR-L 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 716 RRVFCSgeALPTELCREWERLTGAPLHNLYGPTEAAVDVswypACGPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPP 795
Cdd:cd05934 199 RAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGV----IGPRDEPRRPGS---IGRPAPGYEVRIVDDDGQELPA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 796 GVAGDLYLTGIQ---LAQGYLGRPDLTASRfiadpFAPGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEID 872
Cdd:cd05934 270 GEPGELVIRGLRgwgFFKGYYNMPEATAEA-----MRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 873 RVMSGLPDVAQAVSHACvfnqAAATGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:cd05934 343 RAILRHPAVREAAVVAV----PDEVGED--EVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
....*.
gi 635952396 953 DRKALP 958
Cdd:cd05934 417 AKAQLR 422
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
465-954 |
2.52e-46 |
|
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: 173.18 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRL 544
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 545 RMMLEDARPSLLItsedqlarfsdipgleslcyqqplaagddaplalskpDHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:cd17631 85 AYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 625 LWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWP-FIAGAQLVMaepEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVAS 703
Cdd:cd17631 128 VNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVI---LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 704 LDADSVAACRtLRRVFCSGEALPTELCREWERlTGAPLHNLYGPTEAAVDVSWYPacgPELA-AVTGSsvpIGWPVWNTG 782
Cdd:cd17631 205 PRFATTDLSS-LRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLS---PEDHrRKLGS---AGRPVFFVE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 783 LRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASrFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIR 862
Cdd:cd17631 277 VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-AFRDGW------FHTGDLGRLDEDGYLYIVDRKKDMIISG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 863 GQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDARQLVgyLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLA 942
Cdd:cd17631 350 GENVYPAEVEDVLYEHPAVAEVA----VIGVPDEKWGEAVVAV--VVPRPGAELDEDELIAHCRERLARYKIPKSVEFVD 423
|
490
....*....|..
gi 635952396 943 ELPLSANGKLDR 954
Cdd:cd17631 424 ALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
472-957 |
1.38e-44 |
|
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: 168.02 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 472 PALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDA 551
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 552 RPSLLITSEDQLArfsdipgleslcyqqplaagddaplalskpdhtaYIIFTSGSTGRPKGVMVGQTaivnRLLWMQDRY 631
Cdd:cd05919 82 EARLVVTSADDIA----------------------------------YLLYSSGTTGPPKGVMHAHR----DPLLFADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 632 P-----LSAQDVVAQKTPCSFDVSVW-EFWWPFIAGAQLVMAEpeAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLD 705
Cdd:cd05919 124 ArealgLTPGDRVFSSAKMFFGYGLGnSLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 706 ADSvAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAA-VDVSWYPAcgpelAAVTGSSvpiGWPVWNTGLR 784
Cdd:cd05919 202 GSP-DALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPG-----AWRLGST---GRPVPGYEIR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 785 ILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQ 864
Cdd:cd05919 273 LVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 865 RIELGEIDRVMSGLPDVAQAVSHACvfnqaaATGGDARQLVGYLVSDSGLPLDTA---ALKARLAEQLPPHMVPVVLMQL 941
Cdd:cd05919 346 WVSPVEVESLIIQHPAVAEAAVVAV------PESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFV 419
|
490
....*....|....*.
gi 635952396 942 AELPLSANGKLDRKAL 957
Cdd:cd05919 420 DELPRTATGKLQRFKL 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
469-957 |
3.23e-44 |
|
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: 168.26 E-value: 3.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALA--DARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRM 546
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 547 MLEDARPSLLITSEDQL---------------------ARFSDIPGLESLCYQQPLAAGdDAPLALSKPDHTAYIIFTSG 605
Cdd:cd05926 81 YLADLGSKLVLTPKGELgpasraasklglailelaldvGVLIRAPSAESLSNLLADKKN-AKSEGVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 606 STGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCsFDVS--VWEFWWPFIAGAQLVMAepeAHRDPQAMQQFFA 683
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLP---PRFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 684 RYGVTTTHFVPSMLAAFVASLDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPAcgPE 763
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPL--PP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 764 LAAVTGSsvpIGWPVwNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARW 843
Cdd:cd05926 314 GPRKPGS---VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 844 LTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHAC---VFNQaaatggdarQLVGYLVSDSGLPLDTAA 920
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpdeKYGE---------EVAAAVVLREGASVTEEE 454
|
490 500 510
....*....|....*....|....*....|....*..
gi 635952396 921 LKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05926 455 LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
470-957 |
8.67e-44 |
|
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: 165.93 E-value: 8.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 470 DAPALADARWQFSYREMRQQVVALA-QLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLAnRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLItsedqlarfsdipgleslcyqqplaagddaplalsKPdhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd05941 81 TDSEPSLVL-----------------------------------DP---ALILYTSGTTGRPKGVVLTHANLAANVRALV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTP------------CsfdvsvwefwwPFIAGAQLVM------AEPEAHRDPQAMQQFFArygvttt 690
Cdd:cd05941 123 DAWRWTEDDVLLHVLPlhhvhglvnallC-----------PLFAGASVEFlpkfdpKEVAISRLMPSITVFMG------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 691 hfVPSMLAAFVASLDA-------DSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSwYPACGPE 763
Cdd:cd05941 185 --VPTIYTRLLQYYEAhftdpqfARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALS-NPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 764 LAavtGSsvpIGWPVWNTGLRILD-AAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVAR 842
Cdd:cd05941 262 RP---GT---VGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 843 WLTNGAVEYLGR-SDDQLKIRGQRIELGEIDRVMSGLPDVAQavshACVFNQAAATGGDArqLVGYLVSDSGL-PLDTAA 920
Cdd:cd05941 330 VDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSE----CAVIGVPDPDWGER--VVAVVVLRAGAaALSLEE 403
|
490 500 510
....*....|....*....|....*....|....*..
gi 635952396 921 LKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05941 404 LKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
469-957 |
8.95e-42 |
|
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: 161.38 E-value: 8.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSEDQLARF-----SDIPGLESLCYQQP-------------LAAG-DDAPLALSKPDHTAYIIFTSGSTGR 609
Cdd:cd05959 98 EDSRARVVVVSGELAPVLaaaltKSEHTLVVLIVSGGagpeagalllaelVAAEaEQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 610 PKGVMVGQTAIVnrllWMQDRYplsAQDV--VAQKTPCsFDVSVWEF--------WWPFIAGAQLV-MAE-PEAHRDPQA 677
Cdd:cd05959 178 PKGVVHLHADIY----WTAELY---ARNVlgIREDDVC-FSAAKLFFayglgnslTFPLSVGATTVlMPErPTPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 678 MQQF----FarYGVTTthFVPSMLAAFVASLDADSvaacrTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAA-V 752
Cdd:cd05959 250 IRRYrptvF--FGVPT--LYAAMLAAPNLPSRDLS-----SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLhI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 753 DVSWYPAcgpelAAVTGSSvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapGE 832
Cdd:cd05959 321 FLSNRPG-----RVRYGTT---GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 833 rMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshACVfnqAAATGGDARQLVGYLVSDS 912
Cdd:cd05959 387 -WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEA---AVV---GVEDEDGLTKPKAFVVLRP 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 635952396 913 GLP---LDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05959 460 GYEdseALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
456-958 |
1.10e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 162.02 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL 535
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIP---------------------GLESLcyQQPLAAGDDAPL-ALSK 593
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPpdlgrlrawggnpdddepsgsTDETL--DDLIAGSSTAPLpKPPK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHtaYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPC--SFDVSVWEFWWPFiaGAQLVMaepea 671
Cdd:PRK07788 208 PGG--IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL----- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 672 HR--DPQAMQQFFARYGVTTTHFVPSMLAAFVAsLDADSVAA--CRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGP 747
Cdd:PRK07788 279 RRrfDPEATLEDIAKHKATALVVVPVMLSRILD-LGPEVLAKydTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 748 TEAAVDVSWYPAcgpELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGrpdlTASRFIADP 827
Cdd:PRK07788 358 TEVAFATIATPE---DLAEAPGT---VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----GRDKQIIDG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 828 fapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAqavshacvfnQAAATGGD-----AR 902
Cdd:PRK07788 428 ------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVV----------EAAVIGVDdeefgQR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 903 qLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALP 958
Cdd:PRK07788 492 -LRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
490-957 |
1.44e-41 |
|
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: 159.53 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 490 VVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAW----LPLDTGYPDDRLRMMLEDARPSLLITSEDQLAR 565
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLglvfVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 566 FSD------IPGlESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVV 639
Cdd:cd05922 83 LRDalpaspDPG-TVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 640 AQKTPCSFDVSVWEFWWPFIAGAQLVMAEpeAHRDPQAMQQFFARYGVTTTHFVPSmLAAFVASLDADSvAACRTLRRVF 719
Cdd:cd05922 162 LTVLPLSYDYGLSVLNTHLLRGATLVLTN--DGVLDDAFWEDLREHGATGLAGVPS-TYAMLTRLGFDP-AKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CSGEALPTELCREW-ERLTGAPLHNLYGPTEAAVDVSWYPacgPELAAVTGSSvpIGWPVWNTGLRILDAAMRPVPPGVA 798
Cdd:cd05922 238 QAGGRLPQETIARLrELLPGAQVYVMYGQTEATRRMTYLP---PERILEKPGS--IGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 799 GDLYLTGIQLAQGYLGRPdltasRFIADPFAPGERMYrTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDrvmsgl 878
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE------ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 879 pdvaQAVSHACVFNQAAATGGD---ARQLVGYLVSDSGLplDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRK 955
Cdd:cd05922 381 ----AAARSIGLIIEAAAVGLPdplGEKLALFVTAPDKI--DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454
|
..
gi 635952396 956 AL 957
Cdd:cd05922 455 AL 456
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
481-952 |
8.00e-41 |
|
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: 156.77 E-value: 8.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 dqlaRFsdipgleslcyqqplaaGDDAPLALskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVA 640
Cdd:cd05903 82 ----RF-----------------RQFDPAAM--PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 641 QKTPCS-FDVSVWEFWWPFIAGAQLVMAEPeahRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRtLRRVF 719
Cdd:cd05903 139 VASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSR-LRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTGssvpiGWPVWNTGLRILDAAMRPVPPGVAG 799
Cdd:cd05903 215 CGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTD-----GRPLPGVEIKVVDDTGATLAPGVEG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 800 DLYLTGIQLAQGYLGRPDLTASrfiadpfAPGERMYRTGDVARWLTNGAVEYLGRSDDqLKIR-GQRIELGEIDRVMSGL 878
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 879 PDVAQAvshacvfnqAAATGGDAR---QLVGYLVSDSGLPLDTAALKARL-AEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:cd05903 362 PGVIEA---------AVVALPDERlgeRACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
480-957 |
1.04e-39 |
|
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: 153.74 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS 559
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 EdqlarfsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVV 639
Cdd:cd05971 86 G---------------------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 640 AQKTPCS-------FDVSVweFWWPFiaGAQLVmaepeAHR----DPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADS 708
Cdd:cd05971 133 LYWTPADwawigglLDVLL--PSLYF--GVPVL-----AHRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 709 VAAcRTLRRVFCSGEALPTELCrEWERLT-GAPLHNLYGPTEAAVDVSWYPACGPELAAVTGSSVPiGWPVwntglRILD 787
Cdd:cd05971 204 HAQ-VKLRAIATGGESLGEELL-GWAREQfGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIP-GHRV-----AIVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 788 AAMRPVPPGVAGDLyltGIQLAQ-----GYLGRPDLTASRFIADPFapgermyRTGDVARWLTNGAVEYLGRSDDQLKIR 862
Cdd:cd05971 276 DNGTPLPPGEVGEI---AVELPDpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 863 GQRIELGEIDRVMSGLPdvaqAVSHACVFNQAAATGGDarQLVGYLVSDSGLpLDTAALKARLAE----QLPPHMVPVVL 938
Cdd:cd05971 346 GYRIGPAEIEECLLKHP----AVLMAAVVGIPDPIRGE--IVKAFVVLNPGE-TPSDALAREIQElvktRLAAHEYPREI 418
|
490
....*....|....*....
gi 635952396 939 MQLAELPLSANGKLDRKAL 957
Cdd:cd05971 419 EFVNELPRTATGKIRRREL 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
456-957 |
3.28e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 153.91 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL 535
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLITSEDQLARF----SDIPGLESLCY----------------QQPLAAGDDAPLALS-KP 594
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDysatTRLPALEHVVIceteeddphtekmktfTDFLAAGDPAERAPEvDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 595 DHTAYIIFTSGSTGRPKGVMV--GQT----AIVNRLLWMQ--DRY----PLsaqdvvaqktpcsFDVSVWEFWW--PFIA 660
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLthRQLlsnaADWAEYLGLTegDRYlaanPF-------------FHVFGYKAGVnaPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 661 GAQLVmaePEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvAACRTLrRVFCSGEA-LPTELCREWER---- 735
Cdd:PRK07656 233 GATIL---PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-EDLSSL-RLAVTGAAsMPVALLERFESelgv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 736 ---LTGaplhnlYGPTEAAVDVSWYPAcGPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGY 812
Cdd:PRK07656 308 divLTG------YGLSEASGVTTFNRL-DDDRKTVAGT---IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 813 LGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAqavshacvfn 892
Cdd:PRK07656 378 YDDPEATAAAIDADGW------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVA---------- 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 893 QAAATG-GDARQ-LVG--YLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07656 442 EAAVIGvPDERLgEVGkaYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
461-957 |
2.16e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 144.95 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 461 VADQARKTPDAPALAD----ARWqfSYREMRQQVVALAQLLRQRGVKPGDSVAVaLPRSVFLTLALH-GIVEAGAAWLPL 535
Cdd:PRK09088 1 IAFHARLQPQRLAAVDlalgRRW--TYAELDALVGRLAAVLRRRGCVDGERLAV-LARNSVWLVALHfACARVGAIYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLItSEDQLARFSDIPgLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMV 615
Cdd:PRK09088 78 NWRLSASELDALLQDAEPRLLL-GDDAVAAGRTDV-EDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 616 G-----QTAIVNRLLWMQDryplsAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAEPEAhrDPQAMQQFFARYGVTTT 690
Cdd:PRK09088 156 SernlqQTAHNFGVLGRVD-----AHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF--EPKRTLGRLGDPALGIT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 691 HF--VPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREWERlTGAPLHNLYGPTEAAVdVSWYPACGPELAAVT 768
Cdd:PRK09088 229 HYfcVPQMAQAFRAQPGFDA-AALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGT-VFGMSVDCDVIRAKA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 769 GSSvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGA 848
Cdd:PRK09088 306 GAA---GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 849 VEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarqlVGYL--VSDSGLPLDTAALKARLA 926
Cdd:PRK09088 377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECA----VVGMADAQWGE----VGYLaiVPADGAPLDLERIRSHLS 448
|
490 500 510
....*....|....*....|....*....|.
gi 635952396 927 EQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK09088 449 TRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
481-957 |
3.55e-36 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 142.86 E-value: 3.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 DQlarfsdipgleslcyqqplaagddaplalskpdhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVA 640
Cdd:cd05972 81 ED----------------------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 641 QKTPCSFDVSVW-EFWWPFIAGAQLVMAEpEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVAsLDADSVAAcRTLRRVF 719
Cdd:cd05972 127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKF-SHLRLVV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPElaavTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAG 799
Cdd:cd05972 204 SAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVK----PGS---MGRPTPGYDVAIIDDDGRELPPGEEG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 800 DL--YLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDrvmSG 877
Cdd:cd05972 277 DIaiKLPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE---SA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 878 LpdvaqaVSHACVfNQAAATG--GDAR-QLV-GYLVSDSG-LPLDTAA--LKARLAEQLPPHMVPVVLMQLAELPLSANG 950
Cdd:cd05972 347 L------LEHPAV-AEAAVVGspDPVRgEVVkAFVVLTSGyEPSEELAeeLQGHVKKVLAPYKYPREIEFVEELPKTISG 419
|
....*..
gi 635952396 951 KLDRKAL 957
Cdd:cd05972 420 KIRRVEL 426
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
456-957 |
1.22e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 133.86 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV-FLTLALhGIVEAGAAWLP 534
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAaFLELAF-AASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 LDTGYPDDRLRMMLEDARPSLLITSEDqlarFSDIPGLES------LCYQQP---LAAGDD--APLALSKPDHTAYIIFT 603
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEE----FDAIVALETpkividAAAQADsrrLAQGGLeiPPQAAVAPTDLVRLMYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 604 SGSTGRPKGVM----------------VGQTAiVNRLLWMQDRYPLSAQDVvaqktpcsfdvsvwefwwPFIAG-AQLVM 666
Cdd:PRK06145 158 SGTTDRPKGVMhsygnlhwksidhviaLGLTA-SERLLVVGPLYHVGAFDL------------------PGIAVlWVGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 667 AEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCREWERL-TGAPLHNLY 745
Cdd:PRK06145 219 LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDL-DSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 746 GPTEAAVDVSWYPAcGPELAAV--TGSSVPigwpvwNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRF 823
Cdd:PRK06145 298 GLTETCSGDTLMEA-GREIEKIgsTGRALA------HVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 824 IADPFapgermyRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshacvfnqAAATGGDAR- 902
Cdd:PRK06145 371 YGDWF-------RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEA---------AVIGVHDDRw 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 635952396 903 --QLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK06145 435 geRITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
456-957 |
1.44e-32 |
|
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: 133.40 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQ--FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV---FLTLALHgivEAGA 530
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVeavIALLALH---RLGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 531 AWLPLDTGYPDDRLRMMLE-----------DARPS-LLITSEDQLARFSDIPGLESLCyqqplAAGDDAPLALSKPDHTA 598
Cdd:cd05923 79 VPALINPRLKAAELAELIErgemtaaviavDAQVMdAIFQSGVRVLALSDLVGLGEPE-----SAGPLIEDPPREPEQPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 599 YIIFTSGSTGRPKGVMVGQTAIVNRLLWM--QDRYPLSAQDVVAQKTPCSFDVSVWE-FWWPFIAGAQLVMAEpeaHRDP 675
Cdd:cd05923 154 FVFYTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAvLVAALALDGTYVVVE---EFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 676 QAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAvdVS 755
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAG-LKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM--NS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WY---PACGPELAAVTGSSVPIgwpvwntgLRILDAAMRPVPPGVAGDLYLTGIQLA--QGYLGRPDLTASRFIadpfap 830
Cdd:cd05923 308 LYmrdARTGTEMRPGFFSEVRI--------VRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 831 gERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdarQLVGYLVS 910
Cdd:cd05923 374 -DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVV----VIGVADERWG---QSVTACVV 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 635952396 911 DSGLPLDTAALKAR-LAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05923 446 PREGTLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
480-957 |
1.51e-32 |
|
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: 133.91 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVAL---PRSVFLTLALHGIveaGAAWLPLDTGYPDDRLRMMLEDARPSLL 556
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM---GAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 557 ITSEDQLAR-----------------FSDIPGLES-----LCYQQPLAAGDDAPLALSKPDHTAYII-FTSGSTGRPKGV 613
Cdd:cd12119 102 FVDRDFLPLleaiaprlptvehvvvmTDDAAMPEPagvgvLAYEELLAAESPEYDWPDFDENTAAAIcYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 614 MVGQTAIVNRLL--WMQDRYPLSAQDVVAQKTPCsFDVSVWEFwwPFIA---GAQLVMaePEAHRDPQAMQQFFARYGVT 688
Cdd:cd12119 182 VYSHRSLVLHAMaaLLTDGLGLSESDVVLPVVPM-FHVNAWGL--PYAAamvGAKLVL--PGPYLDPASLAELIEREGVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 689 TTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCREWERLtGAPLHNLYGPTEAA--VDVSWYPACGPELAA 766
Cdd:cd12119 257 FAAGVPTVWQGLLDHLEANGRDL-SSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSplGTVARPPSEHSNLSE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 767 VTGSSVPI--GWPVWNTGLRILDAAMRPVP--PGVAGDLYLTGIQLAQGYLGRPDlTASRFIADPFapgermYRTGDVAR 842
Cdd:cd12119 335 DEQLALRAkqGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGW------LRTGDVAT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 843 WLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshACVfnqaaatgG------DARQLVgYLVSDSGLPL 916
Cdd:cd12119 408 IDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEA---AVI--------GvphpkwGERPLA-VVVLKEGATV 475
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 635952396 917 DTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd12119 476 TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
465-957 |
2.33e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 134.03 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALADARW------QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV-FLTLALhGIVEAGAAWLPLDT 537
Cdd:PRK13295 34 VASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWeFTVLYL-ACSRIGAVLNPLMP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 538 GYPDDRLRMMLEDARPSLLITS--------EDQLARF-SDIPGLESLCY----------------QQPLAAGDDAPLALS 592
Cdd:PRK13295 113 IFRERELSFMLKHAESKVLVVPktfrgfdhAAMARRLrPELPALRHVVVvggdgadsfeallitpAWEQEPDAPAILARL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 593 K--PDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVS-VWEFWWPFIAGAQLVMAEP 669
Cdd:PRK13295 193 RpgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLQDI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 670 eahRDPQAMQQFFARYGVTTThfvpsMLAA-FVASLdADSVAACR----TLRRVFCSGEALPTELCREWERLTGAPLHNL 744
Cdd:PRK13295 273 ---WDPARAAELIRTEGVTFT-----MASTpFLTDL-TRAVKESGrpvsSLRTFLCAGAPIPGALVERARAALGAKIVSA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 745 YGPTEAAVDVSWYPACGPELAAVTGssvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFi 824
Cdd:PRK13295 344 WGMTENGAVTLTKLDDPDERASTTD-----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 825 adpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLkIRG-QRIELGEIDRVMSGLPDVAQAvshacvfnqAAATGGDAR- 902
Cdd:PRK13295 418 -------DGWFDTGDLARIDADGYIRISGRSKDVI-IRGgENIPVVEIEALLYRHPAIAQV---------AIVAYPDERl 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 903 --QLVGYLVSDSGLPLDTAALKARLAEQ-LPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK13295 481 geRACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
481-952 |
3.33e-32 |
|
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: 133.86 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 DQLARFSDIPGL----ESLCYQQP-----------------LAAGD---DAPLALSKPDHTA---------YIIFTSGST 607
Cdd:cd17634 165 GGVRAGRSVPLKknvdDALNPNVTsvehvivlkrtgsdidwQEGRDlwwRDLIAKASPEHQPeamnaedplFILYTSGTT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 608 GRPKGVMVGQTAIVNRLLW-MQDRYPLSAQDVVAqktpCSFDVS-----VWEFWWPFIAGAQLVMAEPEA-HRDPQAMQQ 680
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYW----CTADVGwvtghSYLLYGPLACGATTLLYEGVPnWPTPARMWQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 681 FFARYGVTTTHFVPSMLAAfVASLDADSVAA--CRTLRRVFCSGEALPTELCR-EWERLTGA--PLHNLYGPTEaavdVS 755
Cdd:cd17634 321 VVDKHGVNILYTAPTAIRA-LMAAGDDAIEGtdRSSLRILGSVGEPINPEAYEwYWKKIGKEkcPVVDTWWQTE----TG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WypACGPELAAV----TGSSVPigwPVWNTGLRILDAAMRPVPPGVAGDLYLTGI--QLAQGYLGRPDltasRFIADPFA 829
Cdd:cd17634 396 G--FMITPLPGAielkAGSATR---PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFS 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 830 PGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshACVFNQAAATGgdaRQLVGYLV 909
Cdd:cd17634 467 TFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA---AVVGIPHAIKG---QAPYAYVV 540
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 635952396 910 SDSGL-PLDT--AALKARLAEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:cd17634 541 LNHGVePSPElyAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
456-957 |
3.34e-32 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 132.96 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAawLPL 535
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTgYPDDR---LRMMLEDARPSLLITSeDQLARFSDIPGLESLCYQQP-----LAAGD-----------DAPLALSK--- 593
Cdd:COG1021 104 FA-LPAHRraeISHFAEQSEAVAYIIP-DRHRGFDYRALARELQAEVPslrhvLVVGDageftsldallAAPADLSEprp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 -PDHTAYIIFTSGSTGRPKGV---------MVGQTAIVNRLLwMQDRY----------PLSAqdvvaqktPCSFDVsvwe 653
Cdd:COG1021 182 dPDDVAFFQLSGGTTGLPKLIprthddylySVRASAEICGLD-ADTVYlaalpaahnfPLSS--------PGVLGV---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 654 fwwpFIAGAQLVMAEpeahrDPQAMQQF--FARYGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCR 731
Cdd:COG1021 249 ----LYAGGTVVLAP-----DPSPDTAFplIERERVTVTALVPPLALLWLDAAERSR-YDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 732 EWERLTGAPLHNLYGPTEAAV------DvswypacgPELAAVTGSSVPIgwPVWNTgLRILDAAMRPVPPGVAGDLYLTG 805
Cdd:COG1021 319 RVRPALGCTLQQVFGMAEGLVnytrldD--------PEEVILTTQGRPI--SPDDE-VRIVDEDGNPVPPGEVGELLTRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 806 IQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLkIR-GQRIELGEIDRVMSGLPDVAQA 884
Cdd:COG1021 388 PYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDA 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 885 vshACVfnqaaatgGDARQLVG-----YLVSDsGLPLDTAALKARLAEQ-LPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:COG1021 461 ---AVV--------AMPDEYLGerscaFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
458-957 |
8.94e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 131.54 E-value: 8.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 458 SALVADQARktPDAPAL---ADARWqfSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV---FLTLAlhgIVEAGAA 531
Cdd:PRK07514 7 DALRAAFAD--RDAPFIetpDGLRY--TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPealALYLA---TLRAGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 532 WLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDI------PGLESL-------CYQQPLAAGDDAPLALSKPDHTA 598
Cdd:PRK07514 80 FLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIaaaagaPHVETLdadgtgsLLEAAAAAPDDFETVPRGADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 599 YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDV--------------VAqkTPCSfdvsvwefwwpFIAGAQL 664
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVlihalpifhthglfVA--TNVA-----------LLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 665 VMAepeAHRDPQAMQQFFAR----YGVTTthFVPSMLAAfvASLDADsvaACRTLrRVFCSGEA-LPTELCREWERLTGA 739
Cdd:PRK07514 227 IFL---PKFDPDAVLALMPRatvmMGVPT--FYTRLLQE--PRLTRE---AAAHM-RLFISGSApLLAETHREFQERTGH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 740 PLHNLYGPTEAAVDVSwypacGPELAAVTGSSVpiGWPVWNTGLRILD-AAMRPVPPGVAGDLYLTGIQLAQGYLGRPDL 818
Cdd:PRK07514 296 AILERYGMTETNMNTS-----NPYDGERRAGTV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 819 TASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDqLKIRG------QRIElGEIDRvmsgLPDVAQA----VSHA 888
Cdd:PRK07514 369 TAEEFRADGF------FITGDLGKIDERGYVHIVGRGKD-LIISGgynvypKEVE-GEIDE----LPGVVESavigVPHP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 889 cVFNQAAatggdarqlVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07514 437 -DFGEGV---------TAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
451-957 |
1.01e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 132.09 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 451 PLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGA 530
Cdd:PRK06178 29 PHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 531 AWLPLDTGYPDDRLRMMLEDARPSLLITsEDQLA------------------RFSD-------IPGLESLCYQQPLAAG- 584
Cdd:PRK06178 109 VHVPVSPLFREHELSYELNDAGAEVLLA-LDQLApvveqvraetslrhvivtSLADvlpaeptLPLPDSLRAPRLAAAGa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 585 -----------DDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqdrYPLSAQDVVAQ--KTPCSFDVSV 651
Cdd:PRK06178 188 idllpalractAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV---------YTAAAAYAVAVvgGEDSVFLSFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 652 WEFW---------WPFIAGAQLVMAepeAHRDPQAMQQFFARYGVTTThfvpSMLA-AFVASLDADSVAA--CRTLRRVF 719
Cdd:PRK06178 259 PEFWiagenfgllFPLFSGATLVLL---ARWDAVAFMAAVERYRVTRT----VMLVdNAVELMDHPRFAEydLSSLRQVR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CSG--EALPTELCREWERLTGAPLHNL-YGPTEAAVDVSWypACGPELAAVTGSSVPI--GWPVWNTGLRILD-AAMRPV 793
Cdd:PRK06178 332 VVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTF--TAGFQDDDFDLLSQPVfvGLPVPGTEFKICDfETGELL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 794 PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDR 873
Cdd:PRK06178 410 PLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 874 VMSGLPdvaqAVSHACVFNQAAATGGdaRQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMqLAELPLSANGKLD 953
Cdd:PRK06178 483 LLGQHP----AVLGSAVVGRPDPDKG--QVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVR 555
|
....
