|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
196-677 |
2.14e-166 |
|
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: 495.12 E-value: 2.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALTDevgaavtdrlgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd05930 81 EDSGAKLVLTD----