gi 635952396 954 RKAL 957
Cdd:PRK06178 556 KQDL 559
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
443-957 |
1.58e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 131.42 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 443 AAVNDTVVPLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALP-RSVFLTLA 521
Cdd:PRK06155 9 AARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGnRIEFLDVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 522 LhgiveaGAAWL-----PLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDI-PGLESL------------------CY 577
Cdd:PRK06155 89 L------GCAWLgaiavPINTALRGPQLEHILRNSGARLLVVEAALLAALEAAdPGDLPLpavwlldapasvsvpagwST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 578 QQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTaivnRLLW----MQDRYPLSAQDVVAQKTPCSFDVSVWE 653
Cdd:PRK06155 163 APLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 654 FWWPFIAGAQLVMAEP-EAHRDPQAMqqffARYGVTTTHFVPSMLAAFVASLDADSVAACRtLRRVFcsGEALPTELCRE 732
Cdd:PRK06155 239 FFQALLAGATYVLEPRfSASGFWPAV----RRHGATVTYLLGAMVSILLSQPARESDRAHR-VRVAL--GPGVPAALHAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 733 WERLTGAPLHNLYGPTEAAVdvswyPACGPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQ---LA 809
Cdd:PRK06155 312 FRERFGVDLLDGYGSTETNF-----VIAVTHGSQRPGS---MGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 810 QGYLGRPDLTASRFIADPFAPGERMYRTGDvarwltnGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshac 889
Cdd:PRK06155 384 TGYFGMPEKTVEAWRNLWFHTGDRVVRDAD-------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAA---- 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 890 VFNQAAATGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK06155 453 VFPVPSELGED--EVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
481-884 |
1.12e-30 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 126.85 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 DQLARFSdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVA 640
Cdd:cd05969 81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 641 qktpCSFDV-----SVWEFWWPFIAGAQLVMAEPEAhrDPQAMQQFFARYGVTTTHFVPS---ML----AAFVASLDADS 708
Cdd:cd05969 135 ----CTADPgwvtgTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTairMLmkegDELARKYDLSS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 709 vaacrtLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTE-AAVDVSWYPaCGPelaAVTGSsvpIGWPVWNTGLRILD 787
Cdd:cd05969 209 ------LRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTEtGSIMIANYP-CMP---IKPGS---MGKPLPGVKAAVVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 788 AAMRPVPPGVAGDLYLTG--IQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQR 865
Cdd:cd05969 276 ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR 348
|
410
....*....|....*....
gi 635952396 866 IELGEIDRVMSGLPDVAQA 884
Cdd:cd05969 349 VGPFEVESALMEHPAVAEA 367
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
456-957 |
2.41e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 127.41 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALvadqaRKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAV-ALPRS-VFLTLALHGIVEAGAAWL 533
Cdd:PRK06188 18 LVSAL-----KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNRPeVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 -PLdtGYPDDRLrMMLEDARPSLLITSEDQ--------LARFSDIPGLESLC---YQQPLAAG----DDAPL-ALSKPDH 596
Cdd:PRK06188 93 hPL--GSLDDHA-YVLEDAGISTLIVDPAPfveralalLARVPSLKHVLTLGpvpDGVDLLAAaakfGPAPLvAAALPPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 597 TAYIIFTSGSTGRPKGVMvgqtaIVNRLLWMQDRYPLSAqdvvaqktpcsfdvsvWEfwWPfiAGAQLVMAEPEAHR--- 673
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVM-----GTHRSIATMAQIQLAE----------------WE--WP--ADPRFLMCTPLSHAgga 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 674 ------------------DPQAMQQFFARYGVTTTHFVPSMLAAFvasLDADSVAA--CRTLRRVFCSGEAL-PTELCRE 732
Cdd:PRK06188 225 fflptllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYAL---LDHPDLRTrdLSSLETVYYGASPMsPVRLAEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 733 WERLtGAPLHNLYGPTEAAVDVSW-----YPACGPELAAVTGSSVPigwpvWNTgLRILDAAMRPVPPGVAGDLYLTGIQ 807
Cdd:PRK06188 302 IERF-GPIFAQYYGQTEAPMVITYlrkrdHDPDDPKRLTSCGRPTP-----GLR-VALLDEDGREVAQGEVGEICVRGPL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 808 LAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQavsh 887
Cdd:PRK06188 375 VMDGYWNRPEETAEAFRDG-------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQ---- 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 888 ACVFNQAAATGGDArqLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK06188 444 VAVIGVPDEKWGEA--VTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
482-957 |
1.01e-29 |
|
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: 123.74 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITsed 561
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 562 qlarfsdipgleslcyqqplaagddaplaLSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQ 641
Cdd:cd05935 80 -----------------------------GSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 642 KTPCsFDVS--VWEFWWPFIAGAQLVMAepeAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVF 719
Cdd:cd05935 131 CLPL-FHVTgfVGSLNTAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKT-RDLSSLKVLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAvtgssvpIGWPVWNTGLRILDA-AMRPVPPGVA 798
Cdd:cd05935 206 GGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQC-------LGIP*FGVDARVIDIeTGRELPPNEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 799 GDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGL 878
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 879 PdvaqAVSHACVFNQAAATGGDARQlvGYLVSDSGLPLDTAALK----ARlaEQLPPHMVPVVLMQLAELPLSANGKLDR 954
Cdd:cd05935 356 P----AI*EVCVISVPDERVGEEVK--AFIVLRPEYRGKVTEEDiiewAR--EQMAAYKYPREVEFVDELPRSASGKILW 427
|
...
gi 635952396 955 KAL 957
Cdd:cd05935 428 RLL 430
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
456-960 |
2.51e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 124.49 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALP--RSVFLTLALHGIVeaGAAWL 533
Cdd:PRK13382 44 GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRnhRGFVEALLAANRI--GADIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRLRMMLEDARPSLLITSEDQLAR----FSDIPGL------ESLCYQQPLAAGDDAPLALS---KPDHTAYI 600
Cdd:PRK13382 122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSATvdraLADCPQAtrivawTDEDHDLTVEVLIAAHAGQRpepTGRKGRVI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 601 IFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCsfdVSVWEFwwpfiagAQLV----MAEPEAHR--- 673
Cdd:PRK13382 202 LLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPM---FHAWGF-------SQLVlaasLACTIVTRrrf 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 674 DPQAMQQFFARYGVTTTHFVPSMLAAFV-ASLDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAV 752
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRIMdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 753 DVSWYPAcgpELAAVTGSSvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRpdlTASRFIadpfapgE 832
Cdd:PRK13382 352 IATATPA---DLRAAPDTA---GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFH-------D 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 833 RMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAqavshacvfnQAAATGGDARQ----LVGYL 908
Cdd:PRK13382 416 GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVA----------EAAVIGVDDEQygqrLAAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 635952396 909 VSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLP 960
Cdd:PRK13382 486 VLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
461-957 |
2.73e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.82 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 461 VADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLcyQQPLAAGDDAPLALSKPDH-------TAYII-FTSGSTGRPK 611
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYV--QRVISITSLKEIEDRKIDNfveknesASFIIcYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 612 GVMVGQTAI----VNRLLWMQdrypLSAQDVVAQKTPCSFDVSVWEFWWP-FIAGAQLVMAEpeaHRDPQAMQQFFARYG 686
Cdd:PRK06839 166 GAVLTQENMfwnaLNNTFAID----LTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVPR---KFEPTKALSMIEKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 687 VTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREW-ERltGAPLHNLYGPTEAAVDVswYPACGPELA 765
Cdd:PRK06839 239 VTVVMGVPTIHQALINCSKFET-TNLQSVRWFYNGGAPCPEELMREFiDR--GFLFGQGFGMTETSPTV--FMLSEEDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 766 AVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRfIADPFapgermYRTGDVARWLT 845
Cdd:PRK06839 314 RKVGS---IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW------LCTGDLARVDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 846 NGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDARqlVGYLVSDSGLPLDTAALKARL 925
Cdd:PRK06839 384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVA----VVGRQHVKWGEIP--IAFIVKKSSSVLIEKDVIEHC 457
|
490 500 510
....*....|....*....|....*....|..
gi 635952396 926 AEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK06839 458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
453-928 |
3.58e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.83 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 453 PATTLSALVADQARKTPDAPAL---ADARWQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEA 528
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALrekEDGIWQsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 529 GAAWLPLdtgYPDDR---LRMMLEDARPSLLITS-EDQLARF----SDIPGLE---------------SLCYQQPLAAGD 585
Cdd:COG1022 89 GAVTVPI---YPTSSaeeVAYILNDSGAKVLFVEdQEQLDKLlevrDELPSLRhivvldprglrddprLLSLDELLALGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 586 --------DAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDV---------VAQKTpcsfd 648
Cdd:COG1022 166 evadpaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRtlsflplahVFERT----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 649 vsvWEFWWpFIAGAQLVMAEpeahrDPQAMQQFFARYGVTTTHFVP----SMLAAFVASLDADS----------VAACRT 714
Cdd:COG1022 241 ---VSYYA-LAAGATVAFAE-----SPDTLAEDLREVKPTFMLAVPrvweKVYAGIQAKAEEAGglkrklfrwaLAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 715 -------------------------------------LRRVFCSGEALPTELCReWERLTGAPLHNLYGPTEAAVDVSwy 757
Cdd:COG1022 312 yararlagkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELAR-FFRALGIPVLEGYGLTETSPVIT-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 758 paCGPELAAVTGSsvpIGWPVWNTGLRIldaamrpvppGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRT 837
Cdd:COG1022 389 --VNRPGDNRIGT---VGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 838 GDVARWLTNGAVEYLGRSDDQLKIRG------QRIElgeiDRvMSGLPDVAQAVshacVFnqaaatgGDARQLVGYLVSd 911
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIVTSGgknvapQPIE----NA-LKASPLIEQAV----VV-------GDGRPFLAALIV- 510
|
570
....*....|....*..
gi 635952396 912 sglpLDTAALKARLAEQ 928
Cdd:COG1022 511 ----PDFEALGEWAEEN 523
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
481-957 |
8.74e-29 |
|
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: 122.78 E-value: 8.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTG----YPDDRLR------MMLED 550
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPptydEPNARLRklrhiwQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 551 ARpslLITSEDQLARF------SDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:cd05906 120 PV---VLTDAELVAEFagletlSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 625 LWMQDRYPLSAQDVVAQKTPCSFDVSVWEF-WWPFIAGAQLVMAEPEAH-RDPQAMQQFFARYGVTTT---HFVPSMLAA 699
Cdd:cd05906 197 AGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEEIlADPLRWLDLIDRYRVTITwapNFAFALLND 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 700 FVASLDADSvAACRTLRRVFCSGEALPTELCREWERL---TGAP---LHNLYGPTEAAVDVSWYPACGPELAAVTGSSVP 773
Cdd:cd05906 277 LLEEIEDGT-WDLSSLRYLVNAGEAVVAKTIRRLLRLlepYGLPpdaIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 774 IGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVArWLTNGAVEYLG 853
Cdd:cd05906 356 LGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 854 RSDDQLKIRGQRIELGEIDRVMSGLPDVaqAVSHACVFNQAAAtGGDARQLVGYLVSDSGLPLDTAALKARLAEQL---- 929
Cdd:cd05906 429 RTKDTIIVNGVNYYSHEIEAAVEEVPGV--EPSFTAAFAVRDP-GAETEELAIFFVPEYDLQDALSETLRAIRSVVsrev 505
|
490 500 510
....*....|....*....|....*....|.
gi 635952396 930 ---PPHMVPVvlmQLAELPLSANGKLDRKAL 957
Cdd:cd05906 506 gvsPAYLIPL---PKEEIPKTSLGKIQRSKL 533
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
454-950 |
9.25e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 122.54 E-value: 9.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 454 ATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWL 533
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRLRMMLEDARPSLLIT------------------SEDQLAR--------FSDIPGLESLCYQQPLAAGDDA 587
Cdd:PRK06164 89 AVNTRYRSHEVAHILGRGRARWLVVwpgfkgidfaailaavppDALPPLRaiavvddaADATPAPAPGARVQLFALPDPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 588 PLA-----LSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGA 662
Cdd:PRK06164 169 PPAaagerAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 663 QLVMAEP-EAHRDPQAMQqffaRYGVTTTHFVPSMLAAFVASLDADsvAACRTLRRV-FCSGEALPTELCrEWERLTGAP 740
Cdd:PRK06164 249 PLVCEPVfDAARTARALR----RHRVTHTFGNDEMLRRILDTAGER--ADFPSARLFgFASFAPALGELA-ALARARGVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 741 LHNLYGPTEAAVDVSWYPACGPELAAVTGSsvpiGWPVWNTG-LRILDAAMRPV-PPGVAGDLYLTGIQLAQGYLGRPDL 818
Cdd:PRK06164 322 LTGLYGSSEVQALVALQPATDPVSVRIEGG----GRPASPEArVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNPDA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 819 TASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDV--AQAVshacvfnqAAA 896
Cdd:PRK06164 398 TARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVaaAQVV--------GAT 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 897 TGGDARQlVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELP--LSANG 950
Cdd:PRK06164 464 RDGKTVP-VAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANG 518
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
481-957 |
1.02e-28 |
|
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: 121.09 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY--PDDRLRMMLEDARpsLLIT 558
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFgpKAIEHRLRTSGAR--LVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 559 SEDQLARFSDIPGLEslcyqqplaagddaplalskpdhtayiIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDV 638
Cdd:cd05973 79 DAANRHKLDSDPFVM---------------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 639 VAqktpCSFDVSvWEFWWPFIAGAQLVMAEP----EAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRT 714
Cdd:cd05973 132 FW----NAADPG-WAYGLYYAITGPLALGHPtillEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 715 LRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPEL-AAVTGSSVPiGWPVwntglRILDAAMRPV 793
Cdd:cd05973 207 LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVhAGSAGRAMP-GWRV-----AVLDDDGDEL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 794 PPGVAG----DLYLTGIQLAQGYLGRPDLTASrfiadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELG 869
Cdd:cd05973 281 GPGEPGrlaiDIANSPLMWFRGYQLPDTPAID----------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 870 EIDRVMSGLPDVAQAvshACVFNQAAATGGDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSAN 949
Cdd:cd05973 351 DVESALIEHPAVAEA---AVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
....*...
gi 635952396 950 GKLDRKAL 957
Cdd:cd05973 428 GKIQRFLL 435
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
482-957 |
1.41e-28 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 121.28 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLrQRGVKPGDSVAVALPRS-----VFLTLALHGIVEAGAAWlpldTGYPDDrLRMMLEDARPSLL 556
Cdd:cd05909 9 TYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSaggalANFALALSGKVPVMLNY----TAGLRE-LRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 557 ITSeDQLARFSDIPGLESLCYQQPLAAGDD---------------------------APLALSKPDHTAYIIFTSGSTGR 609
Cdd:cd05909 83 LTS-KQFIEKLKLHHLFDVEYDARIVYLEDlrakiskadkckaflagkfppkwllriFGVAPVQPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 610 PKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPC--SFDVSVwEFWWPFIAGAQLVMAePEAhRDPQAMQQFFARYGV 687
Cdd:cd05909 162 PKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTG-CLWLPLLSGIKVVFH-PNP-LDYKKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 688 TTTHFVPSMLAAFVASLDADSVAacrTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSwypACGPELAAV 767
Cdd:cd05909 239 TILLGTPTFLRGYARAAHPEDFS---SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVIS---VNTPQSPNK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 768 TGSsvpIGWPVWNTGLRILD-AAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTAsrfiadpFAPGERMYRTGDVARWLTN 846
Cdd:cd05909 313 EGT---VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 847 GAVEYLGRSDDQLKIRGQRIELGEI-DRVMSGLPdvaQAVSHACVFNQAAATGgdaRQLVGYLVSDSGLPLD-TAALKAR 924
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIeDILSEILP---EDNEVAVVSVPDGRKG---EKIVLLTTTTDTDPSSlNDILKNA 456
|
490 500 510
....*....|....*....|....*....|...
gi 635952396 925 LAEQLpphMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05909 457 GISNL---AKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
456-957 |
2.20e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 124.27 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARW-QFSYREMRQQVVALAQLLRqRGVKPGDSVAVALPRSVF-----LTLALHGIVeag 529
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADSTGgELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAgalanLALLLAGKV--- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 aawlPLDTGYP--DDRLRMMLEDARPSLLITSE------------DQLARFSDIPGLESLCYQ-------QPLAAGDDAP 588
Cdd:PRK08633 692 ----PVNLNYTasEAALKSAIEQAQIKTVITSRkfleklknkgfdLELPENVKVIYLEDLKAKiskvdklTALLAARLLP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 589 LAL--------SKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPC--SFDVSVwEFWWPF 658
Cdd:PRK08633 768 ARLlkrlygptFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPL 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 659 IAGAQLVmaepeAHRDP---QAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREWER 735
Cdd:PRK08633 847 LEGIKVV-----YHPDPtdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLHP-LMFASLRLVVAGAEKLKPEVADAFEE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 736 LTGAPLHNLYGPTEAA--VDVSWYPACGPELAAVTGS---SVpiGWPVWNTGLRILDA-AMRPVPPGVAGDLYLTGIQLA 809
Cdd:PRK08633 921 KFGIRILEGYGATETSpvASVNLPDVLAADFKRQTGSkegSV--GMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQVM 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 810 QGYLGRPDLTASrFIADpfAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEI-DRVMSGLPDVAQAVsha 888
Cdd:PRK08633 999 KGYLGDPEKTAE-VIKD--IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVeEELAKALGGEEVVF--- 1072
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635952396 889 cvfnqaAATG-GDAR---QLVgylVSDSGLPLDTAALKARLAE-QLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK08633 1073 ------AVTAvPDEKkgeKLV---VLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
456-957 |
2.53e-28 |
|
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: 120.51 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL 535
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLITSeDQLARFSdipgleslcyQQPLAAgddaPLALSKPDhTAYIIFTSGSTGRPK---- 611
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIVP-DRHAGFD----------HRALAR----ELAESIPE-VALFLLSGGTTGTPKlipr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 612 -----GVMVGQTAIVNRLLwMQDRY--PLSAQDVVAQKTPCSFDVsvwefwwpFIAGAQLVMAEPEahrDPQAMQQFFAR 684
Cdd:cd05920 160 thndyAYNVRASAEVCGLD-QDTVYlaVLPAAHNFPLACPGVLGT--------LLAGGRVVLAPDP---SPDAAFPLIER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 685 YGVTTTHFVPSmlaafVASLDADSVAACR----TLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDvswYPAC 760
Cdd:cd05920 228 EGVTVTALVPA-----LVSLWLDAAASRRadlsSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLN---YTRL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 761 G--PELAAVTGssvpiGWPVW-NTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRT 837
Cdd:cd05920 300 DdpDEVIIHTQ-----GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 838 GDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVaqavshacvfnQAAATGGDARQLVG-----YLVSdS 912
Cdd:cd05920 369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAV-----------HDAAVVAMPDELLGerscaFVVL-R 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 635952396 913 GLPLDTAALKARLAEQ-LPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05920 437 DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
463-956 |
6.38e-28 |
|
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: 120.04 E-value: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 463 DQARKTPDAPALA--------DARWqfSYREMRQQVVALAQLLRQRGvKPGDSVAVALPRSVFLTLALHGIVEAG--AAW 532
Cdd:cd05931 1 RRAAARPDRPAYTflddeggrEETL--TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGaiAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 533 LPLDTGYP-DDRLRMMLEDARPSLLITSEDQLAR----FSDIPGLESL----CYQQPLAAGDDAPLALSKPDHTAYIIFT 603
Cdd:cd05931 78 LPPPTPGRhAERLAAILADAGPRVVLTTAAALAAvrafAASRPAAGTPrllvVDLLPDTSAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 604 SGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWW-PFIAGAQLVMAEPEAH-RDP----QA 677
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLtPLYSGGPSVLMSPAAFlRRPlrwlRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 678 MqqffARYGVTTThFVPSMlaAF-----------VASLDADSVAA---------CRTLRRVF---------------CSG 722
Cdd:cd05931 238 I----SRYRATIS-AAPNF--AYdlcvrrvrdedLEGLDLSSWRValngaepvrPATLRRFAeafapfgfrpeafrpSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 723 EALPTELcrewerLTGAPLHNlyGPTEAAVDVSWYPACGPELAAVTGSSVPI---GWPVWNTGLRILDAA-MRPVPPGVA 798
Cdd:cd05931 311 LAEATLF------VSGGPPGT--GPVVLRVDRDALAGRAVAVAADDPAARELvscGRPLPDQEVRIVDPEtGRELPDGEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 799 GDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARwLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGL 878
Cdd:cd05931 383 GEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 879 PDVAQAvshACVFNQAAATGGDARQLVGYLVSDSGLPLDTAALKARLAE------QLPPHMvpVVLMQLAELPLSANGKL 952
Cdd:cd05931 462 HPALRP---GCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAavarehGVAPAD--VVLVRPGSIPRTSSGKI 536
|
....
gi 635952396 953 DRKA 956
Cdd:cd05931 537 QRRA 540
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
464-957 |
8.40e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 118.91 E-value: 8.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 464 QARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDR 543
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 544 LRMMLEDARPSLLITSEDQLARFSdipGLESLCYqQPLAAGDDAPLALSKP---DHTAYIIFTSGSTGRPKGVMvgQT-- 618
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLI---PGISVKF-AELMNGPKEEAEIQEEfdlDEVATIMYTSGTTGKPKGVI--QTyg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 619 -----AIVNRL---LWMQDRY----PLsaqdvvaqktpcsFDVS--------VwefwwpfIAGAQLVMAEpeaHRDPQAM 678
Cdd:PRK03640 165 nhwwsAVGSALnlgLTEDDCWlaavPI-------------FHISglsilmrsV-------IYGMRVVLVE---KFDAEKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 679 QQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcrTLRRVFCSG--EALPT-ELCREWerltGAPLHNLYGPTEAAvdvS 755
Cdd:PRK03640 222 NKLLQTGGVTIISVVSTMLQRLLERLGEGTYPS--SFRCMLLGGgpAPKPLlEQCKEK----GIPVYQSYGMTETA---S 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WYPACGPELAAVT-GSSvpiGWPVWNTGLRILDAAmRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgerm 834
Cdd:PRK03640 293 QIVTLSPEDALTKlGSA---GKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF------ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 835 yRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDARqlVGYLVSDSgl 914
Cdd:PRK03640 363 -KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAG----VVGVPDDKWGQVP--VAFVVKSG-- 433
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 635952396 915 PLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK03640 434 EVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
450-955 |
1.47e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 119.33 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 450 VPLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAG 529
Cdd:PRK05605 27 LDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWL---PLdtgYPDDRLRMMLED--AR---------PSLLITSED-------------------QLARFSDIPGL---- 572
Cdd:PRK05605 107 AVVVehnPL---YTAHELEHPFEDhgARvaivwdkvaPTVERLRRTtpletivsvnmiaampllqRLALRLPIPALrkar 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 573 -------------ESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL----WMQDrypLSA 635
Cdd:PRK05605 184 aaltgpapgtvpwETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkaWVPG---LGD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 636 QD-VVAQKTPC--SFDVSVWEFWWPFIAGAQLVMAEPEAHRDPQAMQqffaRYGVTTTHFVPSMLAAFVASLDADSVAaC 712
Cdd:PRK05605 261 GPeRVLAALPMfhAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMK----KHPPTWLPGVPPLYEKIAEAAEERGVD-L 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 713 RTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEaavdvswypaCGPELAA--VTGSSVP--IGWPVWNTGLRILDA 788
Cdd:PRK05605 336 SGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTE----------TSPIIVGnpMSDDRRPgyVGVPFPDTEVRIVDP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 789 --AMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRI 866
Cdd:PRK05605 406 edPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 867 ELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPL 946
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAA----VVGLPREDGSE--EVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPR 552
|
....*....
gi 635952396 947 SANGKLDRK 955
Cdd:PRK05605 553 DQLGKVRRR 561
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
452-842 |
3.04e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 118.14 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 452 LPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGA 530
Cdd:PRK08314 7 LPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 531 AWLPLDTGYPDDRLRMMLEDARPSLLITSEDQL-----------------ARFSD----------------------IPG 571
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELApkvapavgnlrlrhvivAQYSDylpaepeiavpawlraepplqaLAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 572 LESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVM----VGQTAIVNRLLWMQdrypLSAQDVVAQKTPCsF 647
Cdd:PRK08314 167 GGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMhthrTVMANAVGSVLWSN----STPESVVLAVLPL-F 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 648 DVS--VWEFWWPFIAGAQLVMAePEAHRDpqAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEAL 725
Cdd:PRK08314 242 HVTgmVHSMNAPIYAGATVVLM-PRWDRE--AAARLIERYRVTHWTNIPTMVVDFLASPGLAE-RDLSSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 726 PTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAvtgssvpIGWPVWNTGLRILDAAM-RPVPPGVAGDLYLT 804
Cdd:PRK08314 318 PEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQC-------LGIPTFGVDARVIDPETlEELPPGEVGEIVVH 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 635952396 805 GIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDVAR 842
Cdd:PRK08314 391 GPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGR 425
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
471-957 |
3.93e-27 |
|
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: 116.42 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 471 APALADARWQFSYREMRQQVVALAQLLRQRGV-KPGDSVAVALPRSVFLTLALHGIVEAGA---AWLPL----DTGYPdd 542
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAiavATMPLlrpkELAYI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 543 rlrmmLEDARPSLLITSEdqlarfsdipgleslcyqqplaagddaplALSKPDHTAYIIFTSGSTGRPKGVMvgqtAIVN 622
Cdd:cd05958 79 -----LDKARITVALCAH-----------------------------ALTASDDICILAFTSGTTGAPKATM----HFHR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 623 RLLWMQDRYP-----LSAQDVVAQKTPCSFDVSV-WEFWWPFIAGAQLVMAEpeaHRDPQAMQQFFARYGVTTTHFVPSM 696
Cdd:cd05958 121 DPLASADRYAvnvlrLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFTAPTA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 697 LAAFVASLDAdSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAavdVSWYPACGPElAAVTGSSvpiGW 776
Cdd:cd05958 198 YRAMLAHPDA-AGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM---FHIFISARPG-DARPGAT---GK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 777 PVWNTGLRILDAAMRPVPPGVAGDLYLTGiqlaqgylgrPdlTASRFIADP----FAPGERMYrTGDVARWLTNGAVEYL 852
Cdd:cd05958 270 PVPGYEAKVVDDEGNPVPDGTIGRLAVRG----------P--TGCRYLADKrqrtYVQGGWNI-TGDTYSRDPDGYFRHQ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 853 GRSDDQLKIRGQRIELGEIDRVMSGLPDVAQ-AVshacvfnqaAATGGDARQLV--GYLVSDSGL---PLDTAALKARLA 926
Cdd:cd05958 337 GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEcAV---------VGHPDESRGVVvkAFVVLRPGVipgPVLARELQDHAK 407
|
490 500 510
....*....|....*....|....*....|.
gi 635952396 927 EQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05958 408 AHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
455-957 |
4.00e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.93 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 455 TTLSALVADQARKTPDAPALADAR-WQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWL 533
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRL---------RMML-----EDARPSLLITS-EDQLARFSDI-------PGLESLCYQQPLAagDDAPLAL 591
Cdd:PRK06087 103 PLLPSWREAELvwvlnkcqaKMFFaptlfKQTRPVDLILPlQNQLPQLQQIvgvdklaPATSSLSLSQIIA--DYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 592 SKP---DHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWE-FWWPFIAGAQLVMA 667
Cdd:PRK06087 181 AITthgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGARSVLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 668 EpeaHRDPQAMQQFFARYGVT----TTHFVPSMLAAfvasLDADSvAACRTLRRVFCSGEALPTELCRE-WERltGAPLH 742
Cdd:PRK06087 261 D---IFTPDACLALLEQQRCTcmlgATPFIYDLLNL----LEKQP-ADLSALRFFLCGGTTIPKKVAREcQQR--GIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 743 NLYGPTEAAVDVSWYPACGPELAAVTGssvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASR 822
Cdd:PRK06087 331 SVYGSTESSPHAVVNLDDPLSRFMHTD-----GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 823 FIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHACvfnqaaatgGDAR 902
Cdd:PRK06087 406 LDEEGW------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM---------PDER 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 903 ---QLVGYLV-SDSGLPLDTAALKARLAEQ-LPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK06087 471 lgeRSCAYVVlKAPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
598-957 |
1.99e-26 |
|
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: 111.65 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 598 AYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPcSFDVSVWEFWWP-FIAGAQLVMAEPEahrdpQ 676
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLLERN-----Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 677 AMQQFFARYGVTTTHFVPSMLAAFVASLDAdsVAACRTLRRVFCSGEALPTELCREWERLtGAPLHNLYGPTEAAVDVSW 756
Cdd:cd17630 77 ALAEDLAPPGVTHVSLVPTQLQRLLDSGQG--PAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 757 YPACGPELAAVtgssvpigwpvwntGLRILDAAMRPVPPGVagdLYLTGIQLAQGYLGRPdltasrfIADPFaPGERMYR 836
Cdd:cd17630 154 KRPDGFGRGGV--------------GVLLPGRELRIVEDGE---IWVGGASLAMGYLRGQ-------LVPEF-NEDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 837 TGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPdvaqAVSHACVFNQAAATGGdaRQLVGYLVSDSglPL 916
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHP----AVRDAFVVGVPDEELG--QRPVAVIVGRG--PA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 635952396 917 DTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd17630 281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
457-957 |
4.82e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 114.32 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 457 LSALVADQARktPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAwlPLD 536
Cdd:PRK10946 27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 537 TGYPDDRLRmMLEDAR---PSLLITSEdQLARFSDIPGLESLCYQQP-----LAAGDDAPLALSK--------------- 593
Cdd:PRK10946 103 ALFSHQRSE-LNAYASqiePALLIADR-QHALFSDDDFLNTLVAEHSslrvvLLLNDDGEHSLDDainhpaedftatpsp 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHTAYIIFTSGSTGRPK---------------GVMVGQTAIVNRLLW---MQDRYPLSaqdvvaqkTPCSFDVsvwefw 655
Cdd:PRK10946 181 ADEVAFFQLSGGSTGTPKliprthndyyysvrrSVEICGFTPQTRYLCalpAAHNYPMS--------SPGALGV------ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 656 wpFIAGAQLVMAepeahRDPQAMQQF--FARYGVTTTHFVPSMLAAFV-ASLDADSVAACRTLRRVFCSGEALPTELCRE 732
Cdd:PRK10946 247 --FLAGGTVVLA-----PDPSATLCFplIEKHQVNVTALVPPAVSLWLqAIAEGGSRAQLASLKLLQVGGARLSETLARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 733 WERLTGAPLHNLYGPTEAAVDvswYPACG-PELAAVTGSSVPIGwPvwNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQG 811
Cdd:PRK10946 320 IPAELGCQLQQVFGMAEGLVN---YTRLDdSDERIFTTQGRPMS-P--DDEVWVADADGNPLPQGEVGRLMTRGPYTFRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 812 YLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshACVF 891
Cdd:PRK10946 394 YYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHA---ALVS 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635952396 892 NQAAATGgdaRQLVGYLVSDSglPLDTAALKARLAEQ------LPPHmvpvvLMQLAELPLSANGKLDRKAL 957
Cdd:PRK10946 465 MEDELMG---EKSCAFLVVKE--PLKAVQLRRFLREQgiaefkLPDR-----VECVDSLPLTAVGKVDKKQL 526
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
457-1109 |
5.99e-26 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 115.13 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 457 LSALVADQARKT--PDAPALAdARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAG-AAWL 533
Cdd:PRK06060 6 LAGLLAEQASEAgwYDRPAFY-AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvMAFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRlRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGV 613
Cdd:PRK06060 85 ANPELHRDDH-ALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 614 MVGQTAIVNRLLWM-QDRYPLSAQDVVAQKTPCSFDVSVW-EFWWPFIAGAQLVMAEPEAHRDPQAMqqFFARYGVTTTH 691
Cdd:PRK06060 164 IHRHADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGLGnSVWFPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 692 FVPSMLAAFVASLDADSVaacRTLRRVFCSGEALPTELCrewERLT----GAPLHNLYGPTEA-------AVDvSWYPAc 760
Cdd:PRK06060 242 GVPNFFARVIDSCSPDSF---RSLRCVVSAGEALELGLA---ERLMeffgGIPILDGIGSTEVgqtfvsnRVD-EWRLG- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 761 gpelaaVTGSSVPigwPVwntGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPdltasrfiaDPFAPGERMYRTGDV 840
Cdd:PRK06060 314 ------TLGRVLP---PY---EIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 841 ARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGlpdvAQAVSHACVFNQAAATGgdARQLVGYLVSDSGLPLDTAA 920
Cdd:PRK06060 373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE----DEAVAEAAVVAVRESTG--ASTLQAFLVATSGATIDGSV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 921 LK---ARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALplptlggeRSGRPPEPGMETLVATAFSQLLGcEVNDIDA- 996
Cdd:PRK06060 447 MRdlhRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL--------RKQSPTKPIWELSLTEPGSGVRA-QRDDLSAs 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 997 DFFALGGHS---LLAMRLAAqLSRQLARQVTpgQVMVASTVGKLS----ALLAADLS------DEQ-----ARRLGLDTL 1058
Cdd:PRK06060 518 NMTIAGGNDggaTLRERLVA-LRQERQRLVV--DAVCAEAAKMLGepdpWSVDQDLAfselgfDSQmtvtlCKRLAAVTG 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 635952396 1059 LPLRESDGptlfcfhpasgfaWQF---SVLARYLSPRwsITGIQSpRPQGPMAS 1109
Cdd:PRK06060 595 LRLPETVG-------------WDYgsiSGLAQYLEAE--LAGGHG-RLKSAGPV 632
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
7-239 |
1.52e-25 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 107.05 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 7 LVAAQPGIWMAERLSTlpgAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFgEPSIID 86
Cdd:COG4908 1 LSPAQKRFLFLEPGSN---AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADL-PLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 87 LRTAPDPHRAAT--ERMQADLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGE 164
Cdd:COG4908 77 LSALPEPEREAEleELVAEEASRPFDLARG-PLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 165 ATPESPFT-PFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRL 239
Cdd:COG4908 156 PPPLPELPiQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEAL 231
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
455-957 |
1.53e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.01 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 455 TTLSALVADQARKTPDAPALADARWqfSYREMRQQVVALAQllRQRGVkpgDSVAVALPRSVFLTLALHGIVEAGAAWLP 534
Cdd:PRK07787 2 ASLNPAAVAAAADIADAVRIGGRVL--SRSDLAGAATAVAE--RVAGA---RRVAVLATPTLATVLAVVGALIAGVPVVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 LDTGYPDDRLRMMLEDARPSLLITSEDqlarfSDIPGLESLCYQqpLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVM 614
Cdd:PRK07787 75 VPPDSGVAERRHILADSGAQAWLGPAP-----DDPAGLPHVPVR--LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 615 VGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCsFDVS--VWEFWWPFIAGAQLV-MAEPeahrDPQAMQQffARYGVTTTH 691
Cdd:PRK07787 148 LSRRAIAADLDALAEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQ--ALSEGGTLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 692 F-VPSMLAAFVAslDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSwypacgpelAAVTGS 770
Cdd:PRK07787 221 FgVPTVWSRIAA--DPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLS---------TRADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 771 SVP--IGWPVWNTGLRILDAAMRPVPPGVA--GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTN 846
Cdd:PRK07787 290 RRPgwVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 847 GAVEYLGR-SDDQLKIRGQRIELGEIDRVMSGLPDVAqavshacvfnQAAATG-GDA---RQLVGYLVSDSglPLDTAAL 921
Cdd:PRK07787 364 GMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVR----------EAAVVGvPDDdlgQRIVAYVVGAD--DVAADEL 431
|
490 500 510
....*....|....*....|....*....|....*.
gi 635952396 922 KARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07787 432 IDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
456-952 |
1.77e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 112.33 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAvALPRS--VFLTLALhGIVEAGAAWL 533
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVA-ALGHNsdAYALLWL-ACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRLRMMLEDARPSLLITSEDQLAR--------FSDIPGLESLCYQQPLAAGDDAPLALSKPDHT-------- 597
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVDPALAPTaeaalallPVDTLILSLVLGGREAPGGWLDFADWAEAGSVaepdvela 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 598 ----AYIIFTSGSTGRPKGVMVGQTAIVNRLL-------WMQDRYPL-------SAQdvvaqktpcsFDVsvweFWWPFI 659
Cdd:PRK08316 170 dddlAQILYTSGTESLPKGAMLTHRALIAEYVscivagdMSADDIPLhalplyhCAQ----------LDV----FLGPYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 660 A-GAQ-LVMAEPeahrDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREW-ERL 736
Cdd:PRK08316 236 YvGATnVILDAP----DPELILRTIEAERITSFFAPPTVWISLLRHPDFDT-RDLSSLRKGYYGASIMPVEVLKELrERL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 737 TGAPLHNLYGPTEAAvdvswyP---ACGPELAAVTGSSVpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYL 813
Cdd:PRK08316 311 PGLRFYNCYGQTEIA------PlatVLGPEEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 814 GRPDLTASRFIADPFapgermyRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA----VSH-- 887
Cdd:PRK08316 383 DDPEKTAEAFRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVavigLPDpk 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635952396 888 ------ACVfnqaaatggdarqlvgylVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:PRK08316 456 wieavtAVV------------------VPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
433-957 |
2.43e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 113.13 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 433 MLSANELARLAAVNDtvVPLPA----TTLSALVADQARKTPDAPAL--------ADARWQFSYREMRQQVVALAQLLRQR 500
Cdd:PRK07529 1 MPAFATLADIEAIEA--VPLAArdlpASTYELLSRAAARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 501 GVKPGDSVAVALP---RSVFLTLA--LHGIV-----------------EAGAAWLPLDTGYPDDRLRMMLEDAR---PSL 555
Cdd:PRK07529 79 GVGPGDVVAFLLPnlpETHFALWGgeAAGIAnpinpllepeqiaellrAAGAKVLVTLGPFPGTDIWQKVAEVLaalPEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 556 LITSEDQLARFSDIPGLESLCYQQPLA-----------AGDDAPLALS----KPDHTAYIIFTSGSTGRPK------GVM 614
Cdd:PRK07529 159 RTVVEVDLARYLPGPKRLAVPLIRRKAharildfdaelARQPGDRLFSgrpiGPDDVAAYFHTGGTTGMPKlaqhthGNE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 615 VGQTAIVNRLLWMQDryplsaQDVVAQKTPCsFDV--SVWEFWWPFIAGAQLVMAEPEAHRDPQAMQQFF---ARYGVTT 689
Cdd:PRK07529 239 VANAWLGALLLGLGP------GDTVFCGLPL-FHVnaLLVTGLAPLARGAHVVLATPQGYRGPGVIANFWkivERYRINF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 690 THFVPSMLAAF----VASLDADSvaacrtLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELa 765
Cdd:PRK07529 312 LSGVPTVYAALlqvpVDGHDISS------LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERR- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 766 avTGSsvpIGWPVWNTGLRIL-----DAAMRPVPPGVAGDLYLTGIQLAQGYLgRPDLTASRFIadpfapGERMYRTGDV 840
Cdd:PRK07529 385 --IGS---VGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 841 AR-------WLTngaveylGRSDDqLKIR-GQRIELGEIDRVMSGLPDVAqavshacvfnQAAATG---GDARQL-VGYL 908
Cdd:PRK07529 453 GRidadgyfWLT-------GRAKD-LIIRgGHNIDPAAIEEALLRHPAVA----------LAAAVGrpdAHAGELpVAYV 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 635952396 909 VSDSGLPLDTAALKARLAEQLP-PHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07529 515 QLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
454-957 |
6.63e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 110.54 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 454 ATTLSALVAdqARKTPDAPAL--ADARWqfSYREMRQQVVALAQLLRQR--GVKPGdSVAVALPRSVFLTLALHGIVEAG 529
Cdd:PRK07867 4 APTVAELLL--PLAEDDDRGLyfEDSFT--SWREHIRGSAARAAALRARldPTRPP-HVGVLLDNTPEFSLLLGAAALSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPG------LESLCYQQPLA--AGDDAPLALSKPDHTAYII 601
Cdd:PRK07867 79 IVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPgvrvinVDSPAWADELAahRDAEPPFRVADPDDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 602 FTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIA-GAQLVMaepeahRDPQAMQQ 680
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAaGASIAL------RRKFSASG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 681 FFA---RYGVTTTHFVPSMLAAFVASL----DADSvaacrTLRRVFcSGEALPTELcREWERLTGAPLHNLYGPTEAAVD 753
Cdd:PRK07867 233 FLPdvrRYGATYANYVGKPLSYVLATPerpdDADN-----PLRIVY-GNEGAPGDI-ARFARRFGCVVVDGFGSTEGGVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 754 VSWYPACGPelaavtGSsvpIGWPVwnTGLRILDAAM-RPVPPGVAGDLYLTGIQLAQGYLGRPDlTASRFIA---DPFA 829
Cdd:PRK07867 306 ITRTPDTPP------GA---LGPLP--PGVAIVDPDTgTECPPAEDADGRLLNADEAIGELVNTA-GPGGFEGyynDPEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 830 PGERM----YRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarQLV 905
Cdd:PRK07867 374 DAERMrggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA----VYAVPDPVVGD--QVM 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 635952396 906 GYLVSDSGLPLDTAALKARLAEQ--LPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07867 448 AALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
456-841 |
8.51e-25 |
|
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: 110.02 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADAR--WQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWL 533
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRLRMMLEDARPSLLITS---EDQLARFS-------DIPGLESLCYQ-QPLAAGDDAPLALSKPDHTAYIIF 602
Cdd:cd05904 86 TANPLSTPAEIAKQVKDSGAKLAFTTaelAEKLASLAlpvvlldSAEFDSLSFSDlLFEADEAEPPVVVIKQDDVAALLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 603 TSGSTGRPKGVM------VGQTAIVNRLLWMQDRYPlsaqDVVAQKTP-------CSFDVSvwefwwPFIAGAQLVmaep 669
Cdd:cd05904 166 SSGTTGRSKGVMlthrnlIAMVAQFVAGEGSNSDSE----DVFLCVLPmfhiyglSSFALG------LLRLGATVV---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 670 eahrdpqAMQQFFA--------RYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCREW-ERLTGAP 740
Cdd:cd05904 232 -------VMPRFDLeellaaieRYKVTHLPVVPPIVLALVKSPIVDKYDL-SSLRQIMSGAAPLGKELIEAFrAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 741 LHNLYGPTEA-AVDVSWYPACgpELAAVTGSSvpiGWPVWNTGLRILDAAM-RPVPPGVAGDLYLTGIQLAQGYLGRPDL 818
Cdd:cd05904 304 LGQGYGMTEStGVVAMCFAPE--KDRAKYGSV---GRLVPNVEAKIVDPETgESLPPNQTGELWIRGPSIMKGYLNNPEA 378
|
410 420
....*....|....*....|...
gi 635952396 819 TASRFIADPFapgermYRTGDVA 841
Cdd:cd05904 379 TAATIDKEGW------LHTGDLC 395
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
481-884 |
2.21e-24 |
|
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: 109.71 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALP---RSVFLTLA------LHGIVEAGAAWLPLDTgypddrlrmMLEDA 551
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPmipEAAIAMLAcarigaIHSVVFGGFAAKELAS---------RIDDA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 552 RPSLLITSE---------------DQLARFSDIPGLESLCYQQPLAAGD----------DAPLALSKP--------DHTA 598
Cdd:cd05967 154 KPKLIVTAScgiepgkvvpykpllDKALELSGHKPHHVLVLNRPQVPADltkpgrdldwSELLAKAEPvdcvpvaaTDPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 599 YIIFTSGSTGRPKGVM--VGQTAIVnrLLW-MQDRYPLSAQDVvaqktpcsfdvsvwefWW-----------------PF 658
Cdd:cd05967 234 YILYTSGTTGKPKGVVrdNGGHAVA--LNWsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 659 IAGAQLVMAE--PEAHRDPQAMQQFFARYGVTTTHFVPSMLAAF-VASLDADSVAAC--RTLRRVFCSGEAL--PTelcR 731
Cdd:cd05967 296 LHGATTVLYEgkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrKEDPDGKYIKKYdlSSLRTLFLAGERLdpPT---L 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 732 EW-ERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTGSSvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGiQLAQ 810
Cdd:cd05967 373 EWaENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSP---GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPP 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 811 GYLGRPDLTASRFIADPFA--PGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:cd05967 449 GCLLTLWKNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC 522
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
456-953 |
3.67e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 108.43 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL 535
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPDDRLRMMLEDARPSLLITSEDQLARFSDI----PGLESLC----------------YQQPLAAGDDAPLAL--SK 593
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVlprlPKLRTLVvvedgsgndllpgavdYEDALAAGSPERDFGerSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHtaYIIFTSGSTGRPKGVMVGQTAIVNRLL----WMQDRYPLSAQDVVAQKTPCS----FDVSvwefwwPFIAGA--- 662
Cdd:PRK07798 164 DDL--YLLYTGGTTGMPKGVMWRQEDIFRVLLggrdFATGEPIEDEEELAKRAAAGPgmrrFPAP------PLMHGAgqw 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 663 ---------QLVMAEPEAHRDPQAMQQFFARYGVTTTHFV-PSMLAAFVASLDADSVAACRTLRRVFCSGEALPTELCRE 732
Cdd:PRK07798 236 aafaalfsgQTVVLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYDLSSLFAIASGGALFSPSVKEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 733 W-ERLTGAPLHNLYGPTEAAvdvswypACGpeLAAVTGSSVPIGWPVWNTGLR--ILDAAMRPVPPG--VAGDLYLTGiQ 807
Cdd:PRK07798 316 LlELLPNVVLTDSIGSSETG-------FGG--SGTVAKGAVHTGGPRFTIGPRtvVLDEDGNPVEPGsgEIGWIARRG-H 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 808 LAQGYLGRPDLTASRFiadPFAPGERMYRTGDVARWLTNGAVEYLGRsdDQLKIR--GQRIELGEIDRVMSGLPDVAQAV 885
Cdd:PRK07798 386 IPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADAL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 886 shacVFNQAAATGGdarQLVGYLVS-DSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLD 953
Cdd:PRK07798 461 ----VVGVPDERWG---QEVVAVVQlREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
459-965 |
1.13e-23 |
|
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: 107.58 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 459 ALVADQARKTPDAPALadaRWQ--------FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGA 530
Cdd:cd05968 65 QLLDKWLADTRTRPAL---RWEgedgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 531 AWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDI---PGLESLCYQQP--------------------------- 580
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVnlkEEADKACAQCPtvekvvvvrhlgndftpakgrdlsyde 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 581 LAAGDDAPLALSKPDHTAYIIFTSGSTGRPKG---VMVGqtaivnrllwmqdrYPLSAqdvvAQKTPCSFDVSVWE--FW 655
Cdd:cd05968 222 EKETAGDGAERTESEDPLMIIYTSGTTGKPKGtvhVHAG--------------FPLKA----AQDMYFQFDLKPGDllTW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 656 -----W---PF------IAGAQLVMAE--PEaHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRTLRRVF 719
Cdd:cd05968 284 ftdlgWmmgPWlifgglILGATMVLYDgaPD-HPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 720 CS-GEALPTELCREWERLTG---APLHNLYGPTEAAvdvswypacGPELAAVTGSSV-PIGW--PVWNTGLRILDAAMRP 792
Cdd:cd05968 363 GStGEPWNPEPWNWLFETVGkgrNPIINYSGGTEIS---------GGILGNVLIKPIkPSSFngPVPGMKADVLDESGKP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 793 VPPGVaGDLYLTG--IQLAQGYLGRPDltasRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGE 870
Cdd:cd05968 434 ARPEV-GELVLLApwPGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAE 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 871 IDRVMSGLPDVAQAvshACVFNQAAATGgdaRQLVGYLVSDSGLPlDTAALKARLAEQLPPHM----VPVVLMQLAELPL 946
Cdd:cd05968 509 IESVLNAHPAVLES---AAIGVPHPVKG---EAIVCFVVLKPGVT-PTEALAEELMERVADELgkplSPERILFVKDLPK 581
|
570
....*....|....*....
gi 635952396 947 SANGKLDRKALPLPTLGGE 965
Cdd:cd05968 582 TRNAKVMRRVIRAAYLGKE 600
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
451-957 |
1.71e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 106.64 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 451 PLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGA 530
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 531 AWLPLDTGYPDDRLRMMLEDARPSLLI-------TSEDQLARFS----------DIPGLESLC----------------- 576
Cdd:PRK07059 99 VVVNVNPLYTPRELEHQLKDSGAEAIVvlenfatTVQQVLAKTAvkhvvvasmgDLLGFKGHIvnfvvrrvkkmvpawsl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 577 -----YQQPLAAGddAPLALSK----PDHTAYIIFTSGSTGRPKGVMVGQTAIV-NRL---LWMQ---DRYPLSAQDVVA 640
Cdd:PRK07059 179 pghvrFNDALAEG--ARQTFKPvklgPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqmeAWLQpafEKKPRPDQLNFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 641 QKTPCS--FDVSVWEFWWPFIAGAQLVMAEPeahRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAaCRTLRRV 718
Cdd:PRK07059 257 CALPLYhiFALTVCGLLGMRTGGRNILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLD-FSKLIVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 719 FCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELaavTGSsvpIGWPVWNTGLRILDAAMRPVPPGVA 798
Cdd:PRK07059 333 NGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEF---SGT---IGLPLPSTEVSIRDDDGNDLPLGEP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 799 GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVmsgl 878
Cdd:PRK07059 407 GEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEV---- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 879 pdvaqAVSHACVFNQAAATGGDAR--QLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKA 956
Cdd:PRK07059 477 -----VASHPGVLEVAAVGVPDEHsgEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRE 551
|
.
gi 635952396 957 L 957
Cdd:PRK07059 552 L 552
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
479-944 |
1.76e-23 |
|
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: 105.37 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 479 WQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLdtgYPD---DRLRMMLEDARPS 554
Cdd:cd05907 3 WQpITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI---YPTssaEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 555 LLITSedqlarfsdipgleslcyqqplaagddaplalsKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLS 634
Cdd:cd05907 80 ALFVE---------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 635 AQDVVAQKTPCS--FDVSVWEfWWPFIAGAQLVMAEPeahrdPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAC 712
Cdd:cd05907 127 EGDRHLSFLPLAhvFERRAGL-YVPLLAGARIYFASS-----AETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 713 R----------TLRRVFCSGEALPTELCREWERLtGAPLHNLYGPTE--AAVdvswypACGPELAAVTGSsvpIGWPVWN 780
Cdd:cd05907 201 KrklfdlavggRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTEtsAVV------TLNPPGDNRIGT---VGKPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 781 TGLRIldaamrpvppGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLK 860
Cdd:cd05907 271 VEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLII 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 861 IR-GQRIELGEIDRVMSGLPdvaqAVSHACVFnqaaatgGDARQLVGYLVSdsglpLDTAALKARLAEQLPPHMVPVVLM 939
Cdd:cd05907 335 TSgGKNISPEPIENALKASP----LISQAVVI-------GDGRPFLVALIV-----PDPEALEAWAEEHGIAYTDVAELA 398
|
....*
gi 635952396 940 QLAEL 944
Cdd:cd05907 399 ANPAV 403
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
482-957 |
1.20e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 103.62 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSED 561
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 562 QLARFSDI--PGLESLCYQQP---LAA-GDDAPLALSKPDHTAY--------------------IIFTSGSTGRPKGV-- 613
Cdd:PRK12406 93 LLHGLASAlpAGVTVLSVPTPpeiAAAyRISPALLTPPAGAIDWegwlaqqepydgppvpqpqsMIYTSGTTGHPKGVrr 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 614 ---MVGQTAIvnrllWMQDR---YPLsAQDVVAQKT-------PCSFDVSVWEFwwpfiaGAQLVMaepEAHRDPQAMQQ 680
Cdd:PRK12406 173 aapTPEQAAA-----AEQMRaliYGL-KPGIRALLTgplyhsaPNAYGLRAGRL------GGVLVL---QPRFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 681 FFARYGVTTTHFVPSMlaaFVASLD-ADSVAA---CRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVdVSW 756
Cdd:PRK12406 238 LIERHRITHMHMVPTM---FIRLLKlPEEVRAkydVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGA-VTF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 757 ypaCGPELAAVTGSSVPIGWPvwNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQ-GYLGRPDLTAS----RFIAdpfapg 831
Cdd:PRK12406 314 ---ATSEDALSHPGTVGKAAP--GAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFIT------ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 832 ermyrTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVaqavsHAC-VFNQAAATGGDArqLVGYLVS 910
Cdd:PRK12406 383 -----SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGV-----HDCaVFGIPDAEFGEA--LMAVVEP 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 635952396 911 DSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK12406 451 QPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
456-957 |
1.53e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 103.22 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPAL------ADARwQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAG 529
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALifessgGVVR-RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWLPLDTGYPDDRLRMMLEDARPSLLITSE------DQLARFSDIP------------------GLESLCYQQPLAAGD 585
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAqfypmyRQIQQEDATPlrhicltrvalpaddgvsSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 586 DAPLAlskPDHTAYIIFTSGSTGRPKGVMVG-------------QTAivnrlLWMQDRY--PLSAQDVVAQktpCSFDVS 650
Cdd:PRK08008 167 APPLS---TDDTAEILFTSGTTSRPKGVVIThynlrfagyysawQCA-----LRDDDVYltVMPAFHIDCQ---CTAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 651 VwefwwpFIAGAQLVMAEPEAHRdpqAMQQFFARYGVTTTHFVPSMLAAFVAS-LDADSVAACrtLRRVFCSgEALPTEL 729
Cdd:PRK08008 236 A------FSAGATFVLLEKYSAR---AFWGQVCKYRATITECIPMMIRTLMVQpPSANDRQHC--LREVMFY-LNLSDQE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 730 CREWERLTGAPLHNLYGPTEAAV--------DVSWYPAcgpelaavtgssvpIGWPVWNTGLRILDAAMRPVPPGVAGDL 801
Cdd:PRK08008 304 KDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWPS--------------IGRPGFCYEAEIRDDHNRPLPAGEIGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 802 YLTGI---QLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGL 878
Cdd:PRK08008 370 CIKGVpgkTIFKEYYLDPKATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 879 PDVAQAVshacVFNQAAATGGDArqLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK08008 444 PKIQDIV----VVGIKDSIRDEA--IKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
480-885 |
3.21e-22 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 101.67 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS 559
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 EDqlarfsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVV 639
Cdd:cd17640 85 ND--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 640 AQKTPC--SFDVSVWEFWwpFIAGAQlvmaepEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRTLRR 717
Cdd:cd17640 133 LSILPIwhSYERSAEYFI--FACGCS------QAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 718 VF-------------CSGEALPTELCREWErLTGAPLHNLYGPTEAAVDVSwypaCGPELAAVTGSsvpIGWPVWNTGLR 784
Cdd:cd17640 205 LFlfflsggifkfgiSGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVS----ARRLKCNVRGS---VGRPLPGTEIK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 785 ILDAAMR-PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIR- 862
Cdd:cd17640 277 IVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTIVLSn 350
|
410 420
....*....|....*....|...
gi 635952396 863 GQRIELGEIDRVMSGLPDVAQAV 885
Cdd:cd17640 351 GENVEPQPIEEALMRSPFIEQIM 373
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
594-957 |
3.36e-22 |
|
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: 99.86 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHTAYIIFTSGSTGRPK------GVMVGQTAIVNRLLWMQDRyplsaqDVVAQKTPCsFDV--SVWEFWWPFIAGAQLV 665
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKlaqhthSNEVYNAWMLALNSLFDPD------DVLLCGLPL-FHVngSVVTLLTPLASGAHVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 666 MAEPEAHRDPQAMQQFF---ARYGVTTTHFVPSMLAAFVA-SLDADsvaaCRTLRRVFCSGEALPTELCREWERLTGAPL 741
Cdd:cd05944 74 LAGPAGYRNPGLFDNFWklvERYRITSLSTVPTVYAALLQvPVNAD----ISSLRFAMSGAAPLPVELRARFEDATGLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 742 HNLYGPTEAAVDVSWYPACGPELAAvtgsSVPIGWPVWNTGLRILDA---AMRPVPPGVAGDLYLTGIQLAQGYLgRPDL 818
Cdd:cd05944 150 VEGYGLTEATCLVAVNPPDGPKRPG----SVGLRLPYARVRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYL-YTEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 819 TASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDqLKIR-GQRIELGEIDRVMSGLPdvaqAVSHACVFNQAAAT 897
Cdd:cd05944 225 NKNAFVADGW------LNTGDLGRLDADGYLFITGRAKD-LIIRgGHNIDPALIEEALLRHP----AVAFAGAVGQPDAH 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635952396 898 GGDARqlVGYLVSDSGLPLDTAALKARLAEQLPPH-MVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05944 294 AGELP--VAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
450-957 |
3.64e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 102.61 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 450 VPLPA----TTLSALVADQARktPDAPALADARWQF--SYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLAL 522
Cdd:PLN02574 32 VPLPSdpnlDAVSFIFSHHNH--NGDTALIDSSTGFsiSYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 523 HGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLAR----------------FSDIPGLESLCYQQPLAAGDD 586
Cdd:PLN02574 110 LAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKlsplgvpvigvpenydFDSKRIEFPKFYELIKEDFDF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 587 APLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVN------RLLWMQDRYPLSAQDVVAQKTPCS-FDVSVWEFWWPFI 659
Cdd:PLN02574 190 VPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAmvelfvRFEASQYEYPGSDNVYLAALPMFHiYGLSLFVVGLLSL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 660 AGAQLVMAEpeahRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRTLRRVFCSGEALPTELCREW-ERLTG 738
Cdd:PLN02574 270 GSTIVVMRR----FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPH 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 739 APLHNLYGPTE-AAVDVSWYPACGPELAAVTGSSVPigwpvwNTGLRILD-AAMRPVPPGVAGDLYLTGIQLAQGYLGRP 816
Cdd:PLN02574 346 VDFIQGYGMTEsTAVGTRGFNTEKLSKYSSVGLLAP------NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 817 DLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMsglpdvaqaVSHACVFNQAAA 896
Cdd:PLN02574 420 KATQSTIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVL---------ISHPEIIDAAVT 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 897 TGGD---ARQLVGYLVSDSGLPLDTAALKARLAEQLPPH--MVPVVLMQlaELPLSANGKLDRKAL 957
Cdd:PLN02574 485 AVPDkecGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYkkVRKVVFVQ--SIPKSPAGKILRREL 548
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
454-957 |
4.03e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 102.04 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 454 ATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWL 533
Cdd:PRK07470 6 VMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTGYPDDRLRMMLEDARPSLLI--------------TSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHT-- 597
Cdd:PRK07470 86 PTNFRQTPDEVAYLAEASGARAMIchadfpehaaavraASPDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDdp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 598 AYIIFTSGSTGRPKGVMV--GQTAIV--NRLL-WMQDRYPLSAQDVVAqktPCSFDVSVWEFwWPFIAGAQLVMAePEAH 672
Cdd:PRK07470 166 CWFFFTSGTTGRPKAAVLthGQMAFVitNHLAdLMPGTTEQDASLVVA---PLSHGAGIHQL-CQVARGAATVLL-PSER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 673 RDPQAMQQFFARYGVTTTHFVPSMLAAFVASldaDSVAAC--RTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEA 750
Cdd:PRK07470 241 FDPAEVWALVERHRVTNLFTVPTILKMLVEH---PAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 751 AVDVSWYPACGPELAAVTGSSV-PIGWPvwNTG--LRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP 827
Cdd:PRK07470 318 TGNITVLPPALHDAEDGPDARIgTCGFE--RTGmeVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGW 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 828 FapgermyRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPdvaqAVSHACVFNQAAATGGDARqlVGY 907
Cdd:PRK07470 396 F-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP----AVSEVAVLGVPDPVWGEVG--VAV 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 635952396 908 LVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07470 463 CVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
465-957 |
8.57e-22 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 101.03 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALA---DA--RWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV---FLTLALHGI----VEAGAAW 532
Cdd:cd05970 27 AKEYPDKLALVwcdDAgeERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYefwYSLLALHKLgaiaIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 533 LPLDTGYPDDR--LRMML-----------EDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGD-DAPLALSKP--DH 596
Cdd:cd05970 107 TAKDIVYRIESadIKMIVaiaednipeeiEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDfERPTANSYPcgED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 597 TAYIIFTSGSTGRPKGVMVGQT----AIVNRLLWmQDRYPLSAQDVVAQKtpcSFDVSVW-EFWWPFIAGAQLVMAEPEA 671
Cdd:cd05970 187 ILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYW-QNVREGGLHLTVADT---GWGKAVWgKIYGQWIAGAAVFVYDYDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 672 HrDPQAMQQFFARYGVTTTHFVPS----MLAAFVASLDADSVAACRTlrrvfcSGEALPTELCREWERLTGAPLHNLYGP 747
Cdd:cd05970 263 F-DPKALLEKLSKYGVTTFCAPPTiyrfLIREDLSRYDLSSLRYCTT------AGEALNPEVFNTFKEKTGIKLMEGFGQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 748 TEAAVDVSWYPACGPElaavTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYL-----TGIQLAQGYLGRPDLTASR 822
Cdd:cd05970 336 TETTLTIATFPWMEPK----PGS---MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgKPVGLFGGYYKDAEKTAEV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 823 FiadpfapGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMsglpdvaqaVSHACVFnQAAATGgdar 902
Cdd:cd05970 409 W-------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL---------IQHPAVL-ECAVTG---- 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 903 qlvgylVSDsglPLDTAALKARL--------AEQL------------PPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05970 468 ------VPD---PIRGQVVKATIvlakgyepSEELkkelqdhvkkvtAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
482-957 |
2.66e-21 |
|
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: 98.19 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLlitsed 561
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 562 qlarfsdipgleslcyqqplaagddaplalskpDHTAYIIFTSGSTGRPKGVMvgQT-------AIVNRL---LWMQDRY 631
Cdd:cd05912 77 ---------------------------------DDIATIMYTSGTTGKPKGVQ--QTfgnhwwsAIGSALnlgLTEDDNW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 632 pLSAQDVvaqktpcsFDVSvwefwwpfiaGAQLVM--------AEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVAS 703
Cdd:cd05912 122 -LCALPL--------FHIS----------GLSILMrsviygmtVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 704 LDADSVAacrTLRRVFCSGEALPT---ELCREwerlTGAPLHNLYGPTEAAvdvSWYPACGPELAAVTGSSVpiGWPVWN 780
Cdd:cd05912 183 LGEGYPN---NLRCILLGGGPAPKpllEQCKE----KGIPVYQSYGMTETC---SQIVTLSPEDALNKIGSA--GKPLFP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 781 TGLRILDAAmrpVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVARWLTNGAVEYLGRSDDQLK 860
Cdd:cd05912 251 VELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLII 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 861 IRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdarQL-VGYLVSDSglPLDTAALKARLAEQLPPHMVPVVLM 939
Cdd:cd05912 321 SGGENIYPAEIEEVLLSHPAIKEAG----VVGIPDDKWG---QVpVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIY 391
|
490
....*....|....*...
gi 635952396 940 QLAELPLSANGKLDRKAL 957
Cdd:cd05912 392 FVDELPRTASGKLLRHEL 409
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
455-958 |
4.58e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.53 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 455 TTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLP 534
Cdd:PRK13383 35 TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 LDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPglESLCYQQPLAAGDDAPLALSKPDHTAYIIF-TSGSTGRPKGV 613
Cdd:PRK13383 115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGAD--DAVAVIDPATAGAEESGGRPAVAAPGRIVLlTSGTTGKPKGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 614 MVGQTAIVNRLLWMQ--DRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMaepEAHRDPQAMQQFFARYGVTTTH 691
Cdd:PRK13383 193 PRAPQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLT---HRHFDAEAALAQASLHRADAFT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 692 FVPSMLAAFvasLDADSVAACRT----LRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPAcgpelaAV 767
Cdd:PRK13383 270 AVPVVLARI---LELPPRVRARNplpqLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPA------DL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 768 TGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGrpdlTASRFIADPfapgerMYRTGDVARWLTNG 847
Cdd:PRK13383 341 RDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDG------MTSTGDMGYLDNAG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 848 AVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdaRQLVGYLVSDSGLPLDTAALKARLAE 927
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA----VIGVPDERFG--HRLAAFVVLHPGSGVDAAQLRDYLKD 484
|
490 500 510
....*....|....*....|....*....|.
gi 635952396 928 QLPPHMVPVVLMQLAELPLSANGKLDRKALP 958
Cdd:PRK13383 485 RVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
452-957 |
7.57e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.03 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 452 LPATTLSALVAD----QARKTPDAPAL--ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGI 525
Cdd:PRK05852 9 PMASDFGPRIADlvevAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 526 VEAGAAWLPLDTGYP--DDRLRMMLEDARPSLL---------------------ITSEDQLARFSDIPGLESLCYQQPLA 582
Cdd:PRK05852 89 SRADLVVVPLDPALPiaEQRVRSQAAGARVVLIdadgphdraepttrwwpltvnVGGDSGPSGGTLSVHLDAATEPTPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 583 AgddAPLALSKPDhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGA 662
Cdd:PRK05852 169 S---TPEGLRPDD--AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 663 QLVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACR-TLRRVFCSGEALPTELCREWERLTGAPL 741
Cdd:PRK05852 244 GAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPaALRFIRSCSAPLTAETAQALQTEFAAPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 742 HNLYGPTEAAVDVSWYPACGPELAAVTGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTAS 821
Cdd:PRK05852 324 VCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 822 RFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFnqaaatgGDA 901
Cdd:PRK05852 404 NFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAA----VF-------GVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635952396 902 RQLVGYLVSDSGLPLDTAA-----LKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK05852 466 DQLYGEAVAAVIVPRESAPptaeeLVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
463-957 |
1.06e-20 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 97.54 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 463 DQARKTPDAPAL-------ADARWqfSYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLP 534
Cdd:cd05928 19 EKAGKRPPNPALwwvngkgDEVKW--SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 LDTGYPDDRLRMMLEDARPSLLITSeDQLARFSDIPGLESLCYQQPLAAGD---DAPLALSK------PDHTAY------ 599
Cdd:cd05928 97 GTIQLTAKDILYRLQASKAKCIVTS-DELAPEVDSVASECPSLKTKLLVSEksrDGWLNFKEllneasTEHHCVetgsqe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 ---IIFTSGSTGRPKGV-----MVGQTAIVNRLLWMQdrypLSAQDVVAQKTPCSFDVSVW-EFWWPFIAGAqLVMAEPE 670
Cdd:cd05928 176 pmaIYFTSGTTGSPKMAehshsSLGLGLKVNGRYWLD----LTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 671 AHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASlDADSVAAcRTLRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEA 750
Cdd:cd05928 251 PRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKF-PSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTET 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 751 AVdvswypACG-PELAAVTGSSVPIGWPVWNtgLRILDAAMRPVPPGVAGDLyltGIQLA--------QGYLGRPDLTAS 821
Cdd:cd05928 329 GL------ICAnFKGMKIKPGSMGKASPPYD--VQIIDDNGNVLPPGTEGDI---GIRVKpirpfglfSGYVDNPEKTAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 822 RFIADpfapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA------------VSHAC 889
Cdd:cd05928 398 TIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESavvsspdpirgeVVKAF 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 890 VFNQAAATGGDARQLvgylvsdsglpldTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05928 471 VVLAPQFLSHDPEQL-------------TKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
452-1047 |
1.59e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.09 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 452 LPATTLSALvADQARKTPDAPAL------ADARWQFSYREMRQQVVALAQLLRQRGVkPGDSVAVALPRSVFLTLALHGI 525
Cdd:PRK05691 7 LPLTLVQAL-QRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 526 VEAGAAWLPldtGYP--------DDRLRMMLEDARPSLLITSED--------QLARFSDIPGLesLCYQQ---PLAAGDD 586
Cdd:PRK05691 85 LYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADlrdsllqmEELAAANAPEL--LCVDTldpALAEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 587 APlALsKPDHTAYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQD-RYPLSAQDVVAQKTPCSFDVS-VWEFWWPFIAGAQ 663
Cdd:PRK05691 160 EP-AL-QPDDIAFLQYTSGSTALPKGVQVSHGNLVaNEQLIRHGfGIDLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 664 LVMAEPEAHRD-PQAMQQFFARYGVTTT---HFVPSMLAAFVA-------------------------SLD--ADSVAAC 712
Cdd:PRK05691 238 CVLMSPAYFLErPLRWLEAISEYGGTISggpDFAYRLCSERVSesalerldlsrwrvaysgsepirqdSLErfAEKFAAC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 713 RTLRRVF--CSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSwyPACGPELaavtgssVPIGWPVWNTGLRILDAAM 790
Cdd:PRK05691 318 GFDPDSFfaSYGLAEATLFVSGGRRGQGIPALELDAEALARNRAE--PGTGSVL-------MSCGRSQPGHAVLIVDPQS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 791 RPV-PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDVArWLTNGAVEYLGRSDDQLKIRGQRIELG 869
Cdd:PRK05691 389 LEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 870 EIDRVMSGLPDVAQAVSHAcvfnqAAATGGDARQLVGYLVSDS-----GLPLDT--AALKARLAEQLPPHMVPVVLMQLA 942
Cdd:PRK05691 465 DIEKTVEREVEVVRKGRVA-----AFAVNHQGEEGIGIAAEISrsvqkILPPQAliKSIRQAVAEACQEAPSVVLLLNPG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 943 ELPLSANGKLDRKALPL-------------PTLGGERSGRPPEPG--METLVATAFSQLLGCEVNDIDADFFALGGHSLL 1007
Cdd:PRK05691 540 ALPKTSSGKLQRSACRLrladgsldsyalfPALQAVEAAQTAASGdeLQARIAAIWCEQLKVEQVAADDHFFLLGGNSIA 619
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 635952396 1008 AMRLAAQLSRQLARQVTPGQVMVASTVGKLSALLAADLSD 1047
Cdd:PRK05691 620 ATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAG 659
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
481-957 |
3.10e-20 |
|
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: 95.33 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRmmledarpsllitse 560
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLR--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 DQLARfsdipGLESLCYQQPLAAGDDaPLALskpdhtayiIFTSGSTGRPKGVMVGQTAI----VNRLLWMQdrypLSAQ 636
Cdd:cd05974 66 DRVDR-----GGAVYAAVDENTHADD-PMLL---------YFTSGTTSKPKLVEHTHRSYpvghLSTMYWIG----LKPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 637 DVVAQKTPCSFDVSVWE-FWWPFIAGAQlVMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVaslDADSVAACRTL 715
Cdd:cd05974 127 DVHWNISSPGWAKHAWScFFAPWNAGAT-VFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLI---QQDLASFDVKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 716 RRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPAcgpeLAAVTGSsvpIGWPVWNTGLRILDAAMRPVPP 795
Cdd:cd05974 203 REVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPG----QPVKAGS---MGRPLPGYRVALLDPDGAPATE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 796 G-VAGDLYLT-GIQLAQGYLGRPDLTASrfiadpfAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDR 873
Cdd:cd05974 276 GeVALDLGDTrPVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 874 VMSGLPDVAQAvshacvfnqAAATGGDARQLV---GYLVSDSGL---PLDTAALKARLAEQLPPHMvPVVLMQLAELPLS 947
Cdd:cd05974 349 VLIEHPAVAEA---------AVVPSPDPVRLSvpkAFIVLRAGYepsPETALEIFRFSRERLAPYK-RIRRLEFAELPKT 418
|
490
....*....|
gi 635952396 948 ANGKLDRKAL 957
Cdd:cd05974 419 ISGKIRRVEL 428
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
466-951 |
5.26e-20 |
|
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: 95.80 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 466 RKTPDAPALADA----RWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRS---VFLTLALHGIveaGAAWL---Pl 535
Cdd:cd05943 80 ADADDPAAIYAAedgeRTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIpeaVVAMLATASI---GAIWSscsP- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGYPD--DRLRMMledaRPSLLITSE---------DQLARFSDI-PGLESL----------CYQQP------------- 580
Cdd:cd05943 156 DFGVPGvlDRFGQI----EPKVLFAVDaytyngkrhDVREKVAELvKGLPSLlavvvvpytvAAGQPdlskiakaltled 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 581 -LAAGDDAPLALSKP--DHTAYIIFTSGSTGRPKGVMVGQTAIV------NRLLWmqdryPLSAQDVVAQKTPCSfdvsv 651
Cdd:cd05943 232 fLATGAAGELEFEPLpfDHPLYILYSSGTTGLPKCIVHGAGGTLlqhlkeHILHC-----DLRPGDRLFYYTTCG----- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 652 WEFWWPFIA----GAQLVMA-EPEAHRDPQAMQQFFARYGVTttHFVPSmlAAFVASLDADSVAACRT-----LRRVFCS 721
Cdd:cd05943 302 WMMWNWLVSglavGATIVLYdGSPFYPDTNALWDLADEEGIT--VFGTS--AKYLDALEKAGLKPAEThdlssLRTILST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 722 GEALPTElCREW---ERLTGAPLHNLYGPTEAavdVSWYPACGPELAAVTGssvPIGWPVWNTGLRILDAAMRPVPpGVA 798
Cdd:cd05943 378 GSPLKPE-SFDYvydHIKPDVLLASISGGTDI---ISCFVGGNPLLPVYRG---EIQCRGLGMAVEAFDEEGKPVW-GEK 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 799 GDLYLTGIQLAQ--GYLGRPDltASRFIADPFA--PGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRV 874
Cdd:cd05943 450 GELVCTKPFPSMpvGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRV 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 875 MSGLPDVAQAVshaCVFNQAAatGGDARqLVGYLVSDSGLPLDTA---ALKARLAEQLPPHMVPVVLMQLAELPLSANGK 951
Cdd:cd05943 526 VEKIPEVEDSL---VVGQEWK--DGDER-VILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
447-954 |
5.68e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 95.61 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 447 DTVVPLPATTLSALVADQARKTPDAPALA----DARWqfSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLAL 522
Cdd:PRK12583 10 GGDKPLLTQTIGDAFDATVARFPDREALVvrhqALRY--TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 523 HGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLIT-----SEDQLARFSDI-PGLES---------------------- 574
Cdd:PRK12583 88 FATARIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELlPGLAEgqpgalacerlpelrgvvslap 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 575 ------LCYQQPLAAGD-------DAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQ 641
Cdd:PRK12583 168 apppgfLAWHELQARGEtvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 642 KTPcsfdvsvweFWWPF----------IAGAQLVMaePEAHRDPQAMQQFFARYGVTTTHFVPSMlaaFVASLDADSVAA 711
Cdd:PRK12583 248 PVP---------LYHCFgmvlanlgcmTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTM---FIAELDHPQRGN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 712 --CRTLRRVFCSGEALPTELCRE-WERLTGAPLHNLYGPTEAAvdvswypacgpELAAVTGSSVPIGWPVWNTG------ 782
Cdd:PRK12583 314 fdLSSLRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTETS-----------PVSLQTTAADDLERRVETVGrtqphl 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 783 -LRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgerMYrTGDVARWLTNGAVEYLGRSDDQLKI 861
Cdd:PRK12583 383 eVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 862 RGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQL 941
Cdd:PRK12583 457 GGENIYPREIEEFLFTHPAVADVQ----VFGVPDEKYGE--EIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFV 530
|
570
....*....|...
gi 635952396 942 AELPLSANGKLDR 954
Cdd:PRK12583 531 DEFPMTVTGKVQK 543
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
597-954 |
1.08e-19 |
|
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: 91.94 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 597 TAYIIFTSGSTGRPKGVMVG-QTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMAepeahRDP 675
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLAnKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG-----GEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 676 QAMQQFFAR---YGVTTTHFVPSMLAAFVaSLDADSVAACRTLRRVFCSGEALPTELCR--EWERLTGAPLHnlYGPTE- 749
Cdd:cd17635 78 TTYKSLFKIlttNAVTTTCLVPTLLSKLV-SELKSANATVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQV--YGLSEt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 750 AAVDVSWYPACGPELAAVtgssvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA 829
Cdd:cd17635 155 GTALCLPTDDDSIEINAV-------GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 830 PGERMYRTGDVARWLTngaveylGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshACvfnqAAATGGDARQLVGYLV 909
Cdd:cd17635 228 TGDLGERREDGFLFIT-------GRSSESINCGGVKIAPDEVERIAEGVSGVQEC---AC----YEISDEEFGELVGLAV 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 635952396 910 SDSGLPLDTA--ALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDR 954
Cdd:cd17635 294 VASAELDENAirALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
594-954 |
1.40e-19 |
|
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: 91.96 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTP---CsFDVSVwefwwPFIA----GAQLVM 666
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPlfhC-FGSVL-----GVLAclthGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 667 aePEAHRDPQAMQQFFARYGVTTTHFVPSMlaaFVASLDADSVAA--CRTLRRVFCSGEALPTELCRE-WERLTGAPLHN 743
Cdd:cd05917 75 --PSPSFDPLAVLEAIEKEKCTALHGVPTM---FIAELEHPDFDKfdLSSLRTGIMAGAPCPPELMKRvIEVMNMKDVTI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 744 LYGPTEAAvdvswyPACgpeLAAVTGSSVP-----IGWPVWNTGLRILDAAMRPVPP-GVAGDLYLTGIQLAQGYLGRPD 817
Cdd:cd05917 150 AYGMTETS------PVS---TQTRTDDSIEkrvntVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 818 LTASRfiadpfAPGERMYRTGDVARWLTNGAVEYLGRSDDQLkIRG-QRIELGEIDRVMSGLPDVAQavshACVFNQAAA 896
Cdd:cd05917 221 KTAEA------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSD----VQVVGVPDE 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 897 TGGDarQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDR 954
Cdd:cd05917 290 RYGE--EVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
4-424 |
2.40e-19 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 92.44 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEE-GEVWQWVAADRTFGEP 82
Cdd:cd19539 1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 83 SIIDLRTAPDPHRAAteRMQADLAQD--LRVDGGNPLVCHqLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAW 160
Cdd:cd19539 81 VRDLSDPDSDRERRL--EELLRERESrgFDLDEEPPIRAV-LGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 161 QRGEATPE-SPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAA--GSDIWRMKLEMNADAFR 237
Cdd:cd19539 158 RKGPAAPLpELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRPRPAGFPypGADLRFELDAELVAALR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 238 RLAGHApQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRMGSAALTSTGPVLNVLPLAVHIDAQETLADLAMRLAAQL 317
Cdd:cd19539 238 ELAKRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 318 KKMRRHQRYDAEQIVRDSG--KAAGDEPLFGPVLNVKVF-DYQLDIDGVQAVTHTLATGPVNDLELALFPDETG-GLSLE 393
Cdd:cd19539 317 VDAQRHQELPFQQLVAELPvdRDAGRHPLVQIVFQVTNApAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGtGLRGS 396
|
410 420 430
....*....|....*....|....*....|.
gi 635952396 394 ILANKARYDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19539 397 LGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
462-884 |
3.41e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 93.04 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 462 ADQARKtpDAPAL----ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDT 537
Cdd:PRK04319 53 ADGGRK--DKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 538 GYPDDRLRMMLEDARPSLLITSEDQLAR--FSDIPGLES--------------LCYQQPLA-AGDDAPLALSKPDHTAYI 600
Cdd:PRK04319 131 AFMEEAVRDRLEDSEAKVLITTPALLERkpADDLPSLKHvllvgedveegpgtLDFNALMEqASDEFDIEWTDREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 601 IFTSGSTGRPKGVMVGQTAIVNRllWMQDRYPLSAQDVvaqktpcsfDVsvweFW------W----------PFIAGAQL 664
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHNAMLQH--YQTGKYVLDLHED---------DV----YWctadpgWvtgtsygifaPWLNGATN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 665 VMAEPEAhrDPQAMQQFFARYGVTTTHFVPS---ML----AAFVASLDADSvaacrtLRRVFCSGEALPTELCREWERLT 737
Cdd:PRK04319 276 VIDGGRF--SPERWYRILEDYKVTVWYTAPTairMLmgagDDLVKKYDLSS------LRHILSVGEPLNPEVVRWGMKVF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 738 GAPLHNLYGPTE-AAVDVSWYPAcgpeLAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYL-TGI-QLAQGYLG 814
Cdd:PRK04319 348 GLPIHDNWWMTEtGGIMIANYPA----MDIKPGS---MGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGWpSMMRGIWN 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 815 RPDLTASRFIADpfapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:PRK04319 421 NPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEA 483
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
469-951 |
4.18e-19 |
|
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: 92.36 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPSLLITSedqlarfsdipglESLCYQQPLAAGDDAPLALSKPDHTAYII--FTSGSTGRPKGVMVGQ-----TAIV 621
Cdd:cd12118 98 RHSEAKVLFVD-------------REFEYEDLLAEGDPDFEWIPPADEWDPIAlnYTSGTTGRPKGVVYHHrgaylNALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 622 NRLLWMQDRYPlsaqdvVAQKTPCSFDVSVWEFWW--PFIAGAQLVMaepeAHRDPQAMQQFFARYGVttTHF--VPSML 697
Cdd:cd12118 165 NILEWEMKQHP------VYLWTLPMFHCNGWCFPWtvAAVGGTNVCL----RKVDAKAIYDLIEKHKV--THFcgAPTVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 698 AAFVASLDADSVAACRTLrRVFCSGEALPTELCREWERLTGAPLHnLYGPTEA---AVDVSWYPAC----GPE---LAAV 767
Cdd:cd12118 233 NMLANAPPSDARPLPHRV-HVMTAGAPPPAAVLAKMEELGFDVTH-VYGLTETygpATVCAWKPEWdelpTEErarLKAR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 768 TGSSVPIgwpvwNTGLRILDAA-MRPVP-PGV-AGDLYLTGIQLAQGYLGRPDLTasrfiADPFAPGerMYRTGDVARWL 844
Cdd:cd12118 311 QGVRYVG-----LEEVDVLDPEtMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEAT-----AEAFRGG--WFHSGDLAVIH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 845 TNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDArqLVGYLVSDSGLPLDTAALKAR 924
Cdd:cd12118 379 PDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAA----VVARPDEKWGEV--PCAFVELKEGAKVTEEEIIAF 452
|
490 500
....*....|....*....|....*....
gi 635952396 925 LAEQLPPHMVP--VVLMqlaELPLSANGK 951
Cdd:cd12118 453 CREHLAGFMVPktVVFG---ELPKTSTGK 478
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
463-883 |
2.67e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 90.34 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 463 DQARKTPDAPALA---------DARWQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV-F--LTLALHGiveAG 529
Cdd:PRK09274 14 RAAQERPDQLAVAvpggrgadgKLAYDeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLeFfaLTFALFK---AG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWLPLDTGYPDDRLRMMLEDARPSLLIT-SEDQLARF-----------------SDIPG---LESLCYQQPLAagdDAP 588
Cdd:PRK09274 91 AVPVLVDPGMGIKNLKQCLAEAQPDAFIGiPKAHLARRlfgwgkpsvrrlvtvggRLLWGgttLATLLRDGAAA---PFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 589 LALSKPDHTAYIIFTSGSTGRPKGV------MVGQ-TAIVNRLLWMQDRYPLSAQDVVAQKTPCsfdvsvwefwwpfiAG 661
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVvythgmFEAQiEALREDYGIEPGEIDLPTFPLFALFGPA--------------LG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 662 AQLVMAEPEAHR----DPQAMQQFFARYGVTTThFVPSMLAAFVAsldadsvAACR-------TLRRVFCSGEALPTELc 730
Cdd:PRK09274 234 MTSVIPDMDPTRpatvDPAKLFAAIERYGVTNL-FGSPALLERLG-------RYGEangiklpSLRRVISAGAPVPIAV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 731 reWERLT-----GAPLHNLYGPTEA----------AVDVSW------------YPACGPELAAVTGSSVPIgwPVWNTGL 783
Cdd:PRK09274 305 --IERFRamlppDAEILTPYGATEAlpissiesreILFATRaatdngagicvgRPVDGVEVRIIAISDAPI--PEWDDAL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 784 RildaamrpVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPfaPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:PRK09274 381 R--------LATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAG 450
|
490 500
....*....|....*....|
gi 635952396 864 QRIELGEIDRVMSGLPDVAQ 883
Cdd:PRK09274 451 GTLYTIPCERIFNTHPGVKR 470
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
461-952 |
2.89e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 89.84 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 461 VADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAV-ALPRSVFLTLALhGIVEAGAAWLPLDTGY 539
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLIlMLNRTEFVESVL-AANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 PDDRLRMMLEDARPSLLITsEDQLARFS-----DIPGLE------------SLCYQQPLAAGDDAPLALSKPDHT-AYII 601
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVT-EAALAPVAtavrdIVPLLStvvvaggssddsVLGYEDLLAEAGPAHAPVDIPNDSpALIM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 602 FTSGSTGRPKGVMVGQTAIVNRLL-----WMQDRyplsAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMaEPEAHRDPQ 676
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHANLTGQAMtclrtNGADI----NSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI-YPLGAFDPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 677 AMQQFFARYGVTTTHFVPSMLAAFVasldADSVAACRTLR-RVFCSGEA--LPTELCREWERLTGAPLHNLYGPTEAAvd 753
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVC----AEQQARPRDLAlRVLSWGAApaSDTLLRQMAATFPEAQILAAFGQTEMS-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 754 vswyP-AC---GPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTasrfiADPFA 829
Cdd:PRK07786 330 ----PvTCmllGEDAIRKLGS---VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEAT-----AEAFA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 830 PGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDARQLVGyLV 909
Cdd:PRK07786 398 GG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVA----VIGRADEKWGEVPVAVA-AV 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 635952396 910 SDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:PRK07786 471 RNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
480-854 |
4.76e-18 |
|
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: 88.67 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPsllits 559
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 edqlarfsdipgleslcyqqplaagdDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVv 639
Cdd:cd05910 76 --------------------------DAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 640 aqktpcsfDVSVWEFWWPFIAGAQLVMAEPE------AHRDPQAMQQFFARYGVTTTHFVPSMLAAfVASLDADSVAACR 713
Cdd:cd05910 129 --------DLATFPLFALFGPALGLTSVIPDmdptrpARADPQKLVGAIRQYGVSIVFGSPALLER-VARYCAQHGITLP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 714 TLRRVFCSGEALPTELCREWERLT--GAPLHNLYGPTEAavdvswYPAC---GPELAAVT------GSSVPIGWPVWNTG 782
Cdd:cd05910 200 SLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA------LPVSsigSRELLATTtaatsgGAGTCVGRPIPGVR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 783 LRILDAAMRP---------VPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERM-YRTGDVARWLTNGAVEYL 852
Cdd:cd05910 274 VRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFwHRMGDLGYLDDEGRLWFC 350
|
..
gi 635952396 853 GR 854
Cdd:cd05910 351 GR 352
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
465-840 |
8.71e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 88.21 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPA--LADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDD 542
Cdd:PRK13391 7 AQTTPDKPAviMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 543 RLRMMLEDARPSLLITSEDQL----ARFSDIPGLEsLC--------------YQQPLAAGDDAPLAlSKPDHTAyIIFTS 604
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLdvarALLKQCPGVR-HRlvldgdgelegfvgYAEAVAGLPATPIA-DESLGTD-MLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 605 GSTGRPKGVmvgqtaivnrllwmqdRYPLSAQDVVAQKTPCSFDVSVWEFW--WPFIAGAQLVMAEPEA----------- 671
Cdd:PRK13391 164 GTTGRPKGI----------------KRPLPEQPPDTPLPLTAFLQRLWGFRsdMVYLSPAPLYHSAPQRavmlvirlggt 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 672 -----HRDPQAMQQFFARYGVTTTHFVPSMlaaFVASLDADSVAACR----TLRRVFCSGEALPTELCREWERLTGAPLH 742
Cdd:PRK13391 228 vivmeHFDAEQYLALIEEYGVTHTQLVPTM---FSRMLKLPEEVRDKydlsSLEVAIHAAAPCPPQVKEQMIDWWGPIIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 743 NLYGPTEAAvdvsWYPACGPELAAVTGSSVpiGWPVWNTgLRILDAAMRPVPPGVAGDLYLTGIQLAQgYLGRPDLTASR 822
Cdd:PRK13391 305 EYYAATEGL----GFTACDSEEWLAHPGTV--GRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEA 376
|
410
....*....|....*...
gi 635952396 823 FIADPfapgeRMYRTGDV 840
Cdd:PRK13391 377 RHPDG-----TWSTVGDI 389
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
456-957 |
1.69e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 87.62 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQ-LLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLP 534
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 LDTGYPDDRLRMMLEDARPSLLI-------TSEDQLA----------RFSDIPGLE-----------------------S 574
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVvidnfgtTVQQVIAdtpvkqvittGLGDMLGFPkaalvnfvvkyvkklvpeyringA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 575 LCYQQPLAAGDD--APLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL----WMQDRYPL-SAQDVVAQKTPCS- 646
Cdd:PRK08751 186 IRFREALALGRKhsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLeEGCEVVITALPLYh 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 647 -FDVSVWEFWWPFIAGAQLVMAEPeahRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEAL 725
Cdd:PRK08751 266 iFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDF-SSLKMTLGGGMAV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 726 PTELCREWERLTGAPLHNLYGPTEAAVDVSWYPAcgpELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTG 805
Cdd:PRK08751 342 QRSVAERWKQVTGLTLVEAYGLTETSPAACINPL---TLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEIGELCIKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 806 IQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAqav 885
Cdd:PRK08751 416 PQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL--- 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 886 shacvfnQAAATG---GDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK08751 487 -------EVAAVGvpdEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
31-424 |
2.47e-17 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 86.10 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 31 HYVE-----LRGALDPTLLGKAIVAGLQQADTLSLRFEEEE-GEVWQWVAADRTFGEPsIIDLRT-APDPHRAATER-MQ 102
Cdd:cd19543 23 AYVEqmvitLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLPWR-ELDLSHlSEAEQEAELEAlAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 103 ADLAQDLRVDGGNPLVCHqLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGEATPESPFTPfaevvdeYQ 182
Cdd:cd19543 102 EDRERGFDLARAPLMRLT-LIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVRP-------YR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 183 RYAgseAW--QRDK----AFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRLAGHAPQ--------CQP 248
Cdd:cd19543 174 DYI---AWlqRQDKeaaeAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQhgvtlntvVQG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 249 AdlalalTTLWLGRLCNRMDYAAGFIFMRRmgSAAL----TSTGPVLNVLPLAVHIDAQETLADLAMRLAAQLKKMRRHQ 324
Cdd:cd19543 251 A------WALLLSRYSGRDDVVFGTTVSGR--PAELpgieTMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 325 RYDAEQIvrdSGKAAGDEPLFG--------PVLNVKVFDYQ---LDIDGVQAVTHTlatgpvN-DLELALFPDETggLSL 392
Cdd:cd19543 323 YVPLYEI---QAWSEGKQALFDhllvfenyPVDESLEEEQDedgLRITDVSAEEQT------NyPLTVVAIPGEE--LTI 391
|
410 420 430
....*....|....*....|....*....|..
gi 635952396 393 EILANKARYDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19543 392 KLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
474-893 |
2.76e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 86.77 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 474 LADARWQF-SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDR----LRMML 548
Cdd:cd05908 8 LGDKKEKFvSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHklklNKVWN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARPsLLITSEDQLARFsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd05908 88 TLKNP-YLITEEEVLCEL---------------------------ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DRYPLSAQDVVAQKTPCSFDVSVWEFWW-PFIAGA-QLVMAEPEAHRDPQAMQQFFARYGVTTTHfVPSMLAAFVASLDA 706
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFHLaPLIAGMnQYLMPTRLFIRRPILWLKKASEHKATIVS-SPNFGYKYFLKTLK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 707 DSVAA---CRTLRRVFCSGEALPTELCREW------ERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAVTG-------- 769
Cdd:cd05908 219 PEKANdwdLSSIRMILNGAEPIDYELCHEFldhmskYGLKRNAILPVYGLAEASVGASLPKAQSPFKTITLGrrhvthge 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 770 -------------SSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYR 836
Cdd:cd05908 299 pepevdkkdseclTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 837 TGDVArWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHAC-VFNQ 893
Cdd:cd05908 373 TGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACgVNNS 429
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
451-938 |
3.61e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.85 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 451 PLPATTLSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALP-RSVFLTLALhGIVEAG 529
Cdd:PRK08279 33 PDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMEnRPEYLAAWL-GLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPG----------LESLCYQQPLAAGDDAPLALSKPDH--- 596
Cdd:PRK08279 112 AVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARAdlarpprlwvAGGDTLDDPEGYEDLAAAAAGAPTTnpa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 597 ---------TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIA-GAQLVM 666
Cdd:PRK08279 192 srsgvtakdTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAaGATLAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 667 AEpeahrdpqamqQFFA--------RYGVTTTHFVPSM----LAAFVASLDADsvaacRTLRRVFcsGEALPTELCREWE 734
Cdd:PRK08279 272 RR-----------KFSAsrfwddvrRYRATAFQYIGELcrylLNQPPKPTDRD-----HRLRLMI--GNGLRPDIWDEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 735 RLTGAP-LHNLYGPTEAAV---DVSWYP-ACG--PELAAVTGSSVPI----GWPVWNTglrilDAAMRPVPPGVAGDLyL 803
Cdd:PRK08279 334 QRFGIPrILEFYAASEGNVgfiNVFNFDgTVGrvPLWLAHPYAIVKYdvdtGEPVRDA-----DGRCIKVKPGEVGLL-I 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 804 TGIQLAQ---GYlGRPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPD 880
Cdd:PRK08279 408 GRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635952396 881 VAQAVshacVFN-QAAATGGDArqlvGY--LVSDSGLPLDTAALKARLAEQLPPHMVPVVL 938
Cdd:PRK08279 487 VEEAV----VYGvEVPGTDGRA----GMaaIVLADGAEFDLAALAAHLYERLPAYAVPLFV 539
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
459-957 |
5.28e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 85.97 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 459 ALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWL---P 534
Cdd:PRK05677 28 AVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 535 L-----------DTG-----------------YPDDRLRMML----EDARP---SLLITS-----EDQLARFSdIPGleS 574
Cdd:PRK05677 108 LytaremehqfnDSGakalvclanmahlaekvLPKTGVKHVIvtevADMLPplkRLLINAvvkhvKKMVPAYH-LPQ--A 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 575 LCYQQPLAAGDDAPL--ALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLwmQDRYPLSAQ-----DVVAQKTPCsf 647
Cdd:PRK05677 185 VKFNDALAKGAGQPVteANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML--QCRALMGSNlnegcEILIAPLPL-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 648 dVSVWEFwwPFIAGAQLVMAepeAH-------RDPQAMQQFFARYGVTtthfvpsmlaAFVAsLDADSVAACRT------ 714
Cdd:PRK05677 261 -YHIYAF--TFHCMAMMLIG---NHnilisnpRDLPAMVKELGKWKFS----------GFVG-LNTLFVALCNNeafrkl 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 715 ----LRRVFCSGEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPACGPELAAvtgssvpIGWPVWNTGLRILDAAM 790
Cdd:PRK05677 324 dfsaLKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGT-------IGIPVPSTLCKVIDDDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 791 RPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGE 870
Cdd:PRK05677 397 NELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 871 IDRVMSGLPDVAqavshacvfnQAAATG------GDARQLvgYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAEL 944
Cdd:PRK05677 471 LEDVLAALPGVL----------QCAAIGvpdeksGEAIKV--FVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDEL 538
|
570
....*....|...
gi 635952396 945 PLSANGKLDRKAL 957
Cdd:PRK05677 539 PTTNVGKILRREL 551
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
480-885 |
5.31e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.01 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV-----FLTLALHGIVEAgaawlPLDTGYPDDRLRMMLEDARPS 554
Cdd:PLN02860 32 RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDlylewLLAVACAGGIVA-----PLNYRWSFEEAKSAMLLVRPV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 555 LLITSED-----QLARFSDIPG------LESLCYQQPLAAGD-----------DAPLAL---SKPDHTAYIIFTSGSTGR 609
Cdd:PLN02860 107 MLVTDETcsswyEELQNDRLPSlmwqvfLESPSSSVFIFLNSflttemlkqraLGTTELdyaWAPDDAVLICFTSGTTGR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 610 PKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGA-QLVMAEPEAHRDPQAMQQffarYGVT 688
Cdd:PLN02860 187 PKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAcHVLLPKFDAKAALQAIKQ----HNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 689 TTHFVPSMLAAFVASLDADSVAACR-TLRRVFCSGEALPTELCREWERL-TGAPLHNLYGPTEAAVDVSWYPACGPELAA 766
Cdd:PLN02860 263 SMITVPAMMADLISLTRKSMTWKVFpSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMTEACSSLTFMTLHDPTLES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 767 VTG----------SSVP------IGWPVWNTGLRI-LDAAMRpvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADPFa 829
Cdd:PLN02860 343 PKQtlqtvnqtksSSVHqpqgvcVGKPAPHVELKIgLDESSR------VGRILTRGPHVMLGYWGQNSETASVLSNDGW- 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 830 pgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAV 885
Cdd:PLN02860 416 -----LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVV 466
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
481-882 |
1.74e-16 |
|
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: 84.03 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 dqlarfsdipgleslcyqqplaagddaplalskPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVV- 639
Cdd:cd05914 88 ---------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 640 -----AQKTPCSFDvsvweFWWPFIAGAQLVMAE--PEAHRDPQAMQQFFARYGVTT---------THFVPSM------- 696
Cdd:cd05914 135 silplHHIYPLTFT-----LLLPLLNGAHVVFLDkiPSAKIIALAFAQVTPTLGVPVplviekifkMDIIPKLtlkkfkf 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 697 -LAAFVASLDADSVAACRTLR------RVFCSGEA-LPTELCREWERLtGAPLHNLYGPTEAAVDVSWYPACGPELAAVt 768
Cdd:cd05914 210 kLAKKINNRKIRKLAFKKVHEafggniKEFVIGGAkINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRLGSA- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 769 gssvpiGWPVWNTGLRILDaamrPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGA 848
Cdd:cd05914 288 ------GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAEGY 351
|
410 420 430
....*....|....*....|....*....|....*
gi 635952396 849 VEYLGRSDDQLKI-RGQRIELGEIDRVMSGLPDVA 882
Cdd:cd05914 352 LYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVL 386
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
463-957 |
2.64e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 83.68 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 463 DQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPgDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDD 542
Cdd:PRK07638 9 KHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 543 RLRMMLEDARPSLLITSEDQLARFSDIPG--LESLCYQQPLAAGDDAPLALSKPDHTA-YIIFTSGSTGRPKGVMVGQTA 619
Cdd:PRK07638 88 ELKERLAISNADMIVTERYKLNDLPDEEGrvIEIDEWKRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 620 IVNRLLWMQDRYPLSAQDVVAqkTPCSFDVSVwefwwpFIAGA-------QLVMAEPEAhrDPQAMQQFFARYGVTTTHF 692
Cdd:PRK07638 168 WLHSFDCNVHDFHMKREDSVL--IAGTLVHSL------FLYGAistlyvgQTVHLMRKF--IPNQVLDKLETENISVMYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 693 VPSMLAAFVaSLDA--DSVAacrtlrRVFCSGEALPTElcrEWERLTG----APLHNLYGPTEaavdVSWYPACGPELAA 766
Cdd:PRK07638 238 VPTMLESLY-KENRviENKM------KIISSGAKWEAE---AKEKIKNifpyAKLYEFYGASE----LSFVTALVDEESE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 767 VTGSSVpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGrpdltasrfiadpfapGERMYRTGDVARWLTN 846
Cdd:PRK07638 304 RRPNSV--GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII----------------GGVLARELNADGWMTV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 847 GAVEYL---------GRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDarQLVGYLVSDSglplD 917
Cdd:PRK07638 366 RDVGYEdeegfiyivGREKNMILFGGINIFPEEIESVLHEHPAVDEIV----VIGVPDSYWGE--KPVAIIKGSA----T 435
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 635952396 918 TAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07638 436 KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
5-424 |
3.81e-16 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 82.50 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 5 LPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRF-EEEEGEVWQWV--AADRTFGE 81
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFiEDGLGQPVQVVhrQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 82 PSIIDLRTAPDPHRAATERmqaDLAQDLRVDGGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQ 161
Cdd:cd19536 82 LDLTPLEEQLDPLRAYKEE---TKIRRFDLGRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 162 RGEATPESPFTPFAEVVDEYQRYAGSEAWQRdkaFWQAQRQAlpspASLSAAPLGGRAAGSDI---WRMKLEMNADAFRR 238
Cdd:cd19536 159 EYKPLSLPPAQPYRDFVAHERASIQQAASER---YWREYLAG----ATLATLPALSEAVGGGPeqdSELLVSVPLPVRSR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 239 LAGHAPQCQPADLALALTTLWLGRLCNRMDYAAGFIFMRRmgSAALTST----GPVLNVLPLAVHIdAQETLADLAMRLA 314
Cdd:cd19536 232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGR--SEETTGAerllGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 315 AQLKKMRRHQRYDAEQIVRDSGKaagdEPLFGPVLNVKVFDYQ----LDIDGVQAVTHTL--ATGPVNDLELALFPDEtG 388
Cdd:cd19536 309 EQELESLSHEQVPLADIQRCSEG----EPLFDSIVNFRHFDLDfglpEWGSDEGMRRGLLfsEFKSNYDVNLSVLPKQ-D 383
|
410 420 430
....*....|....*....|....*....|....*.
gi 635952396 389 GLSLEILANKARYDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19536 384 RLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
453-957 |
5.36e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 82.77 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 453 PATTLSALVADQArkTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGD-SVAVALPRSVFLTLALHGIVEAGAA 531
Cdd:PRK13388 1 MRDTIAQLLRDRA--GDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAALGGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 532 WLPLDtgyPDDRLRMMLEDARPS---LLITSEDQLARFS--DIPGLESL-----CYQQPLA-AGDDAPLALSKPDHTAYI 600
Cdd:PRK13388 79 LVGLN---TTRRGAALAADIRRAdcqLLVTDAEHRPLLDglDLPGVRVLdvdtpAYAELVAaAGALTPHREVDAMDPFML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 601 IFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIA-GAQLvmaepeAHRDPQAMQ 679
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVAsGAAV------ALPAKFSAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 680 QFFA---RYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFcSGEALPTELcREWERLTGAPLHNLYGPTEAAVDVSW 756
Cdd:PRK13388 230 GFLDdvrRYGATYFNYVGKPLAYILATPERPDDAD-NPLRVAF-GNEASPRDI-AEFSRRFGCQVEDGYGSSEGAVIVVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 757 YPACGPelaavtGSsvpIGWPVwnTGLRILDAA-MRPVPPGV-------------AGDLYLT-GIQLAQGYLGRPDLTAS 821
Cdd:PRK13388 307 EPGTPP------GS---IGRGA--PGVAIYNPEtLTECAVARfdahgallnadeaIGELVNTaGAGFFEGYYNNPEATAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 822 RFiadpfAPGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGDa 901
Cdd:PRK13388 376 RM-----RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVA----VYAVPDERVGD- 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 902 rQLVGYLVSDSGLPLDTAALKARLAEQ--LPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK13388 444 -QVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
481-952 |
1.15e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 81.49 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSE 560
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 561 D------------------QLARFSDIPGLESlcYQQPLAAGDDAPLALSKP-DHTAYiifTSGSTGRPKGVM-----VG 616
Cdd:PRK08276 92 AladtaaelaaelpagvplLLVVAGPVPGFRS--YEEALAAQPDTPIADETAgADMLY---SSGTTGRPKGIKrplpgLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 617 QTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFD--VSVWEFWWPFIAGAQLVMaepeAHRDPQAMQQFFARYGVTTTHFVP 694
Cdd:PRK08276 167 PDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHtaPLRFGMSALALGGTVVVM----EKFDAEEALALIERYRVTHSQLVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 695 SMlaaFVASLD-ADSVAA---CRTLRRVFCSGEALPTELCR---EWerlTGAPLHNLYGPTEAAVdvswYPACGPELAAV 767
Cdd:PRK08276 243 TM---FVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRamiDW---WGPIIHEYYASSEGGG----VTVITSEDWLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 768 TGSSVpiGWPvWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapGERMYRTGDVArWLTNG 847
Cdd:PRK08276 313 HPGSV--GKA-VLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWVTVGDVG-YLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 848 AVEYL-GRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVS------------HACVFNQAAATGGDARqlvgylvsdsgl 914
Cdd:PRK08276 383 GYLYLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVfgvpdeemgervKAVVQPADGADAGDAL------------ 450
|
490 500 510
....*....|....*....|....*....|....*...
gi 635952396 915 pldTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKL 952
Cdd:PRK08276 451 ---AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
466-957 |
1.26e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 81.79 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 466 RKTPDAPALADARWQFSYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWL---PL------ 535
Cdd:PRK12492 35 KKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPLytarem 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 -----DTG-----------------YPDDRLRMMLE----DARPS----LLITSEDQLARFsdIPGL---ESLCYQQPLA 582
Cdd:PRK12492 115 rhqfkDSGaralvylnmfgklvqevLPDTGIEYLIEakmgDLLPAakgwLVNTVVDKVKKM--VPAYhlpQAVPFKQALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 583 AGDDA---PLALSKPDhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLwmQDRYPLSAQDVVAQktpcsfdvsvwefwwPFI 659
Cdd:PRK12492 193 QGRGLslkPVPVGLDD-IAVLQYTGGTTGLAKGAMLTHGNLVANML--QVRACLSQLGPDGQ---------------PLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 660 AGAQLVMAEPEAHRDPQAMQQFFARYGVTTTHFV----PSMLAAFVASLDADSVAACRTLRRVFCS-------------- 721
Cdd:PRK12492 255 KEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVlitnPRDIPGFIKELGKWRFSALLGLNTLFVAlmdhpgfkdldfsa 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 722 -------GEALPTELCREWERLTGAPLHNLYGPTEAAVDVSWYPAcgPELAAVtGSsvpIGWPVWNTGLRILDAAMRPVP 794
Cdd:PRK12492 335 lkltnsgGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPY--GELARL-GT---VGIPVPGTALKVIDDDGNELP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 795 PGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRV 874
Cdd:PRK12492 409 LGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 875 MSGLPDVAQAvshACVFNQAAATGGDARQLVgyLVSDSGLPLDtaALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDR 954
Cdd:PRK12492 483 VMAHPKVANC---AAIGVPDERSGEAVKLFV--VARDPGLSVE--ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILR 555
|
...
gi 635952396 955 KAL 957
Cdd:PRK12492 556 REL 558
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
456-844 |
1.71e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 81.63 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALA-----DARWQF-SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAG 529
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAqrepgHGQWRKvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWLPLDTGYP-----DDRLRMMLEDARPSLLITseDQLARFS------------------DIPGLESLCYQQ----PLA 582
Cdd:PRK12582 130 VPAAPVSPAYSlmshdHAKLKHLFDLVKPRVVFA--QSGAPFAralaaldlldvtvvhvtgPGEGIASIAFADlaatPPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 583 AGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAI-VNRLLWMQDRYPLSAQDVvaqktPCSFDvsvWEFWWPFIAG 661
Cdd:PRK12582 208 AAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMcANIAMQEQLRPREPDPPP-----PVSLD---WMPWNHTMGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 662 AQ----LVMAEPEAHRDP-QAMQQFFAR-----YGVTTTHF--VPSMLAAFVASLDADSvAACRT----LRRVFCSGEAL 725
Cdd:PRK12582 280 NAnfngLLWGGGTLYIDDgKPLPGMFEEtirnlREISPTVYgnVPAGYAMLAEAMEKDD-ALRRSffknLRLMAYGGATL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 726 PTELcreWERL-------TGA--PLHNLYGPTEAA---VDVSWypacGPELAAVtgssvpIGWPVWNTGLRIldaamrpV 793
Cdd:PRK12582 359 SDDL---YERMqalavrtTGHriPFYTGYGATETApttTGTHW----DTERVGL------IGLPLPGVELKL-------A 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 635952396 794 PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWL 844
Cdd:PRK12582 419 PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFV 463
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
5-424 |
1.87e-15 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 80.04 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 5 LPLVAAQPGiwMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRF--EEEEGEVWQWVAADrtfGEP 82
Cdd:cd19542 2 YPCTPMQEG--MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKS---LDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 83 SIIDLRTAPDphraATERMQADLAQDlRVDGGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYrawqr 162
Cdd:cd19542 77 PIEEVETDED----SLDALTRDLLDD-PTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 163 gEATPESPFTPFAEvvdeYQRYAGSEAWQRDKAFWQ-----AQRQALPSpaSLSAAPLGGRAAGSDIWRMKLEmnadAFR 237
Cdd:cd19542 147 -NGQLLPPAPPFSD----YISYLQSQSQEESLQYWRkylqgASPCAFPS--LSPKRPAERSLSSTRRSLAKLE----AFC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 238 RLAGHAPQ--CQPAdlalalTTLWLGRLCNRMDYAAGFIFMRRmgSAALTST----GPVLNVLPLAVHIDAQETLADLAM 311
Cdd:cd19542 216 ASLGVTLAslFQAA------WALVLARYTGSRDVVFGYVVSGR--DLPVPGIddivGPCINTLPVRVKLDPDWTVLDLLR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 312 RLAAQLKKMRRHQRYDAEQIVRDSGKaAGDEPLFGPVLNVKVFDYQLDIDGV-QAVTHTLATGPVNDLELALF-PDETGG 389
Cdd:cd19542 288 QLQQQYLRSLPHQHLSLREIQRALGL-WPSGTLFNTLVSYQNFEASPESELSgSSVFELSAAEDPTEYPVAVEvEPSGDS 366
|
410 420 430
....*....|....*....|....*....|....*
gi 635952396 390 LSLEILANKARYDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19542 367 LKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
756-1043 |
3.54e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 77.87 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WYPACGPELAAVTGSSVPIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGyLGRPDLTASRFIADPFAPGERMY 835
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLL-RIRLLAAAARAPFIPVPYPAQPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 836 RTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMsglpdVAQAVSHACVFNQAAATGGDARQLVGYLVSDSGLP 915
Cdd:COG3433 80 RQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELL-----LVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 916 LDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPLPTL------GGERSGRPPEPGMETLVATAFSQLLGC 989
Cdd:COG3433 155 GLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAaeallaAASPAPALETALTEEELRADVAELLGV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 990 EVNDIDAD--FFALGGHSLLAMRLAAQLsRQLARQVTPGQVMVASTVGKLSALLAA 1043
Cdd:COG3433 235 DPEEIDPDdnLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAA 289
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
466-957 |
4.42e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 80.10 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 466 RKTPDAPALADARWQFSYREMRQQVVALAQLLRQR-GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRL 544
Cdd:PRK08974 34 ARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPREL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 545 RMMLEDARPSLLI-------TSE-----------------DQLARfsdipGLESLC-----YQQPLAAGDDAPLALS--- 592
Cdd:PRK08974 114 EHQLNDSGAKAIVivsnfahTLEkvvfktpvkhviltrmgDQLST-----AKGTLVnfvvkYIKRLVPKYHLPDAISfrs 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 593 -----------KP----DHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRY-PL--SAQDVVAQKTPCS--FDVSVW 652
Cdd:PRK08974 189 alhkgrrmqyvKPelvpEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYgPLlhPGKELVVTALPLYhiFALTVN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 653 EFWWPFIAGAQLVMAEPeahRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCRE 732
Cdd:PRK08974 269 CLLFIELGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDF-SSLKLSVGGGMAVQQAVAER 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 733 WERLTGAPLHNLYGPTEAAVDVSwypACGPELAAVTGSsvpIGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGY 812
Cdd:PRK08974 345 WVKLTGQYLLEGYGLTECSPLVS---VNPYDLDYYSGS---IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 813 LGRPDLTASrFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFN 892
Cdd:PRK08974 419 WQRPEATDE-VIKDGW------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVA----AVG 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 893 QAAATGGDARQLvgYLV-SDSGLPLDtaALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK08974 488 VPSEVSGEAVKI--FVVkKDPSLTEE--ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
463-957 |
1.47e-14 |
|
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: 78.34 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 463 DQARKTPDAPALADA--RWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYP 540
Cdd:cd17642 25 KRYASVPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 541 DDRLRMMLEDARPSLLITSEDQLARF-------------------SDIPGLESL--CYQQPLAAGDDA----PLALSKPD 595
Cdd:cd17642 105 ERELDHSLNISKPTIVFCSKKGLQKVlnvqkklkiiktiiildskEDYKGYQCLytFITQNLPPGFNEydfkPPSFDRDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 596 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDryPLsaqdVVAQKTPCSFDVSVWEFWWPF---------IAGAQLVM 666
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARD--PI----FGNQIIPDTAILTVIPFHHGFgmfttlgylICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 667 AepeahrdPQAMQQFFAR----YGVTTTHFVPSMLAAFVASLDADSVaACRTLRRVFCSGEALPTELCREWERLTGAP-L 741
Cdd:cd17642 259 M-------YKFEEELFLRslqdYKVQSALLVPTLFAFFAKSTLVDKY-DLSNLHEIASGGAPLSKEVGEAVAKRFKLPgI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 742 HNLYGPTEAAVDVSWYP-------ACGpelAAVTGSSVPIGWPvwNTGlRILDAAMRpvppgvaGDLYLTGIQLAQGYLG 814
Cdd:cd17642 331 RQGYGLTETTSAILITPegddkpgAVG---KVVPFFYAKVVDL--DTG-KTLGPNER-------GELCVKGPMIMKGYVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 815 RPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVM-----------SGLPD-VA 882
Cdd:cd17642 398 NPEATKALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILlqhpkifdagvAGIPDeDA 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 883 QAVSHACVFNQAAATGGDaRQLVGYLVSDSglpldTAALKARLAeqlpphmvpVVLMQlaELPLSANGKLDRKAL 957
Cdd:cd17642 472 GELPAAVVVLEAGKTMTE-KEVMDYVASQV-----STAKRLRGG---------VKFVD--EVPKGLTGKIDRRKI 529
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
465-842 |
5.38e-14 |
|
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: 76.32 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALAD----ARWQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGY 539
Cdd:cd05921 5 ARQAPDRTWLAEregnGGWRrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 540 ----PD-DRLRMMLEDARPSLLITSE----------------DQLARFSDIPG-----LESLCYQQPLAAGDDApLALSK 593
Cdd:cd05921 85 slmsQDlAKLKHLFELLKPGLVFAQDaapfaralaaifplgtPLVVSRNAVAGrgaisFAELAATPPTAAVDAA-FAAVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 594 PDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVvaqktPCSFDvsvwefW--WPFIAGAQLVMaEPEA 671
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVLVD------WlpWNHTFGGNHNF-NLVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 672 HR-------DPQAMQQFFAR-----YGVTTTHF--VPSMLAAFVASLDADSVAACRTLRRV---FCSGEALPTELcreWE 734
Cdd:cd05921 232 YNggtlyidDGKPMPGGFEEtlrnlREISPTVYfnVPAGWEMLVAALEKDEALRRRFFKRLklmFYAGAGLSQDV---WD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 735 RLTGA---------PLHNLYGPTEAAvdvswypacgpelaavtGSSVPIGWP---VWNTGLRILDAAMRPVPPGVAGDLY 802
Cdd:cd05921 309 RLQALavatvgeriPMMAGLGATETA-----------------PTATFTHWPterSGLIGLPAPGTELKLVPSGGKYEVR 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 635952396 803 LTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVAR 842
Cdd:cd05921 372 VKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAK 405
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-244 |
1.11e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 27 WSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGevwQWVAADRTFGEPSIIDLRTAPDpHRAATERMQADLA 106
Cdd:PRK12316 3659 WNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAG---GWTAEHLPVELGGALLWRAELD-DAEELERLGEEAQ 3734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 107 QDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGEAtPESP--FTPFAEVVDEYQRY 184
Cdd:PRK12316 3735 RSLDLADG-PLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEA-PRLPakTSSFKAWAERLQEH 3812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635952396 185 AGSEAWQRDKAFWQAQRQALPS--PASLSAAPLGGRAAGSDIWRmkleMNADAFRRLAGHAP 244
Cdd:PRK12316 3813 ARGEALKAELAYWQEQLQGVSSelPCDHPQGALQNRHAASVQTR----LDRELTRRLLQQAP 3870
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
465-884 |
1.23e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 74.91 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 465 ARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRS---VFLTLALHGIveaGAAWLPLDTGYPD 541
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSpetLLAYLALLQC---GARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 542 DRLRMMLEDARPSLLITSEDQLArfsdIPGLESLcyqqPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKgvmvgqtAIV 621
Cdd:PRK09029 90 PLLEELLPSLTLDFALVLEGENT----FSALTSL----HLQLVEGAHAVAWQPQRLATMTLTSGSTGLPK-------AAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 622 NR-----------LLWM----QDRYPLSaqdvvaqkTPCsFDVS----VWEfwWPFiAGAQLVMaePEAHRDPQAMQqff 682
Cdd:PRK09029 155 HTaqahlasaegvLSLMpftaQDSWLLS--------LPL-FHVSgqgiVWR--WLY-AGATLVV--RDKQPLEQALA--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 683 aryGVTTTHFVPSMLAAFVASlDADSVaacrTLRRVFCSGEALPTELCREWERL-----TGaplhnlYGPTEAAVDVswy 757
Cdd:PRK09029 218 ---GCTHASLVPTQLWRLLDN-RSEPL----SLKAVLLGGAAIPVELTEQAEQQgircwCG------YGLTEMASTV--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 758 paCGPELAAVTGssvpIGWPVWNTGLRIldaamrpvppgVAGDLYLTGIQLAQGYLGRPDLTasrfiadPFAPGERMYRT 837
Cdd:PRK09029 281 --CAKRADGLAG----VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFAT 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 635952396 838 GDVARWlTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:PRK09029 337 RDRGEW-QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQV 382
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
476-944 |
2.30e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 73.93 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 476 DARWqfSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSL 555
Cdd:cd05940 1 DEAL--TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 556 LITSedqlarfsdipgleslcyqqplaagddaplalskpdhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSA 635
Cdd:cd05940 79 LVVD-------------------------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 636 QDVVAQKTPCSFDVSVWEFWWP-FIAGAQLVMaepeahRDPQAMQQFFA---RYGVTTTHFVPSMLAAFVASLDADSVAA 711
Cdd:cd05940 122 SDVLYTCLPLYHSTALIVGWSAcLASGATLVI------RKKFSASNFWDdirKYQATIFQYIGELCRYLLNQPPKPTERK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 712 CRtLRRVFcsGEALPTELCREW-ERLTGAPLHNLYGPTE---AAVDVSWYP-ACG--PELAAVTGSSVPIGWPVWN-TGL 783
Cdd:cd05940 196 HK-VRMIF--GNGLRPDIWEEFkERFGVPRIAEFYAATEgnsGFINFFGKPgAIGrnPSLLRKVAPLALVKYDLESgEPI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 784 RILDAAMRPVPPGVAGDL--YLTGIQLAQGYLGrPDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKI 861
Cdd:cd05940 273 RDAEGRCIKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 862 RGQRIELGEIDRVMSGLPDVAQAVSHAcvfnqAAATGGDARQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQL 941
Cdd:cd05940 352 KGENVSTTEVAAVLGAFPGVEEANVYG-----VQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQ 426
|
...
gi 635952396 942 AEL 944
Cdd:cd05940 427 PEM 429
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
451-843 |
2.40e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 74.53 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 451 PLPATTLSALVAdQARKTPDAPALA----DARWQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSV-FLTLALhG 524
Cdd:PRK08180 36 DYPRRLTDRLVH-WAQEAPDRVFLAergaDGGWRrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIeHALLAL-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 525 IVEAGAAWLPLDTGY---PDD--RLRMMLEDARPSLLITSEDQL-------ARFSDIP--------------GLESLCYQ 578
Cdd:PRK08180 114 AMYAGVPYAPVSPAYslvSQDfgKLRHVLELLTPGLVFADDGAAfaralaaVVPADVEvvavrgavpgraatPFAALLAT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 579 QPLAAGDDAPLALSkPDHTAYIIFTSGSTGRPKGVMVGQtaivnRLLwmqdrypLSAQDVVAQKtpcsfdvsvwefwWPF 658
Cdd:PRK08180 194 PPTAAVDAAHAAVG-PDTIAKFLFTSGSTGLPKAVINTH-----RML-------CANQQMLAQT-------------FPF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 659 IAGAQLVMAE--PEAHR--------------------DPQAMQQFFA------RYGVTTTHF-VPSMLAAFVASLDADSV 709
Cdd:PRK08180 248 LAEEPPVLVDwlPWNHTfggnhnlgivlynggtlyidDGKPTPGGFDetlrnlREISPTVYFnVPKGWEMLVPALERDAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 710 AACRTLRRV---FCSGEALPTELcreWERL-------TGAPLHNL--YGPTEAAvdvswyPACgpelAAVTGSSV---PI 774
Cdd:PRK08180 328 LRRRFFSRLkllFYAGAALSQDV---WDRLdrvaeatCGERIRMMtgLGMTETA------PSA----TFTTGPLSragNI 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 775 GWPVWNTGLRIldaamrpVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARW 843
Cdd:PRK08180 395 GLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
457-957 |
2.46e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 74.30 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 457 LSALVADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLD 536
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 537 TGYPDDRLRMMLEDARPSLL------------ITSEDQL-----ARFSD-IPGLESLCY------QQPLAAG-------- 584
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVIlcldlvfprvtnVQSATKIehvivTRIADfLPFPKNLLYpfvqkkQSNLVVKvsesetih 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 585 ---------DDAPLALSKPDHT-AYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQDRYP-LSAQDVVaqktpcsfdVSVW 652
Cdd:PRK06710 186 lwnsvekevNTGVEVPCDPENDlALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNcKEGEEVV---------LGVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 653 EFWWPFIAGAQLVMAEPEAHR-------DPQAMQQFFARYGVTTTHFVPSMLAAFVAS-----LDADSVAACrtlrrvfC 720
Cdd:PRK06710 257 PFFHVYGMTAVMNLSIMQGYKmvlipkfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpllkeYDISSIRAC-------I 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 721 SGEA-LPTELCREWERLTGAPLHNLYGPTEAAvdvswyPACGPEL---AAVTGSsVPIGWPvwNTGLRILDAAMRPV-PP 795
Cdd:PRK06710 330 SGSApLPVEVQEKFETVTGGKLVEGYGLTESS------PVTHSNFlweKRVPGS-IGVPWP--DTEAMIMSLETGEAlPP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 796 GVAGDLYLTGIQLAQGYLGRPDLTASrFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVM 875
Cdd:PRK06710 401 GEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 876 SGLPDVAQAVshacVFNQAAATGGDARQlvGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRK 955
Cdd:PRK06710 474 YEHEKVQEVV----TIGVPDPYRGETVK--AFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
..
gi 635952396 956 AL 957
Cdd:PRK06710 548 VL 549
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
4-200 |
3.09e-13 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 73.54 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLS------TLPGAwsvahyVELRGALDPTLLGKAIvaglqqaDTL-----SLR--FEEEEGEVW 70
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEpgsaayNIPGA------LRLRGPLDVAALERAL-------NELvarheALRttFVEVDGEPV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 71 QWVAADRTFGEPsIIDLRTAPDPHR--AATERMQADLAQ--DLRVDggnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSF 146
Cdd:cd19531 68 QVILPPLPLPLP-VVDLSGLPEAEReaEAQRLAREEARRpfDLARG---PLLRATLLRLGEDEHVLLLTMHHIVSDGWSM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 147 PAITRQIAAIYRAWQRGEATPESP----FTPFAevvdEYQR-YAGSEAWQRDKAFWQAQ 200
Cdd:cd19531 144 GVLLRELAALYAAFLAGRPSPLPPlpiqYADYA----VWQReWLQGEVLERQLAYWREQ 198
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
501-957 |
3.62e-13 |
|
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: 73.57 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 501 GVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLE---DARPSLLITSEDQLARFSDipgleslcY 577
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEikaAALVCGLFTGGGALDGLED--------Y 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 578 QQPLAAGDDAPLA-LSKPDhtaYIIFTSGSTGRPKGVMVGQTA--IVNRLLWM-QDRYPLSAQDVVAQKTPCSFDVSvwe 653
Cdd:cd05929 110 EAAEGGSPETPIEdEAAGW---KMLYSGGTTGRPKGIKRGLPGgpPDNDTLMAaALGFGPGADSVYLSPAPLYHAAP--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 654 FWWPFIA---GAQLVMAEpeaHRDPQAMQQFFARYGVTTTHFVPSM----LAAFVASLDADSVAacrTLRRVFCSGEALP 726
Cdd:cd05929 184 FRWSMTAlfmGGTLVLME---KFDPEEFLRLIERYRVTFAQFVPTMfvrlLKLPEAVRNAYDLS---SLKRVIHAAAPCP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 727 TELCREWERLTGAPLHNLYGPTEAaVDVSWYPacGPELAAVTGSsvpIGWPVwNTGLRILDAAMRPVPPGVAGDLYLTGi 806
Cdd:cd05929 258 PWVKEQWIDWGGPIIWEYYGGTEG-QGLTIIN--GEEWLTHPGS---VGRAV-LGKVHILDEDGNEVPPGEIGEVYFAN- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 807 QLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVS 886
Cdd:cd05929 330 GPGFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 887 ------------HACVfnQAAATGGDARQLVGYLVsdsglpldtAALKARLAEQLPPHMVPVVlmqlAELPLSANGKLDR 954
Cdd:cd05929 404 vgvpdeelgqrvHAVV--QPAPGADAGTALAEELI---------AFLRDRLSRYKCPRSIEFV----AELPRDDTGKLYR 468
|
...
gi 635952396 955 KAL 957
Cdd:cd05929 469 RLL 471
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
479-929 |
3.71e-13 |
|
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: 74.03 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 479 WQF---SYREMRQQVVALAQLLR-QRGVKPGDSVAVALPRSV-FLTLALhGIVEAGAAWLPLDTGYPDDRLRMMLEDARP 553
Cdd:cd17632 63 PRFetiTYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPdYATVDL-ALTRLGAVSVPLQAGASAAQLAPILAETEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 554 SLLITSEDQL------------------------------------ARFSDIPGLESLCYQQPLAAGDDAPLALSKPDHT 597
Cdd:cd17632 142 RLLAVSAEHLdlaveavleggtpprlvvfdhrpevdahraalesarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 598 ----AYIIFTSGSTGRPKGVMVGQTAIVNRLLWM---QDRYPLSAqdVVAQKTPCSFdvsvwefwwpfIAGAQ------- 663
Cdd:cd17632 222 ddplALLIYTSGSTGTPKGAMYTERLVATFWLKVssiQDIRPPAS--ITLNFMPMSH-----------IAGRIslygtla 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 664 -------------------LVMAEP-EAHRDPQAMQQFFARYGVTTTHFVpsmLAAFVASLDADSVAAcrTLRRV----- 718
Cdd:cd17632 289 rggtayfaaasdmstlfddLALVRPtELFLVPRVCDMLFQRYQAELDRRS---VAGADAETLAERVKA--ELRERvlggr 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 719 ----FCSGEALPTELCREWERLTGAPLHNLYGPTEAAvdvswypacgpelaAVTGSSVPIGWPVwntglriLDAAMRPVP 794
Cdd:cd17632 364 llaaVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAG--------------AVILDGVIVRPPV-------LDYKLVDVP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 795 ---------PGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDDQLKI-RGQ 864
Cdd:cd17632 423 elgyfrtdrPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLsQGE 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 865 RIELGEIDRVMSGLPDVAQAVSHacvfnqaaatGGDARQ-LVGYLV--SDSGLPLDTAALKARLAEQL 929
Cdd:cd17632 497 FVTVARLEAVFAASPLVRQIFVY----------GNSERAyLLAVVVptQDALAGEDTARLRAALAESL 554
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
464-952 |
4.07e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 464 QARKTPDAPAL--ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAV--------------ALPRSVFLTLALHGIVE 527
Cdd:PRK13390 6 HAQIAPDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALlsdnspealvvlwaALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 528 AGAAWLPLDTGypddrLRMMLEDARPSLLITS-----EDQLARFSDIPGLESlcYQQPLAAgddAPLALSKPDHTAYIIF 602
Cdd:PRK13390 86 PEADYIVGDSG-----ARVLVASAALDGLAAKvgadlPLRLSFGGEIDGFGS--FEAALAG---AGPRLTEQPCGAVMLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 603 TSGSTGRPKGVM-------VGQ-----TAIVNRLlwmqdrYPLSAQDVVAQKTPCSFDVSVWefWWPFI--AGAQLVMAE 668
Cdd:PRK13390 156 SSGTTGFPKGIQpdlpgrdVDApgdpiVAIARAF------YDISESDIYYSSAPIYHAAPLR--WCSMVhaLGGTVVLAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 669 peaHRDPQAMQQFFARYGVTTTHFVPSMlaaFVASLDADSVAACR----TLRRVFCSGEALPTELCREWERLTGAPLHNL 744
Cdd:PRK13390 228 ---RFDAQATLGHVERYRITVTQMVPTM---FVRLLKLDADVRTRydvsSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 745 YGPTEA----AVDVswypacgPELAAVTGSsvpIGWPVWNTgLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTA 820
Cdd:PRK13390 302 YSSTEAhgmtFIDS-------PDWLAHPGS---VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 821 -SRFIADPFapgerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMS-----------GLPDVAQAVSHA 888
Cdd:PRK13390 371 aAQHPAHPF-----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTmhpavhdvaviGVPDPEMGEQVK 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 635952396 889 CVFNQAAATGGD---ARQLVGYlvsdsglpldtaaLKARLAEQLPPHMVPVVlmqlAELPLSANGKL 952
Cdd:PRK13390 446 AVIQLVEGIRGSdelARELIDY-------------TRSRIAHYKAPRSVEFV----DELPRTPTGKL 495
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
464-957 |
6.25e-13 |
|
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: 73.36 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 464 QARKTPDAPAL------ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLAL---------HGIVEA 528
Cdd:cd05966 62 HLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMlacarigavHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 529 gaawlpldtGYPDDRLRMMLEDARPSLLITSeDQLAR--------------FSDIPGLES------------------LC 576
Cdd:cd05966 142 ---------GFSAESLADRINDAQCKLVITA-DGGYRggkviplkeivdeaLEKCPSVEKvlvvkrtggevpmtegrdLW 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 577 YQQPLA-AGDDAPLALSKPDHTAYIIFTSGSTGRPKGV-------MVGqTAIVNRllWMQDRYPlsaQDVVAqktpCSFD 648
Cdd:cd05966 212 WHDLMAkQSPECEPEWMDSEDPLFILYTSGSTGKPKGVvhttggyLLY-AATTFK--YVFDYHP---DDIYW----CTAD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 649 VSvwefwW----------PFIAGAQLVMAE-----PEAHRdpqaMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACR 713
Cdd:cd05966 282 IG-----WitghsyivygPLANGATTVMFEgtptyPDPGR----YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 714 TLRRVFCS-GEALPTELCReWerltgapLHNLYGPTEAA-VDVSWYPACG-----PeLAAVT----GSSvpiGWPVWNTG 782
Cdd:cd05966 353 SSLRVLGSvGEPINPEAWM-W-------YYEVIGKERCPiVDTWWQTETGgimitP-LPGATplkpGSA---TRPFFGIE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 783 LRILDAAMRPVPPGVAGDLYLT----GIqlAQGYLGRPDltasRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQ 858
Cdd:cd05966 421 PAILDEEGNEVEGEVEGYLVIKrpwpGM--ARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 859 LKIRGQRIELGEIDRVMSGLPDVAqavshacvfnQAAATG------GDArqLVGYLVSDSGLPLDTA---ALKARLAEQL 929
Cdd:cd05966 495 INVSGHRLGTAEVESALVAHPAVA----------EAAVVGrphdikGEA--IYAFVTLKDGEEPSDElrkELRKHVRKEI 562
|
570 580
....*....|....*....|....*...
gi 635952396 930 PPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05966 563 GPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
599-953 |
7.43e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 71.64 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 599 YIIFTSGSTGRPKGVMVGQTAIVNRLLW---MQDRYPLSAQDVVAQKT-----------PCSFDVSVWEFWWPFIAGAQL 664
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGgadFGTGEFTPSEDAHKAAAaaagtvmfpapPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 665 VMaePEAHRDPQAMQQFFARYGVTTTHFV-PSMLAAFVASLDADSVAACRTLRRVfCSGEALPTELCRE--WERLTGAPL 741
Cdd:cd05924 87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPYDLSSLFAI-SSGGALLSPEVKQglLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 742 HNLYGPTEAAVDVSWYPACGPelaAVTGSSVPIgwpvwNTGLRILDAAMRPVPPGVAGdlyltGIQLAQ------GYLGR 815
Cdd:cd05924 164 VDAFGSSETGFTGSGHSAGSG---PETGPFTRA-----NPDTVVLDDDGRVVPPGSGG-----VGWIARrghiplGYYGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 816 PDLTASRFiadPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAA 895
Cdd:cd05924 231 EAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVL----VVGRPD 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 896 ATGGdaRQLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLD 953
Cdd:cd05924 304 ERWG--QEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
480-624 |
7.68e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.73 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAG--AAWLPLDTGYPD-----DRLRMMLEDAR 552
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPLPMGFGGresyiAQLRGMLASAQ 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 553 PSLLITSEDQLARFSDI----PGLESLCYQQpLAAGDDAPLALSK--PDHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:PRK09192 129 PAAIITPDELLPWVNEAthgnPLLHVLSHAW-FKALPEADVALPRptPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
600-884 |
1.66e-12 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 70.02 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 IIFTSGSTGRPKGVMVGQTAIVNR---LLWMQDrypLSAQDVVAQKTPCsFDVSVWEFWWP-FIAGAQLVMAepeAHRDP 675
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQalvLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtFHAGGTNVFV---RRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 676 QAMQQFFARYGVTTTHFVPSMLAAFVAsLDADSVAACRTLRRVFCSGE--ALPTELCREWERLTGAplhnlYGPTEAAVD 753
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIVE-LNADGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPGG-----YGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 754 VSwYPACGPELAAVTGSSVPIgwpvwnTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfapgeR 833
Cdd:cd17636 152 AT-FAALGGGAIGGAGRPSPL------VQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------G 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 635952396 834 MYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:cd17636 218 WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADA 268
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
467-952 |
2.12e-12 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 71.75 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 467 KTPDAPAL-----ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALP---RSVFLTLALHGIveaGAAWlplDTG 538
Cdd:PRK03584 96 RRDDRPAIifrgeDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPnipETVVAMLATASL---GAIW---SSC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 539 YPD-------DRLRMMledaRPSLLITSE---------DQLARFSDI----PGLESLC---YQQPLAAGDDAPLALS--- 592
Cdd:PRK03584 170 SPDfgvqgvlDRFGQI----EPKVLIAVDgyryggkafDRRAKVAELraalPSLEHVVvvpYLGPAAAAAALPGALLwed 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 593 ---------------KPDHTAYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQDRYPLSAQDVVAQKTPCSfdvsvWEFW- 655
Cdd:PRK03584 246 flapaeaaelefepvPFDHPLWILYSSGTTGLPKCIVHGHGGILlEHLKELGLHCDLGPGDRFFWYTTCG-----WMMWn 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 656 W---PFIAGAQLVMAE--PeAHRDPQAMQQFFARYGVttTHFVPSmlAAFVASLDADSVAACRT-----LRRVFCSGEAL 725
Cdd:PRK03584 321 WlvsGLLVGATLVLYDgsP-FYPDPNVLWDLAAEEGV--TVFGTS--AKYLDACEKAGLVPGEThdlsaLRTIGSTGSPL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 726 PTE----LCREWERltGAPLHNLYGPTeaavDVswypaCGpelAAVTGssVPIgWPVW---------NTGLRILDAAMRP 792
Cdd:PRK03584 396 PPEgfdwVYEHVKA--DVWLASISGGT----DI-----CS---CFVGG--NPL-LPVYrgeiqcrglGMAVEAWDEDGRP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 793 VpPGVAGDLYLTgiqlaQ-------GYLGRPDltASRFIADPFA--PGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:PRK03584 459 V-VGEVGELVCT-----KpfpsmplGFWNDPD--GSRYRDAYFDtfPG--VWRHGDWIEITEHGGVVIYGRSDATLNRGG 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 864 QRIELGEIDRVMSGLPDVAQAVshacVFNQAAAtGGDARqLVGYLVSDSGLPLD---TAALKARLAEQLPPHMVPVVLMQ 940
Cdd:PRK03584 529 VRIGTAEIYRQVEALPEVLDSL----VIGQEWP-DGDVR-MPLFVVLAEGVTLDdalRARIRTTIRTNLSPRHVPDKIIA 602
|
570
....*....|..
gi 635952396 941 LAELPLSANGKL 952
Cdd:PRK03584 603 VPDIPRTLSGKK 614
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
469-874 |
3.85e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 70.39 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARW--QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRM 546
Cdd:PLN02246 37 SDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 547 MLEDARPSLLITSE---DQLARFSDIPGLESLCYQQP---------LAAGDDAPLALSK--PDHTAYIIFTSGSTGRPKG 612
Cdd:PLN02246 117 QAKASGAKLIITQScyvDKLKGLAEDDGVTVVTIDDPpegclhfseLTQADENELPEVEisPDDVVALPYSSGTTGLPKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 613 VMVGQTAIVNRLLWMQD----RYPLSAQDVVAQKTP------------CSFDVsvwefwwpfiAGAQLVMAEPEAhrdpQ 676
Cdd:PLN02246 197 VMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPmfhiyslnsvllCGLRV----------GAAILIMPKFEI----G 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 677 AMQQFFARYGVTTTHFVPSMLAAF-----VASLDADSVaacrtlrRVFCSGEAlPteLCREWE-----RLTGAPLHNLYG 746
Cdd:PLN02246 263 ALLELIQRHKVTIAPFVPPIVLAIakspvVEKYDLSSI-------RMVLSGAA-P--LGKELEdafraKLPNAVLGQGYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 747 PTEAavdvswypacGPELA---AVTGSSVPI-----GWPVWNTGLRILDAAM-RPVPPGVAGDLYLTGIQLAQGYLGRPD 817
Cdd:PLN02246 333 MTEA----------GPVLAmclAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPE 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 635952396 818 LTAsrfiadpfapgermyRTGDVARWLTNGAVEYLGRsDDQLKIrgqrielgeIDRV 874
Cdd:PLN02246 403 ATA---------------NTIDKDGWLHTGDIGYIDD-DDELFI---------VDRL 434
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
482-881 |
4.98e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 70.02 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLED--ARPSLLits 559
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDtlRVIGMI--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 EDQLARFSD-----IPGLESLCYQ----QPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDR 630
Cdd:PRK07768 108 GAKAVVVGEpflaaAPVLEEKGIRvltvADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 631 YPLSAQ-DVVAQKTPCSFDVSVWEFWW-PFIAGAQLVMAEP-EAHRDPQAMQQFFARYGVTTT---HFVPSMLAAFVASL 704
Cdd:PRK07768 188 AEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPmDFLRDPLLWAELISKYRGTMTaapNFAYALLARRLRRQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 705 DADSVAACRTLRRVFCSGEAL-PTELcrewERLT--GAPlHNL--------YGPTEAAVDVSwYPACG---------PEL 764
Cdd:PRK07768 268 AKPGAFDLSSLRFALNGAEPIdPADV----EDLLdaGAR-FGLrpeailpaYGMAEATLAVS-FSPCGaglvvdevdADL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 765 AAVTGSSVP-----------IGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYlgrpdLTASRFIADPFAPGer 833
Cdd:PRK07768 342 LAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPAQDADG-- 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 635952396 834 MYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDV 881
Cdd:PRK07768 415 WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
831-959 |
6.51e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 69.29 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 831 GERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdarQLVGYLVS 910
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAV----VYRGKDPVAG---ERVKAKVI 361
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 635952396 911 DSGlPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKALPL 959
Cdd:PRK08308 362 SHE-EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
595-957 |
6.89e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.53 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 595 DHTAYIIFTSGSTGRPKGVMVGQTAIV--------------NRLLWMQDRYPLSAQ----DVVAQKTPCSFDVSVwEFWW 656
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTasadathdrlggpgQWLLALPAHHIAGLQvlvrSVIAGSEPVELDVSA-GFDP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 657 PFIAGAQLVMAEPEahrdpqamqqffaRYgvttTHFVPSMLAAFVASLDAdsVAACRTLRRVFCSGEALPTELCREWERL 736
Cdd:PRK07824 114 TALPRAVAELGGGR-------------RY----TSLVPMQLAKALDDPAA--TAALAELDAVLVGGGPAPAPVLDAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 737 tGAPLHNLYGPTEAAvdvswypacgpelaavtGSSVPIGWPVWNTGLRILDaamrpvppgvaGDLYLTGIQLAQGYLGRP 816
Cdd:PRK07824 175 -GINVVRTYGMSETS-----------------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 817 DltasrfiADPFA-PGerMYRTGDVARwLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPdvaqAVSHACVFNQAa 895
Cdd:PRK07824 226 D-------PDPFAePG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHP----AVADCAVFGLP- 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 896 atggDAR--QLVGYLVSDSGLPLDT-AALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:PRK07824 291 ----DDRlgQRVVAAVVGDGGPAPTlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
599-954 |
1.30e-11 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 67.43 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 599 YIIFTSGSTGRPKGVMVGQTAivnrllWM------QDRYPLSAQDVVAQKTPCSFDVSVWEFWWPFIAGAQLVMaepEAH 672
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERS------WIesfvcnEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 673 RDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSvaacrTLRRVFCSGEALPTELCREWERltGAPLHNL---YGPTE 749
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALARTLEPES-----KIKSIFSSGQKLFESTKKKLKN--IFPKANLiefYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 750 AavdvSWYPACGPELAAVTGSsvpIGWPVWNTGLRILDAAmrpvpPGVAGDLYLTGIQLAQGYLGRPDLTASRFiadpfa 829
Cdd:cd17633 148 L----SFITYNFNQESRPPNS---VGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 830 pgermYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVshacVFNQAAATGGdarQLVGYLV 909
Cdd:cd17633 210 -----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI----VVGIPDARFG---EIAVALY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 635952396 910 sdSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDR 954
Cdd:cd17633 278 --SGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
469-957 |
1.31e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 68.82 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPAL------ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALP---RSVFLTL------ALHGIVEAGAAWL 533
Cdd:PRK10524 67 PEQLALiavsteTDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPmiaEAAFAMLacarigAIHSVVFGGFASH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 534 PLDTgypddrlRMmlEDARPSLLITSE---------------DQ------------------LARFSDIPGLEsLCYQQP 580
Cdd:PRK10524 147 SLAA-------RI--DDAKPVLIVSADagsrggkvvpykpllDEaialaqhkprhvllvdrgLAPMARVAGRD-VDYATL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 581 LA--AGDDAPLALSKPDHTAYIIFTSGSTGRPKGVM--VGQTAiVNRLLWMQDRYPLSAQDVVAqktpCSFDVSvwefwW 656
Cdd:PRK10524 217 RAqhLGARVPVEWLESNEPSYILYTSGTTGKPKGVQrdTGGYA-VALATSMDTIFGGKAGETFF----CASDIG-----W 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 657 ----------PFIAGAQLVMAEPEAHR-DPQAMQQFFARYGVTTTHFVPSML-------AAFVASLDADSvaacrtLRRV 718
Cdd:PRK10524 287 vvghsyivyaPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTAIrvlkkqdPALLRKHDLSS------LRAL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 719 FCSGEAL--PTElcrEW--ERLtGAPLHNLYGPTEAAvdvsWypacgPELAAVTG-SSVPI-----GWPVWNTGLRILDA 788
Cdd:PRK10524 361 FLAGEPLdePTA---SWisEAL-GVPVIDNYWQTETG----W-----PILAIARGvEDRPTrlgspGVPMYGYNVKLLNE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 789 AM-RPVPPGVAGDLYLTGiQLAQGYLG---RPDltaSRFIADPF-APGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:PRK10524 428 VTgEPCGPNEKGVLVIEG-PLPPGCMQtvwGDD---DRFVKTYWsLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAG 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 864 QRIELGEIDRVMSGLPDVAQAvshACVFNQAAATGGDArqlVGYLVSDSGLPLDTAALKARLAEQL------------PP 931
Cdd:PRK10524 504 HRLGTREIEESISSHPAVAEV---AVVGVKDALKGQVA---VAFVVPKDSDSLADREARLALEKEImalvdsqlgavaRP 577
|
570 580
....*....|....*....|....*.
gi 635952396 932 HMVPVVLMqlaeLPLSANGKLDRKAL 957
Cdd:PRK10524 578 ARVWFVSA----LPKTRSGKLLRRAI 599
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
600-954 |
1.35e-11 |
|
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: 67.29 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 IIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTP------CSFDVSVwefwwpFIAGAQLVMAEpeaHR 673
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPlfhiagLNLALAT------FHAGGANVVME---KF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 674 DPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVfcSGEALPtELCREWERLTGAPLHNLYGPTEAAVD 753
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDL-SSLRHV--LGLDAP-ETIQRFEETTGATFWSLYGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 754 VSWYPAcgpelAAVTGSSvpiGWPVWNTGLRILDAAMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapger 833
Cdd:cd17637 152 VTLSPY-----RERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 834 MYRTGDVARWLTNGAVEYLGRS--DDQLKIRGQRIELGEIDRVMSGLPDVAQavshACVFNQAAATGGDARQLVgyLVSD 911
Cdd:cd17637 217 WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAE----VCVIGVPDPKWGEGIKAV--CVLK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 635952396 912 SGLPLDTAAL----KARLAEQLPPHMVPVVlmqlAELPLSANGKLDR 954
Cdd:cd17637 291 PGATLTADELiefvGSRIARYKKPRYVVFV----EALPKTADGSIDR 333
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-244 |
1.68e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.43 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 24 PGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGevwQWVAADRTFGEPSIidLRTAPDPHRAATERMQA 103
Cdd:PRK05691 2809 PQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADG---RWQAEYRAVTAQEL--LWQVTVADFAECAALFA 2883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 104 DLAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGEATPESPFT-PFAEVVDEYQ 182
Cdd:PRK05691 2884 DAQRSLDLQQG-PLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTsAFRDWAARLQ 2962
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 183 RYAGSEAWQRDKAFWQAQ----RQALPspaslsaaplGGRAAGSDIWR----MKLEMNADAFRRLAGHAP 244
Cdd:PRK05691 2963 AYAGSESLREELGWWQAQlggpRAELP----------CDRPQGGNLNRhaqtVSVRLDAERTRQLLQQAP 3022
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
15-245 |
1.87e-11 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 67.66 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 15 WMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFGEP-SIIDLRTAPDP 93
Cdd:cd19534 10 WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRlEVVDLSSLAQA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 94 H--RAATERMQADLaqDLRvDGgnPLVCHQLLRVGDDRwywyQRY----HHLLVDGFSFPAITRQIAAIYRAWQRGEATP 167
Cdd:cd19534 90 AaiEALAAEAQSSL--DLE-EG--PLLAAALFDGTDGG----DRLllviHHLVVDGVSWRILLEDLEAAYEQALAGEPIP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635952396 168 ESPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAgsdiwRMKLEMNADAFRRLAGHAPQ 245
Cdd:cd19534 161 LPSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGDAR-----TVSFTLDEEETEALLQEANA 233
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
482-884 |
2.52e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 67.85 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGA--------------AWLpldTGYPDDRLRM- 546
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAichtvnprlfpeqiAWI---INHAEDRVVIt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 547 ------MLE---DARPSL----LITSEDQLARfSDIPGLesLCYQQPLAAGD-DAPLALSKPDHTAYIIFTSGSTGRPKG 612
Cdd:PRK06018 118 dltfvpILEkiaDKLPSVeryvVLTDAAHMPQ-TTLKNA--VAYEEWIAEADgDFAWKTFDENTAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 613 VM------VGQTAIVNrllwMQDRYPLSAQDVVAQKTPCsFDVSVW--EFWWPFIaGAQLVMaePEAHRDPQAMQQFFAR 684
Cdd:PRK06018 195 VLyshrsnVLHALMAN----NGDALGTSAADTMLPVVPL-FHANSWgiAFSAPSM-GTKLVM--PGAKLDGASVYELLDT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 685 YGVTTTHFVPSMLAAFVASLDADSvAACRTLRRVFCSGEALPTELCREWERLTGAPLHnLYGPTEAAvDVSWYPACGPEL 764
Cdd:PRK06018 267 EKVTFTAGVPTVWLMLLQYMEKEG-LKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRH-AWGMTEMS-PLGTLAALKPPF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 765 AAVTGSS-----VPIGWPVWNTGLRILDAAMRPVP-PGVA-GDLYLTGIQLAQGYLGrpdLTASRFIADPFapgermYRT 837
Cdd:PRK06018 344 SKLPGDArldvlQKQGYPPFGVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYYR---VDGEILDDDGF------FDT 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 635952396 838 GDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:PRK06018 415 GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
481-957 |
6.09e-11 |
|
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: 66.30 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREMRQQVVALAQLLR-QRGVKPGDSVAVALPRS---VFLTLALHGIveaGAAWLPLDTGYPDDRLRMMLEDARPSLL 556
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSpefVFLWLGLWSI---GAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 557 ItsedqlarfsdipgleslcyqqplaagddaplalSKPDHTAYIIFTSGSTGRPKGVmvgqtAIVNRLLWM--------- 627
Cdd:cd05937 83 I----------------------------------VDPDDPAILIYTSGTTGLPKAA-----AISWRRTLVtsnllshdl 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 628 ----QDRY----PL---------SAQDVVAQKTPC-SFDVSVWEFWwpfiagaqlvmaePEAHrDPQAmqqffarygvtt 689
Cdd:cd05937 124 nlknGDRTytcmPLyhgtaaflgACNCLMSGGTLAlSRKFSASQFW-------------KDVR-DSGA------------ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 690 THFVpsmlaaFVASLdadsvaaCRTL-----------RRVFCS-GEALPTELcreWERLT---GAP-LHNLYGPTEAaVD 753
Cdd:cd05937 178 TIIQ------YVGEL-------CRYLlstppspydrdHKVRVAwGNGLRPDI---WERFRerfNVPeIGEFYAATEG-VF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 754 VSWYPACGPELAAVTGSSVPIGWPVWNTGLRIL-------DAAMRP-------VPPGVAGD----LYLTGIQLAQGYLGR 815
Cdd:cd05937 241 ALTNHNVGDFGAGAIGHHGLIRRWKFENQVVLVkmdpetdDPIRDPktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHN 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 816 PDLTASRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHACvfnQAA 895
Cdd:cd05937 321 EDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGV---KVP 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635952396 896 ATGGDARQLVGYLVSDSGLP--LDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLDRKAL 957
Cdd:cd05937 398 GHDGRAGCAAITLEESSAVPteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
452-968 |
7.99e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.19 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 452 LPATTLSALVaDQARKTPDAPAL--ADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAG 529
Cdd:PRK05857 12 LPSTVLDRVF-EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 530 AAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAPLALSKPDhTAY---------- 599
Cdd:PRK05857 91 AIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLD-AASlagnadqgse 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 ----IIFTSGSTGRPKGVMvgqtaIVNRLLW----MQDRYPLSAQDVVAQKTPCS--FDVSVWEFWW---PFIAGAQLVM 666
Cdd:PRK05857 170 dplaMIFTSGTTGEPKAVL-----LANRTFFavpdILQKEGLNWVTWVVGETTYSplPATHIGGLWWiltCLMHGGLCVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 667 AEPEAhrdpQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAAcRTLRRVFCSGEALPTELCREWERlTGAPLHNLYG 746
Cdd:PRK05857 245 GGENT----TSLLEILTTNAVATTCLVPTLLSKLVSELKSANATV-PSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 747 PTEAAVDVSWYPACGPELAAVTGSSVPIGWPVWNTGLRILDAAmRPVPPGVA-----GDLYLTGIQLAQGYLGRPDLTAS 821
Cdd:PRK05857 319 LSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGI-GPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 822 RFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAvshACVFNQAAATGGda 901
Cdd:PRK05857 398 VLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA---ACYEIPDEEFGA-- 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635952396 902 rqLVGYLVSDSGlPLD---TAALKARLA----EQLPPHMVPVVLMQLAELPLSANGKLDRKALPlPTLGGERSG 968
Cdd:PRK05857 466 --LVGLAVVASA-ELDesaARALKHTIAarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASLA-AAATADKAR 535
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
575-952 |
1.11e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 65.88 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 575 LCYQQPLAAGDDAPLALSKPDHTA-YIIFTSGSTGRPKGVMVGQTAIVNRLLW--MQDRYPLSAQDVVAQKTPCsFDVSV 651
Cdd:PRK07008 155 LCYETLVGAQDGDYDWPRFDENQAsSLCYTSGTTGNPKGALYSHRSTVLHAYGaaLPDAMGLSARDAVLPVVPM-FHVNA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 652 WEFwwPFIA---GAQLVMaePEAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACrTLRRVFCSGEALPTE 728
Cdd:PRK07008 234 WGL--PYSApltGAKLVL--PGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFS-TLRRTVIGGSACPPA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 729 LCREWERLTGAPLHNLYGPTEAA-----VDVSWYPACGPElAAVTGSSVPIGWPVWNTGLRILDAAMRPVP-PGVA-GDL 801
Cdd:PRK07008 309 MIRTFEDEYGVEVIHAWGMTEMSplgtlCKLKWKHSQLPL-DEQRKLLEKQGRVIYGVDMKIVGDDGRELPwDGKAfGDL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 802 YLTGIQLAQGYLGRPdltasrfiADPFAPGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDV 881
Cdd:PRK07008 388 QVRGPWVIDRYFRGD--------ASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAV 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 882 AQAvshACVfnQAAATGGDARQLVgYLVSDSGLPLDTAALKA----RLAE-QLPPHMVPVvlmqlAELPLSANGKL 952
Cdd:PRK07008 458 AEA---ACI--ACAHPKWDERPLL-VVVKRPGAEVTREELLAfyegKVAKwWIPDDVVFV-----DAIPHTATGKL 522
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1062-1156 |
1.71e-10 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 62.56 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1062 RESDGPTLFCFHPASGFAWQFSVLARYLSPRWSITGIQSP----RPQGPMASaaSLDEVCEHHLRTLLAQqPHGPYYLFG 1137
Cdd:COG3208 2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPgrgdRLGEPPLT--SLEELADDLAEELAPL-LDRPFALFG 78
|
90
....*....|....*....
gi 635952396 1138 YSLGGTLAQGIAARLRQRG 1156
Cdd:COG3208 79 HSMGALLAFELARRLERRG 97
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
456-863 |
2.46e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 64.58 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 456 TLSALVADQARKTPDAPALA----DARWQ-----FSYREMRQQVVALAQLLRQRGVkPGDSVAVALPRSVFLTLALHGIV 526
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAgvaetLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 527 EAGAAWLPLDT---GYPDDRLRMMLEDARPSLLITS---EDQLARFSDIPGLESlcyqQP---------LAAGDDAPLAL 591
Cdd:PRK05850 81 QAGLIAVPLSVpqgGAHDERVSAVLRDTSPSVVLTTsavVDDVTEYVAPQPGQS----APpvievdlldLDSPRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 592 SKPDHTAYIIFTSGSTGRPKGVMVG-QTAIVNRLLWMQDRYPlsAQDVVAqkTPCSFDVSvwefWWPF------IAG--A 662
Cdd:PRK05850 157 RDLPSTAYLQYTSGSTRTPAGVMVShRNVIANFEQLMSDYFG--DTGGVP--PPDTTVVS----WLPFyhdmglVLGvcA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 663 QLVMAEPEAHRDPQAMQQFFARYgvttTHFVPSMLAAFVASLD-ADSVAACRT---------LRRV--FCSGEalptelc 730
Cdd:PRK05850 229 PILGGCPAVLTSPVAFLQRPARW----MQLLASNPHAFSAAPNfAFELAVRKTsdddmagldLGGVlgIISGS------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 731 rewERLTGAPLH---------NL--------YGPTEAAVDVSWYPACGP---------ELAA------VTGSSVPI---G 775
Cdd:PRK05850 298 ---ERVHPATLKrfadrfapfNLretairpsYGLAEATVYVATREPGQPpesvrfdyeKLSAghakrcETGGGTPLvsyG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 776 WPvWNTGLRILDA-AMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRF---IADPFA--PGERMYRTGDVArWLTNGAV 849
Cdd:PRK05850 375 SP-RSPTVRIVDPdTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDLG-FISEGEL 452
|
490
....*....|....
gi 635952396 850 EYLGRSDDQLKIRG 863
Cdd:PRK05850 453 FIVGRIKDLLIVDG 466
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
447-637 |
2.78e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 64.45 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 447 DTVVPLPATTLSALVADQARKTPDAPAL----ADARWqfSYREMRQQVVALAQLLRQRGVKPGDSVAVALP--------- 513
Cdd:PRK08315 8 PTDVPLLEQTIGQLLDRTAARYPDREALvyrdQGLRW--TYREFNEEVDALAKGLLALGIEKGDRVGIWAPnvpewvltq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 514 -----------------RSVFLTLALHgivEAGAAWLPLDTGYPDDRLRMMLEDARPSLLiTSEDQLARFSDIPGLESLC 576
Cdd:PRK08315 86 fatakigailvtinpayRLSELEYALN---QSGCKALIAADGFKDSDYVAMLYELAPELA-TCEPGQLQSARLPELRRVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 577 Y------------QQPLAAG---DDAPLA-----LSkPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQ 636
Cdd:PRK08315 162 FlgdekhpgmlnfDELLALGravDDAELAarqatLD-PDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEE 240
|
.
gi 635952396 637 D 637
Cdd:PRK08315 241 D 241
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
587-953 |
2.87e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.99 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 587 APLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPC--SFDVSVwEFWWPFIAGAQL 664
Cdd:PRK06814 785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 665 VM-AEPEAHRD-PQAMQQFFARYGVTTTHFvpsmLAAFVASLDADSVaacRTLRRVFCSGEALPTELCREWERLTGAPLH 742
Cdd:PRK06814 864 FLyPSPLHYRIiPELIYDTNATILFGTDTF----LNGYARYAHPYDF---RSLRYVFAGAEKVKEETRQTWMEKFGIRIL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 743 NLYGPTEAAvdvswypacgPELAAVTgssvpigwPVWN---TGLRIL---DAAMRPVPpGV--AGDLYLTGIQLAQGYLg 814
Cdd:PRK06814 937 EGYGVTETA----------PVIALNT--------PMHNkagTVGRLLpgiEYRLEPVP-GIdeGGRLFVRGPNVMLGYL- 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 815 RPDltasrfiadpfAPG------ERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGL-PDVAQAvsh 887
Cdd:PRK06814 997 RAE-----------NPGvleppaDGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHA--- 1062
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 888 acvfnqaAATGGDAR---QLVgyLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSANGKLD 953
Cdd:PRK06814 1063 -------AVSIPDARkgeRII--LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
979-1035 |
3.99e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.80 E-value: 3.99e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 635952396 979 VATAFSQLLGCEVNDI--DADFFALGGHSLLAMRLAAQLSRQLARQVTPGQVMVASTVG 1035
Cdd:pfam00550 3 LRELLAEVLGVPAEEIdpDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
478-638 |
1.05e-09 |
|
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: 62.62 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 478 RWQfSYREMRQQVVALAQLLRQRGVK--PGDSVAVALPRSVFLTLALHGIVEAGAAWLPL-DTGYPDDrLRMMLEDARPS 554
Cdd:cd05927 4 EWI-SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLyDTLGPEA-IEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 555 LLITSedqlarfsdiPGLESLCYQQPLAAGDDAPLALS--KPDHTAYIIFTSGSTGRPKGVMVGQTAIVN---RLLW-MQ 628
Cdd:cd05927 82 IVFCD----------AGVKVYSLEEFEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvaGVFKiLE 151
|
170
....*....|
gi 635952396 629 DRYPLSAQDV 638
Cdd:cd05927 152 ILNKINPTDV 161
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1074-1193 |
1.33e-09 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 59.55 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1074 PASGfAWQFSVLARYLSPRWSITGIQSP--RPQGPMAsaASLDEVCEHHLRTLLAQQPHGPYYLFGYSLGGTLAQGIAAR 1151
Cdd:smart00824 8 APSG-PHEYARLAAALRGRRDVSALPLPgfGPGEPLP--ASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVAAR 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 635952396 1152 LRQRGEAVAFLGLLDTWPPETQNwAEKEANGLDPEVLAEIDR 1193
Cdd:smart00824 85 LEARGIPPAAVVLLDTYPPGDPA-PEGWLPELLRGVFEREDS 125
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-244 |
2.27e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 27 WSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGevwQWVAADRTFGEPSIIDLRTAPDPHRAATERM--QAD 104
Cdd:PRK12467 2201 WNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDG---GWSAMHRAPEQERRPLLWQVVVADKEELEALceQAQ 2277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 105 LAQDLrvdGGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGEA----TPESPFTPFAEVVde 180
Cdd:PRK12467 2278 RSLDL---EEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPvklpAKTSAFKAWAERL-- 2352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635952396 181 yQRYAGSEAWQRDKAFWQAQRQALPS--PASLSAAPLGGRAAGSdiwrMKLEMNADAFRRLAGHAP 244
Cdd:PRK12467 2353 -QTYAASAALADELGYWQAQLQGASTelPCDHPQGGLQRRHAAS----VTTHLDSEWTRRLLQEAP 2413
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
4-210 |
6.33e-09 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 59.97 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFgEPS 83
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSF-HLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 IIDLRTAPDPHRAATERMQADLAQDLRVDGGNPLVChQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAW--Q 161
Cdd:cd20483 80 VIDLSEAADPEAALDQLVRNLRRQELDIEEGEVIRG-WLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALraG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 635952396 162 RGEATPESPFTPFAEVVDEYQRYAGSEAWQRDKAFWQAQRQALPSPASL 210
Cdd:cd20483 159 RDLATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKL 207
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
469-957 |
1.05e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 59.65 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 469 PDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMML 548
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 549 EDARP-----------------SLLITSEDQL---------ARFSDIPGLESLCYQQPLAAGDDAPLALSK-----PDHT 597
Cdd:PLN03102 108 RHAKPkilfvdrsfeplarevlHLLSSEDSNLnlpvifiheIDFPKRPSSEELDYECLIQRGEPTPSLVARmfriqDEHD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 598 AYII-FTSGSTGRPKGVMVGQ-----TAIVNRLLWMQDRYPlsaqdvVAQKTPCSFDVSVWEFWWPFIA--GAQLVM--- 666
Cdd:PLN03102 188 PISLnYTSGTTADPKGVVISHrgaylSTLSAIIGWEMGTCP------VYLWTLPMFHCNGWTFTWGTAArgGTSVCMrhv 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 667 AEPEAHRDPQAmqqffarYGVTTTHFVPSMLAaFVASLDADSVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNlYG 746
Cdd:PLN03102 262 TAPEIYKNIEM-------HNVTHMCCVPTVFN-ILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHA-YG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 747 PTEAavdvswypacgpelaavTGSSVPIGWP-VWN-------------TGLRILDAA---------MRPVPPG--VAGDL 801
Cdd:PLN03102 333 LTEA-----------------TGPVLFCEWQdEWNrlpenqqmelkarQGVSILGLAdvdvknketQESVPRDgkTMGEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 802 YLTGIQLAQGYLGRPDLTASRFiadpfapGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDV 881
Cdd:PLN03102 396 VIKGSSIMKGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 882 AQAVSHA----------CVFNQAAATGGDARQLVGYLVSDSGlpldtaALKARLAEQLPPHMVPVVLMQLAELPLSANGK 951
Cdd:PLN03102 469 LETAVVAmphptwgetpCAFVVLEKGETTKEDRVDKLVTRER------DLIEYCRENLPHFMCPRKVVFLQELPKNGNGK 542
|
....*.
gi 635952396 952 LDRKAL 957
Cdd:PLN03102 543 ILKPKL 548
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
479-957 |
1.30e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.09 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 479 WQFSYREMRQqvvaLAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGA--------------AWL---------PL 535
Cdd:PLN02479 48 WAQTYQRCRR----LASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAvvncvnirlnaptiAFLlehsksevvMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DTGY---PDDRLRMMLEDA----RPSLLITSEDQLAR---FSDIPGLESLCYQQPLAAGDDApLALSKPDHTAYII---F 602
Cdd:PLN02479 124 DQEFftlAEEALKILAEKKkssfKPPLLIVIGDPTCDpksLQYALGKGAIEYEKFLETGDPE-FAWKPPADEWQSIalgY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 603 TSGSTGRPKGVMVGQ-----TAIVNRLLW-MQDryplsaqDVVAQKTPCSFDVSVWEFWWPFIA--GAQLVMAEPEAhrd 674
Cdd:PLN02479 203 TSGTTASPKGVVLHHrgaylMALSNALIWgMNE-------GAVYLWTLPMFHCNGWCFTWTLAAlcGTNICLRQVTA--- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 675 pQAMQQFFARYGVttTHF--VPSMLAAFVASLDADSVAACRTLRRVFCSGEALPTELCREWE----RLTGA-PLHNLYGP 747
Cdd:PLN02479 273 -KAIYSAIANYGV--THFcaAPVVLNTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFAMSekgfRVTHTyGLSETYGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 748 TEAAvdvSWYPACGpELAAVTGSSVPIGWPVWNTGLRILDA----AMRPVPP--GVAGDLYLTGIQLAQGYLGRPDLTas 821
Cdd:PLN02479 350 STVC---AWKPEWD-SLPPEEQARLNARQGVRYIGLEGLDVvdtkTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKAN-- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 822 rfiADPFAPGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA--VSHA--------CVF 891
Cdd:PLN02479 424 ---EEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAsvVARPderwgespCAF 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 892 N--QAAATGGDARQLVGYLVSDSglpldtaalkarlAEQLPPHMVP--VVlmqLAELPLSANGKLDRKAL 957
Cdd:PLN02479 499 VtlKPGVDKSDEAALAEDIMKFC-------------RERLPAYWVPksVV---FGPLPKTATGKIQKHVL 552
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
479-857 |
1.35e-08 |
|
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: 58.97 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 479 WQ-FSYREMRQQVVALAQLLRQRGVKPGDSVAVA---LPRSVFLTLALHGIveaGAAWLPLDTGYPDDRLRMMLEDARPS 554
Cdd:cd17641 9 WQeFTWADYADRVRAFALGLLALGVGRGDVVAILgdnRPEWVWAELAAQAI---GALSLGIYQDSMAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 555 LLITS-EDQLARF----SDIPGLESLCYQQP-----------------LAAGD----------DAPLALSKPDHTAYIIF 602
Cdd:cd17641 86 VVIAEdEEQVDKLleiaDRIPSVRYVIYCDPrgmrkyddprlisfedvVALGRaldrrdpglyEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 603 TSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQD----------------VVAQKTPCSFDVS---------------- 650
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDeyvsvlplpwigeqmySVGQALVCGFIVNfpeepetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 651 ---------VWEfwwpfiAGAQLVMAEPEahrDPQAMQQFFARYGV--------TTTHFVPSMLAAFVASLDADSVAA-- 711
Cdd:cd17641 246 ptfvllpprVWE------GIAADVRARMM---DATPFKRFMFELGMklglraldRGKRGRPVSLWLRLASWLADALLFrp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 712 ------CRTLRRVFCSGEALPTELCREWERLtGAPLHNLYGPTEAAVDVSWYPAcgpelAAVTGSSVpiGWPVWNTGLRI 785
Cdd:cd17641 317 lrdrlgFSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRD-----GDVDPDTV--GVPFPGTEVRI 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635952396 786 LDaamrpvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLTNGAVEYLGRSDD 857
Cdd:cd17641 389 DE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKD 444
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
975-1046 |
2.07e-08 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 52.55 E-value: 2.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 975 METLVATAFSQLLGCEVNDI--DADFFA-LGGHSLLAMRLAAQLSRQLARQVTPGQVMVASTVGKLSALLAADLS 1046
Cdd:COG0236 6 LEERLAEIIAEVLGVDPEEItpDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
438-884 |
2.84e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 58.03 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 438 ELARLAAvndTVVPLpaTTLSALvADQARKTPDAPALADARWQFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVF 517
Cdd:PRK08162 7 GLDRNAA---NYVPL--TPLSFL-ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 518 LTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS----------------------EDQLARFSDIPGLESL 575
Cdd:PRK08162 81 MVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDtefaevarealallpgpkplviDVDDPEYPGGRFIGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 576 CYQQPLAAGdDAPLALSKPDHTAYII---FTSGSTGRPKGVMVGQ-----TAIVNRLLWMQDRYPlsaqdvVAQKTPCSF 647
Cdd:PRK08162 161 DYEAFLASG-DPDFAWTLPADEWDAIalnYTSGTTGNPKGVVYHHrgaylNALSNILAWGMPKHP------VYLWTLPMF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 648 DVSVWEFWW--PFIAGAQLVMaepeahR--DPQAMQQFFARYGVttTHF-----VPSMLaafvASLDADSVAACRTLRRV 718
Cdd:PRK08162 234 HCNGWCFPWtvAARAGTNVCL------RkvDPKLIFDLIREHGV--THYcgapiVLSAL----INAPAEWRAGIDHPVHA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 719 FCSGEALPTELCREWERLtGAPLHNLYGPTE----AAV---DVSWYPACGPELAAVTG-SSVPigWPVwNTGLRILDAA- 789
Cdd:PRK08162 302 MVAGAAPPAAVIAKMEEI-GFDLTHVYGLTEtygpATVcawQPEWDALPLDERAQLKArQGVR--YPL-QEGVTVLDPDt 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 790 MRPVPPG--VAGDLYLTGIQLAQGYLGRPDLTasrfiADPFAPGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIE 867
Cdd:PRK08162 378 MQPVPADgeTIGEIMFRGNIVMKGYLKNPKAT-----EEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENIS 450
|
490
....*....|....*..
gi 635952396 868 LGEIDRVMSGLPDVAQA 884
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVA 467
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
870-951 |
3.69e-08 |
|
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: 51.78 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 870 EIDRVMSGLPDVAQAvshaCVFNQAAATGGDArqLVGYLVSDSGLPLDTAALKARLAEQLPPHMVPVVLMQLAELPLSAN 949
Cdd:pfam13193 1 EVESALVSHPAVAEA----AVVGVPDELKGEA--PVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74
|
..
gi 635952396 950 GK 951
Cdd:pfam13193 75 GK 76
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
482-890 |
4.54e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 57.46 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAVALPRS---VFLTLA------LHGIVEAgaawlpldtGYPDDRLRMMLEDAR 552
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIpeaAVAMLAcarigaVHSVVFG---------GFSAEALADRIIDAG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 553 PSLLITSEDQLAR-------------FSDIPGLES-LCYQQ-----PLAAG-----DDApLALSKPDHTA---------Y 599
Cdd:PRK00174 171 AKLVITADEGVRGgkpiplkanvdeaLANCPSVEKvIVVRRtggdvDWVEGrdlwwHEL-VAGASDECEPepmdaedplF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 IIFTSGSTGRPKGVmVGQTA--IVNRLLWMQDRYPLSAQDVVAqktpCSFDVSvwefwW----------PFIAGAQLVMA 667
Cdd:PRK00174 250 ILYTSGSTGKPKGV-LHTTGgyLVYAAMTMKYVFDYKDGDVYW----CTADVG-----WvtghsyivygPLANGATTLMF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 668 E-----PEAHRdpqaMQQFFARYGVTTTHFVPSmlaafvasldadsvaACRTLRRvfcSGEALPTELCREWERLTGA--- 739
Cdd:PRK00174 320 EgvpnyPDPGR----FWEVIDKHKVTIFYTAPT---------------AIRALMK---EGDEHPKKYDLSSLRLLGSvge 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 740 PLHnlygPtEAAVdvsWYpacgpeLAAVTGSSVPIG--WpvWNT---GLRI--LDAAMrPVPPGVAGdLYLTGIQLA--- 809
Cdd:PRK00174 378 PIN----P-EAWE---WY------YKVVGGERCPIVdtW--WQTetgGIMItpLPGAT-PLKPGSAT-RPLPGIQPAvvd 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 810 ----------QGYL--------------GRPDltasRFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQR 865
Cdd:PRK00174 440 eegnpleggeGGNLvikdpwpgmmrtiyGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHR 515
|
490 500
....*....|....*....|....*
gi 635952396 866 IELGEIDRVMSGLPDVAQAvshACV 890
Cdd:PRK00174 516 LGTAEIESALVAHPKVAEA---AVV 537
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
603-882 |
7.94e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 56.31 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 603 TSGSTGRPKGVmvGQTA--------IVNRLLWMQDrypLSAQDVVaQKTPcSFDvsvweFW---WPFIAGAQLV--MAEP 669
Cdd:COG1541 91 SSGTTGKPTVV--GYTRkdldrwaeLFARSLRAAG---VRPGDRV-QNAF-GYG-----LFtggLGLHYGAERLgaTVIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 670 EAHRDPQAMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRT-LRRVFCSGEALPTELCREWERLTGAPLHNLYGPT 748
Cdd:COG1541 159 AGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLsLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 749 EAAVDVSWypacgpELAAVTGssvpigwPVWNTGLR---ILD-AAMRPVPPGVAGDLYLTGiqlaqgyLGRpdltasrfi 824
Cdd:COG1541 239 EVGPGVAY------ECEAQDG-------LHIWEDHFlveIIDpETGEPVPEGEEGELVVTT-------LTK--------- 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635952396 825 adpfapgERM----YRTGDVARWL--------TNGAVEY-LGRSDDQLKIRGQRIELGEIDRVMSGLPDVA 882
Cdd:COG1541 290 -------EAMplirYRTGDLTRLLpepcpcgrTHPRIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVG 353
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
6-207 |
8.39e-08 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 56.31 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 6 PLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRF--EEEEGEVWQWVAADrtfgepS 83
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLAS------S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 IIDLRTAPDPHRA----ATERMQA---DLAQD--LRVdggnplvchQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIA 154
Cdd:cd19532 77 PLRLEHVQISDEAeveeEFERLKNhvyDLESGetMRI---------VLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 635952396 155 AIYRawQRGEATPESPFTPFAevvdEYQRYA-GSEAWQRDKAFWQAQRQALPSP 207
Cdd:cd19532 148 RAYN--GQPLLPPPLQYLDFA----ARQRQDyESGALDEDLAYWKSEFSTLPEP 195
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
476-629 |
2.45e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.12 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 476 DARW-QFSYReMRqqvvALAQLLRQRGvKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPL-DTGYPD--DRLRMMLEDA 551
Cdd:PRK07769 55 DLTWsQFGAR-NR----AVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 552 RPSLLITSEDQLAR----FSDIPGleslcYQQP-LAAGDDAPLALS----KPDHT----AYIIFTSGSTGRPKGVMVGQT 618
Cdd:PRK07769 129 TPSAILTTTDSAEGvrkfFRARPA-----KERPrVIAVDAVPDEVGatwvPPEANedtiAYLQYTSGSTRIPAGVQITHL 203
|
170
....*....|.
gi 635952396 619 AIVNRLLWMQD 629
Cdd:PRK07769 204 NLPTNVLQVID 214
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
478-634 |
2.56e-07 |
|
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: 54.91 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 478 RWQfSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGaawLPLDTGYP---DDRLRMMLEDARPS 554
Cdd:cd17639 4 KYM-SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 555 LLITSedqlarfsdipgleslcyqqplaagddaplalSKPDHTAYIIFTSGSTGRPKGVMV----------GQTAIVNRL 624
Cdd:cd17639 80 AIFTD--------------------------------GKPDDLACIMYTSGSTGNPKGVMLthgnlvagiaGLGDRVPEL 127
|
170
....*....|....
gi 635952396 625 LWMQDRY----PLS 634
Cdd:cd17639 128 LGPDDRYlaylPLA 141
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
442-627 |
2.72e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.13 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 442 LAAVNDTVVPlPATTLSALVADQARKTPDAPAL--------ADAR-WQFSYREMRQQVVALAQLLrQRGVKPGDSVAVAL 512
Cdd:PRK12476 22 LDADGNIALP-PGTTLISLIERNIANVGDTVAYryldhshsAAGCaVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 513 PRSVFLTLALHGIVEAGAAWLPLDTgyPD-----DRLRMMLEDARPSLLITS---EDQLARF-SDIPGLES----LCYQQ 579
Cdd:PRK12476 100 PQGIDYVAGFFAAIKAGTIAVPLFA--PElpghaERLDTALRDAEPTVVLTTtaaAEAVEGFlRNLPRLRRprviAIDAI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 635952396 580 PLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 627
Cdd:PRK12476 178 PDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQM 225
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
4-424 |
2.84e-07 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 54.35 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIvaglqqADTL----SLR--FEEEEGEVWQWV-AAD 76
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAAL------ADVVarheSLRtvFPEDDGGPYQVVlPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 77 RTFGEPSIIDLrTAPDPHRAATERMQA--DLAQDLrvdggnPLVCHqLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIA 154
Cdd:cd19540 75 EARPDLTVVDV-TEDELAARLAEAARRgfDLTAEL------PLRAR-LFRLGPDEHVLVLVVHHIAADGWSMAPLARDLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 155 AIYRAWQRGEAtPEspFTPFAevVdEYQRYAgseAWQRDK---------------AFWQAQRQALPSPASLSA-----AP 214
Cdd:cd19540 147 TAYAARRAGRA-PD--WAPLP--V-QYADYA---LWQRELlgdeddpdslaarqlAYWRETLAGLPEELELPTdrprpAV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 215 LGGRAAgsdiwRMKLEMNADAFRRLAGHAPQCQpADLAlalttlwlgrlcnrMDYAAGF-IFMRRMGS------------ 281
Cdd:cd19540 218 ASYRGG-----TVEFTIDAELHARLAALAREHG-ATLF--------------MVLHAALaVLLSRLGAgddipigtpvag 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 282 ---AALTST-GPVLNVLPLAVHIDAQETLADLAMR-----LAAqlkkmRRHQRYDAEQIV------RDSGKAagdePLFG 346
Cdd:cd19540 278 rgdEALDDLvGMFVNTLVLRTDVSGDPTFAELLARvretdLAA-----FAHQDVPFERLVealnppRSTARH----PLFQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 347 PVLNVKVFD-YQLDIDGVQAVTHTLATGPVN-DLELALF--PDETG---GLSLEILANKARYDEAELRRHVARLTALLAQ 419
Cdd:cd19540 349 VMLAFQNTAaATLELPGLTVEPVPVDTGVAKfDLSFTLTerRDADGapaGLTGELEYATDLFDRSTAERLADRFVRVLEA 428
|
....*
gi 635952396 420 FAADP 424
Cdd:cd19540 429 VVADP 433
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
4-210 |
1.43e-06 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 52.27 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAADRTFgEPS 83
Cdd:cd19538 1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEA-TPK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 IIDLRTAPD--PHRAATE-RMQADLAQDL--RVdggnplvchQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYR 158
Cdd:cd19538 80 LEIKEVDEEelESEINEAvRYPFDLSEEPpfRA---------TLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 635952396 159 AWQRGEATPESPFTPfaevvdEYQRYAgseAWQ---------------RDKAFWQAQRQALPSPASL 210
Cdd:cd19538 151 ARCKGEAPELAPLPV------QYADYA---LWQqellgdesdpdsliaRQLAYWKKQLAGLPDEIEL 208
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
137-421 |
2.21e-06 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 51.53 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 137 HHLLVDGFSFPAITRQIAAIYRAwqrgeaTPESPFTPFAEVVdEYQRYAGSEAWQRdkaFWQAQRQALPSPA--SLSAAP 214
Cdd:cd19545 121 HHALYDGWSLPLILRQVLAAYQG------EPVPQPPPFSRFV-KYLRQLDDEAAAE---FWRSYLAGLDPAVfpPLPSSR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 215 LGGRAAGSDIWRMKLEMNAdafRRLAGHAPQCQPAdlalalTTLWLGRLCNRMDYAAGFIFMRRmgSAALTS----TGPV 290
Cdd:cd19545 191 YQPRPDATLEHSISLPSSA---SSGVTLATVLRAA------WALVLSRYTGSDDVVFGVTLSGR--NAPVPGieqiVGPT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 291 LNVLPLAVHIDAQETLADLAMRLAAQLKKMRRHQRYDAEQIvRDSGKAAGDEPLFGPVLNVkvfdyQLDIDGVQAVTHTL 370
Cdd:cd19545 260 IATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNI-RRLGPDARAACNFQTLLVV-----QPALPSSTSESLEL 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 635952396 371 ATGPVnDLELALFPdeTGGLSLEILAN------KARYDEAELrrHVARLTALLAQFA 421
Cdd:cd19545 334 GIEEE-SEDLEDFS--SYGLTLECQLSgsglrvRARYDSSVI--SEEQVERLLDQFE 385
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
6-214 |
3.14e-06 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 51.16 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 6 PLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFE-EEEGEVWQWVAADRTFGEPSI 84
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 85 IDLRTAPDPHRAATERMQAD-LAQDLRVDGGnPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRG 163
Cdd:cd19547 83 DWSGEDPDRRAELLERLLADdRAAGLSLADC-PLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 635952396 164 EATPESPFTPFAevvdEYQRYAGSEAWQRDKA--FWQAQRQALpSPASLSAAP 214
Cdd:cd19547 162 REPQLSPCRPYR----DYVRWIRARTAQSEESerFWREYLRDL-TPSPFSTAP 209
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
481-639 |
5.70e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 50.75 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 481 FSYREM--RQQVVALAqLLRQRGVKPGDSVAVALPRS-----VFLTLA------------------LHGIVEAGAAWLPL 535
Cdd:cd05938 6 YTYRDVdrRSNQAARA-LLAHAGLRPGDTVALLLGNEpaflwIWLGLAklgcpvaflntnirskslLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 536 DtgyPDdrLRMMLEDARPSLlitSEDQ-----LARFSDIPGLESLCYQQPLAAGDDAPLALSKPDH---TAYIIFTSGST 607
Cdd:cd05938 85 A---PE--LQEAVEEVLPAL---RADGvsvwyLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTiksPALYIYTSGTT 156
|
170 180 190
....*....|....*....|....*....|....*
gi 635952396 608 GRPKGVMVGQTaivnRLLWMQDRYPLS---AQDVV 639
Cdd:cd05938 157 GLPKAARISHL----RVLQCSGFLSLCgvtADDVI 187
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
585-882 |
6.93e-06 |
|
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: 49.93 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 585 DDAPLALSKPDHTAYIIF--TSGSTGRPkgVMVGQTA--------IVNRLLWMQDRYPlsaqDVVAQKTpcsFDVSVWEF 654
Cdd:cd05913 66 DNYPFGLFAVPREKVVRIhaSSGTTGKP--TVVGYTKndldvwaeLVARCLDAAGVTP----GDRVQNA---YGYGLFTG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 655 WWPFIAGAQL--VMAEPEAHRDPQAMQQFFARYGVTTTHFVPSMlAAFVAS------LDADSVAacrtLRRVFCSGEALP 726
Cdd:cd05913 137 GLGFHYGAERlgALVIPAGGGNTERQLQLIKDFGPTVLCCTPSY-ALYLAEeaeeegIDPRELS----LKVGIFGAEPWT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 727 TELCREWERLTGAPLHNLYGPTEAAvdvswypacGPELAAVTGSSVPIGwpVWNTGLR---ILDAAMRPVPPGVAGDLYL 803
Cdd:cd05913 212 EEMRKRIERRLGIKAYDIYGLTEII---------GPGVAFECEEKDGLH--IWEDHFIpeiIDPETGEPVPPGEVGELVF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 804 TGIqlaqgylgrpdltasrfiaDPFAPGERMYRTGDVARWL--------TNGAVE-YLGRSDDQLKIRGQRIELGEIDRV 874
Cdd:cd05913 281 TTL-------------------TKEAMPLIRYRTRDITRLLpgpcpcgrTHRRIDrITGRSDDMLIIRGVNVFPSQIEDV 341
|
....*...
gi 635952396 875 MSGLPDVA 882
Cdd:cd05913 342 LLKIPGLG 349
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-205 |
9.23e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 27 WSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEvWQWVAADRTFGEPsiIDLRTAPDPH--RAATERMQAD 104
Cdd:PRK12316 1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGG-WQQAYAAPQAGEV--LWQRQAASEEelLALCEEAQRS 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 105 LaqDLRvdgGNPLVCHQLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRGEATPESPFTPFAevvDEYQRY 184
Cdd:PRK12316 1198 L--DLE---QGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWA---RRLHEH 1269
|
170 180
....*....|....*....|.
gi 635952396 185 AGSEAWQRDkaFWQAQRQALP 205
Cdd:PRK12316 1270 AGARAEELD--YWQAQLEDAP 1288
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1065-1163 |
1.01e-05 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 48.07 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1065 DGPTLFCFHPASGFAWQFSVLARYLSPRWSITGI------QSPRPQGPMasaaSLDEVCEHhLRTLLAQQPHGPYYLFGY 1138
Cdd:COG0596 22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPdlrghgRSDKPAGGY----TLDDLADD-LAALLDALGLERVVLVGH 96
|
90 100
....*....|....*....|....*
gi 635952396 1139 SLGGTLAQGIAARLRQRGEAVAFLG 1163
Cdd:COG0596 97 SMGGMVALELAARHPERVAGLVLVD 121
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
480-614 |
1.06e-05 |
|
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: 49.77 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLdtgYPD---DRLRMMLEDARPSLL 556
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635952396 557 ITS--EDQLARFSDIPGLESLCYQQPLAAGDD-----------APL---ALSKPDHTAYIIFTSGSTGRPKGVM 614
Cdd:cd05932 83 FVGklDDWKAMAPGVPEGLISISLPPPSAANCqyqwddliaqhPPLeerPTRFPEQLATLIYTSGTTGQPKGVM 156
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
480-884 |
1.34e-05 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 49.51 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITS 559
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 560 ED--------QLARFSDIPGLES----------LCYQQPLA---------AGDDA-------------PLALSKPDHTAY 599
Cdd:PLN02654 200 NAvkrgpktiNLKDIVDAALDESakngvsvgicLTYENQLAmkredtkwqEGRDVwwqdvvpnyptkcEVEWVDAEDPLF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 600 IIFTSGSTGRPKGVM-VGQTAIVNRLLWMQDRYPLSAQDVVAQKTPCSFDVS-VWEFWWPFIAGAQLVMAE-PEAHRDPQ 676
Cdd:PLN02654 280 LLYTSGSTGKPKGVLhTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATVLVFEgAPNYPDSG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 677 AMQQFFARYGVTTTHFVPSMLAAFVASLDADSVAACRTLRRVFCS-GEALPTELCReWerltgapLHNLYGPTEAAVDVS 755
Cdd:PLN02654 360 RCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSvGEPINPSAWR-W-------FFNVVGDSRCPISDT 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 756 WYPAcgpELAAVTGSSVPIGWPvwntglRILDAAMRP---VPPGVAGDlylTGIQL---AQGYL----GRPDLTAS---- 821
Cdd:PLN02654 432 WWQT---ETGGFMITPLPGAWP------QKPGSATFPffgVQPVIVDE---KGKEIegeCSGYLcvkkSWPGAFRTlygd 499
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635952396 822 --RFIADPFAPGERMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:PLN02654 500 heRYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEA 564
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
480-884 |
6.62e-05 |
|
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: 47.04 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 480 QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSL---- 555
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVllfd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 556 ---LITSEDQLARFSDI---PGLESLC--YQQPLAAGDDAPLALSKPDHTAYII--FTSGSTGRPKGVMVG-QTAIVN-R 623
Cdd:cd05915 104 pnlLPLVEAIRGELKTVqhfVVMDEKApeGYLAYEEALGEEADPVRVPERAACGmaYTTGTTGLPKGVVYShRALVLHsL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 624 LLWMQDRYPLSAQDVVAQKTPCsFDVSVWEFWWPFIAGAQLVMAEPEAHRDpQAMQQFFARYGVTTTHFVPSMLAAFVAS 703
Cdd:cd05915 184 AASLVDGTALSEKDVVLPVVPM-FHVNAWCLPYAATLVGAKQVLPGPRLDP-ASLVELFDGEGVTFTAGVPTVWLALADY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 704 LDADSVAACRTLRRVfcSGEALPTELCREWERLTGAPLHNLYGPTEA---AVDVSWYPACG--PELAAVTGSSVPiGWPV 778
Cdd:cd05915 262 LESTGHRLKTLRRLV--VGGSAAPRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLEslSEEEKLTLKAKT-GLPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 779 WNTGLRILDAAMRPVPPG--VAGDLYLTGIQLAQGYLGRPDLTAsrfiADPFAPGerMYRTGDVARWLTNGAVEYLGRSD 856
Cdd:cd05915 339 PLVRLRVADEEGRPVPKDgkALGEVQLKGPWITGGYYGNEEATR----SALTPDG--FFRTGDIAVWDEEGYVEIKDRLK 412
|
410 420
....*....|....*....|....*...
gi 635952396 857 DQLKIRGQRIELGEIDRVMSGLPDVAQA 884
Cdd:cd05915 413 DLIKSGGEWISSVDLENALMGHPKVKEA 440
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
593-953 |
1.53e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 46.24 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 593 KPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQDRYPLSAQDVVAQKTPC--SFDVSVWEFWwPFIAGAQLVMAE-- 668
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTVGLFT-PLLTGAEVFLYPsp 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 669 ------PEAHRDPQAMQQFfarygvTTTHFVPSMlAAFVASLDAdsvaacRTLRRVFCSGEALPTELCREWERLTGAPLH 742
Cdd:PRK08043 442 lhyrivPELVYDRNCTVLF------GTSTFLGNY-ARFANPYDF------ARLRYVVAGAEKLQESTKQLWQDKFGLRIL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 743 NLYGPTEaavdvswypaCGPelaaVTGSSVPIGWPVWNTGlRIL---DAAMRPVPpGVA--GDLYLTGIQLAQGYL--GR 815
Cdd:PRK08043 509 EGYGVTE----------CAP----VVSINVPMAAKPGTVG-RILpgmDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEK 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 816 PDLTASRFIADpfAPGER---MYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQavsHACVFN 892
Cdd:PRK08043 573 PGVLEVPTAEN--ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635952396 893 QAAATGgdaRQLVgYLVSDSGLPLDTAALKARlAEQLPPHMVPVVLMQLAELPLSANGKLD 953
Cdd:PRK08043 648 SDASKG---EALV-LFTTDSELTREKLQQYAR-EHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
479-876 |
1.53e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 46.17 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 479 WQfSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLIT 558
Cdd:PLN02614 79 WQ-TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 559 SEDQLAR-FSDIP--------------------------GLESLCYQQ--PLAAGDDAPLALSKPDHTAYIIFTSGSTGR 609
Cdd:PLN02614 158 EEKKISElFKTCPnsteymktvvsfggvsreqkeeaetfGLVIYAWDEflKLGEGKQYDLPIKKKSDICTIMYTSGTTGD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 610 PKGVMVGQTAIVN------RLLWMQDRyPLSAQDVVAQKTPCS--FDVSVWE----------FWwpfiAGAQLVMAEPEA 671
Cdd:PLN02614 238 PKGVMISNESIVTliagviRLLKSANA-ALTVKDVYLSYLPLAhiFDRVIEEcfiqhgaaigFW----RGDVKLLIEDLG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 672 HRDP--------------QAMQQ------FFAR--YGVTTTHFVPSM---LAAFVASLDADSVAACRTLR------RVFC 720
Cdd:PLN02614 313 ELKPtifcavprvldrvySGLQKklsdggFLKKfvFDSAFSYKFGNMkkgQSHVEASPLCDKLVFNKVKQglggnvRIIL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 721 SGEALPTELCREWERLTgAPLHNL--YGPTEAAVDVSwypACGPELAAVTGSsvpIGWPVWNTGLRILDA------AMRP 792
Cdd:PLN02614 393 SGAAPLASHVESFLRVV-ACCHVLqgYGLTESCAGTF---VSLPDELDMLGT---VGPPVPNVDIRLESVpemeydALAS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 793 VPpgvAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKI-RGQRIELGEI 871
Cdd:PLN02614 466 TP---RGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENI 535
|
....*
gi 635952396 872 DRVMS 876
Cdd:PLN02614 536 ENIYG 540
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
450-624 |
1.54e-04 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 46.13 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 450 VPLP-ATTLSALVADQARKTPDAPALADARW--QFSYREMRQQVVALAQLLRQRGVKPGDSVAVALPRSVFLTLALHGIV 526
Cdd:PLN02330 22 VPVPdKLTLPDFVLQDAELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 527 EAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSEdqlARFSDIPGLE-------------SLCYQQPLAAGDDAPLALS- 592
Cdd:PLN02330 102 AAGGVFSGANPTALESEIKKQAEAAGAKLIVTND---TNYGKVKGLGlpvivlgeekiegAVNWKELLEAADRAGDTSDn 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 635952396 593 ----KPDHTAyIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:PLN02330 179 eeilQTDLCA-LPFSSGTTGISKGVMLTHRNLVANL 213
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
4-424 |
1.59e-04 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 45.93 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 4 RLPLVAAQPGIWMAERLSTLPGAWSVAHYVELRGALDPTLLGKAIVAGLQQADTLSLRFEEEEGEVWQWVAaDRTFGEPs 83
Cdd:cd19546 4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIL-DADAARP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 84 iiDLRTAPDPHRAATERMQADLAQDLRVDGGNPLVCHqLLRVGDDRWYWYQRYHHLLVDGFSFPAITRQIAAIYRAWQRG 163
Cdd:cd19546 82 --ELPVVPATEEELPALLADRAAHLFDLTRETPWRCT-LFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 164 EATPESP----FTPFA----EVVDEyQRYAGSEAWQRdKAFWQAQRQALPS----PASLSAAPLGGRAAGSdiwrMKLEM 231
Cdd:cd19546 159 RAPERAPlplqFADYAlwerELLAG-EDDRDSLIGDQ-IAYWRDALAGAPDelelPTDRPRPVLPSRRAGA----VPLRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 232 NADAFRRLAgHAPQCQPADLALALTTLWL---GRLCNRMDYAAGFIFMRRMGSAALTS-TGPVLNVLPLAVHIDAQETLA 307
Cdd:cd19546 233 DAEVHARLM-EAAESAGATMFTVVQAALAmllTRLGAGTDVTVGTVLPRDDEEGDLEGmVGPFARPLALRTDLSGDPTFR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 308 DLAMRLAAQLKKMRRHQRYDAEQIV--RDSGKAAGDEPLFGPVLNVKvfDYQLDIDGVQAV----THTLATG-PVNDLEL 380
Cdd:cd19546 312 ELLGRVREAVREARRHQDVPFERLAelLALPPSADRHPVFQVALDVR--DDDNDPWDAPELpglrTSPVPLGtEAMELDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 635952396 381 ALFPDET-------GGLSLEILANKARYDEAELRRHVARLTALLAQFAADP 424
Cdd:cd19546 390 SLALTERrnddgdpDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
582-954 |
2.03e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.53 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 582 AAGDDAPLALSKPDHTAYIIF--TSGSTGRPKGVMVGQTAIVNRLLWMQDRYPL-SAQDVVAQKTPCSFDVSVWEFWWPF 658
Cdd:PRK05851 137 AAHTNRSASLTPPDSGGPAVLqgTAGSTGTPRTAILSPGAVLSNLRGLNARVGLdAATDVGCSWLPLYHDMGLAFLLTAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 659 IAGAQLVMAEPEAHR-DPQAMQQFFARYGVTTT---HFVPSMLAAFVASLDADSVAAcrtLRRVFCSGEalPTElCREWE 734
Cdd:PRK05851 217 LAGAPLWLAPTTAFSaSPFRWLSWLSDSRATLTaapNFAYNLIGKYARRVSDVDLGA---LRVALNGGE--PVD-CDGFE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 735 RLTGA---------PLHNLYGPTEAAVDVSwYPACGP-----ELAAVTGSSVP----IGWPVWNTGLRIldaAMRPVPPG 796
Cdd:PRK05851 291 RFATAmapfgfdagAAAPSYGLAESTCAVT-VPVPGIglrvdEVTTDDGSGARrhavLGNPIPGMEVRI---SPGDGAAG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 797 VA----GDLYLTGIQLAQGYLGrpdltasrfiADPFAPGErMYRTGDVArWLTNGAVEYLGRSDDQLKIRGQRIELGEID 872
Cdd:PRK05851 367 VAgreiGEIEIRGASMMSGYLG----------QAPIDPDD-WFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 873 RVMSGLPDVAQAvshACVfnqAAATG-GDARQlvGYLVSDSGLPLDTAALKARLAEQLPPH--MVP--VVLMQLAELPLS 947
Cdd:PRK05851 435 RVAAQVRGVREG---AVV---AVGTGeGSARP--GLVIAAEFRGPDEAGARSEVVQRVASEcgVVPsdVVFVAPGSLPRT 506
|
....*..
gi 635952396 948 ANGKLDR 954
Cdd:PRK05851 507 SSGKLRR 513
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
593-671 |
2.12e-04 |
|
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: 45.43 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 593 KPDHTAYIIFTSGSTGRPKGVMVGQTAIVnrllW--------MQDRYPLSAQDVVAQKTPCSF-DVSVWEFWWPFIAGAQ 663
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNIT----WtakaasqhMDLRPATVGQESVVSYLPLSHiAAQILDIWLPIKVGGQ 223
|
....*...
gi 635952396 664 LVMAEPEA 671
Cdd:cd05933 224 VYFAQPDA 231
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
32-391 |
2.36e-04 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 45.17 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 32 YVELRGA-LDPTLLGKAIVAGLQQADTLSLRFEEEeGEvwQWVAADRTFGEPSIIDLRTAPDPHR-AATERMQADLA-QD 108
Cdd:cd19535 29 YLEFDGEdLDPDRLERAWNKLIARHPMLRAVFLDD-GT--QQILPEVPWYGITVHDLRGLSEEEAeAALEELRERLShRV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 109 LRVDGGnPLVCHQLLRVGDDRwywyQRYH----HLLVDGFSFPAITRQIAAIYRawQRGEATPESPFTpFAEVVDEYQRY 184
Cdd:cd19535 106 LDVERG-PLFDIRLSLLPEGR----TRLHlsidLLVADALSLQILLRELAALYE--DPGEPLPPLELS-FRDYLLAEQAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 185 AGSeAWQRDKAFWQAQRQALPSPASLSAAPLGGRAAGSDIWRMKLEMNADAFRRLAGHAPQCQ--PAdlalalttlwlgr 262
Cdd:cd19535 178 RET-AYERARAYWQERLPTLPPAPQLPLAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHGvtPS------------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 263 lcnrMDYAAGF------------------IFMRRMGSAALTS-----TgpvlNVLPLAVHIDAQETLADLAMRLAAQLKK 319
Cdd:cd19535 244 ----MVLLTAYaevlarwsgqprfllnltLFNRLPLHPDVNDvvgdfT----SLLLLEVDGSEGQSFLERARRLQQQLWE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635952396 320 MRRHQRYDAEQIVRDSGKAAGDEPLFGPVlnvkVFdyqldidgvqavTHTLATGPVNDLELALFPDETGGLS 391
Cdd:cd19535 316 DLDHSSYSGVVVVRRLLRRRGGQPVLAPV----VF------------TSNLGLPLLDEEVREVLGELVYMIS 371
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
435-883 |
2.37e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 45.60 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 435 SANELARLAAVNDTVVPLPATTLSA--LVADQARKTPDAPALA-----DAR-----WQfSYREMRQQVVALAQLLRQRGV 502
Cdd:PLN02861 21 SAGPVYRSIYAKDGLLDLPADIDSPwqFFSDAVKKYPNNQMLGrrqvtDSKvgpyvWL-TYKEVYDAAIRIGSAIRSRGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 503 KPGDSVAVALPRSVFLTLALHGIVEAGAAWLPLDTGYPDDRLRMMLEDARPSLLITSEDQLA-----------------R 565
Cdd:PLN02861 100 NPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISsilsclpkcssnlktivS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 566 FSDIPGL-----ESLCY------QQPLAAGDDAPLALSKPDHTAYIIFTSGSTGRPKGVMVGQTAI------VNRLLWMQ 628
Cdd:PLN02861 180 FGDVSSEqkeeaEELGVscfsweEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIiaevlsTDHLLKVT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 629 DR-----------YPLSAQDVVAQKTPCSFDVSVWEFWW--------------PFI------------AGAQLVMAEPEA 671
Cdd:PLN02861 260 DRvateedsyfsyLPLAHVYDQVIETYCISKGASIGFWQgdirylmedvqalkPTIfcgvprvydriyTGIMQKISSGGM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 672 HRdpQAMQQFFARYGVTTTH--FVPSMLAAFVASLDADSVAACRTLR-RVFCSGEA-LPTELcREWERLTGAP-LHNLYG 746
Cdd:PLN02861 340 LR--KKLFDFAYNYKLGNLRkgLKQEEASPRLDRLVFDKIKEGLGGRvRLLLSGAApLPRHV-EEFLRVTSCSvLSQGYG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 747 PTEAAvdvswyPACGPELAAVTGSSVPIGWPVWNTGLRILDA------AMRPVPpgvAGDLYLTGIQLAQGYLGRPDLTA 820
Cdd:PLN02861 417 LTESC------GGCFTSIANVFSMVGTVGVPMTTIEARLESVpemgydALSDVP---RGEICLRGNTLFSGYHKRQDLTE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635952396 821 SRFIadpfapgERMYRTGDVARWLTNGAVEYLGRSDDQLKI-RGQRIELGEIDRVMSGLPDVAQ 883
Cdd:PLN02861 488 EVLI-------DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIAS 544
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1063-1175 |
3.01e-04 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 43.84 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 1063 ESDGPTLFCFHPASGFAWQFSVLARYLSPR-WSITGI------QSPRPQGPMAS-AASLDEVceHHLRTLLAQQPHGPYY 1134
Cdd:COG2267 25 GSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFdlrghgRSDGPRGHVDSfDDYVDDL--RAALDALRARPGLPVV 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 635952396 1135 LFGYSLGGTLAQGIAARLRQRGEAVAFLG---LLDTWPPETQNW 1175
Cdd:COG2267 103 LLGHSMGGLIALLYAARYPDRVAGLVLLApayRADPLLGPSARW 146
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
550-621 |
3.48e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.11 E-value: 3.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635952396 550 DARPSLLITSEDQLARFSDIpglESLCYQQPLAAgddaplALSKPDHTAYIIFTSGSTGRPKGVMVGQTAIV 621
Cdd:PLN02387 214 DSDSSLSGSSNWTVSSFSEV---EKLGKENPVDP------DLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIV 276
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
482-630 |
5.01e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.58 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 482 SYREMRQQVVALAQLLRQRGVKPGDSVAV-------------------ALPRSVFLTL---AL-HGIVEAGAAWLPLDTG 538
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIyeetrwewlasiygiwsqsMVAATVYANLgedALaYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 539 YPDDRLRMMLEDARPSLLITSEDQLARFSDIPGLESLCYQQPLAAGDDAP--LALSKP---DHTAYIIFTSGSTGRPKGV 613
Cdd:PTZ00216 203 NVPNLLRLMKSGGMPNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHSAGshHPLNIPennDDLALIMYTSGTTGDPKGV 282
|
170
....*....|....*..
gi 635952396 614 MVGQTAIVNRLLWMQDR 630
Cdd:PTZ00216 283 MHTHGSLTAGILALEDR 299
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
476-615 |
6.58e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.93 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 476 DARWQfSYREMRQQVVALAQLLRQRGVKPGDSVAValprsVFLTLALHGIVE-AGAAW----LPL-DTGYPD-------- 541
Cdd:PLN02736 75 EYKWM-TYGEAGTARTAIGSGLVQHGIPKGACVGL-----YFINRPEWLIVDhACSAYsyvsVPLyDTLGPDavkfivnh 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 542 ----------DRLRMMLE--DARPSL-LIT----SEDQLARFSDIPGLESLCYQQPLAAGDDAPLAL--SKPDHTAYIIF 602
Cdd:PLN02736 149 aevaaifcvpQTLNTLLSclSEIPSVrLIVvvggADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFrpPKPEDVATICY 228
|
170
....*....|...
gi 635952396 603 TSGSTGRPKGVMV 615
Cdd:PLN02736 229 TSGTTGTPKGVVL 241
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
596-957 |
1.63e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.81 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 596 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWmQDRYPLSAQDVVAQKTPCSFD-VSVWEFWWPFIA-GAQLVMAEPEAHR 673
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSNGPHLVGLKY-YWRSIIEKDIPTVVFSHSSIGwVSFHGFLYGSLSlGNTFVMFEGGIIK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 674 DPQAMQQFFA---RYGVTTTHFVPSMLAaFVASLDAD-----SVAACRTLRRVFCSGEALPTELCREWERLTGAPLHNLY 745
Cdd:PTZ00237 334 NKHIEDDLWNtieKHKVTHTLTLPKTIR-YLIKTDPEatiirSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 746 GPTEAAVDVSW--------YPACG---PELAAVTGSSVPIGWPVWNTGLRILDAamrPVPPGVAGDLYLTGIQLAQGYlg 814
Cdd:PTZ00237 413 GQTEIGITYLYcyghinipYNATGvpsIFIKPSILSEDGKELNVNEIGEVAFKL---PMPPSFATTFYKNDEKFKQLF-- 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 815 rpdltaSRFiadpfaPGerMYRTGDVARWLTNGAVEYLGRSDDQLKIRGQRIELGEIDRVMSGLPDVAQAVSHAcVFNQA 894
Cdd:PTZ00237 488 ------SKF------PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIG-IYDPD 552
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 895 AATggdarQLVGYLV---SDSGLPLDTAALKARLAEQLPPHMVPVVLMQ----LAELPLSANGKLDRKAL 957
Cdd:PTZ00237 553 CYN-----VPIGLLVlkqDQSNQSIDLNKLKNEINNIITQDIESLAVLRkiiiVNQLPKTKTGKIPRQII 617
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
1109-1153 |
1.93e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 41.36 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 635952396 1109 SAASLDEVCEHhLRTLLAQQPHGPYYLFGYSLGGTLA-----QGIAARLR 1153
Cdd:PRK11126 45 SVDGFADVSRL-LSQTLQSYNILPYWLVGYSLGGRIAmyyacQGLAGGLC 93
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
593-634 |
4.29e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 41.24 E-value: 4.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 635952396 593 KPDHTAYIIFTSGSTGRPKGVMVGQTAIVNRLlwmqdrYPLS 634
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTV------VPLC 337
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
784-958 |
7.90e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 40.36 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 784 RILDAAMRPVPPGVAGDLYLTGIQLAQGYLgrPDLTASRfiadpfapgeRMYRTGDVARWLTNGAVEYLGRSDDQLKIRG 863
Cdd:PRK07445 287 QVLPHAQITIPANQTGNITIQAQSLALGYY--PQILDSQ----------GIFETDDLGYLDAQGYLHILGRNSQKIITGG 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635952396 864 QRIELGEIDRVM--SGLpdvaqaVSHACVFNQAAATGGDarQLVGYLVSDSGlPLDTAALKARLAEQLPPHMVPVVLMQL 941
Cdd:PRK07445 355 ENVYPAEVEAAIlaTGL------VQDVCVLGLPDPHWGE--VVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPV 425
|
170
....*....|....*..
gi 635952396 942 AELPLSANGKLDRKALP 958
Cdd:PRK07445 426 PQLPRNPQGKINRQQLQ 442
|
|
| |
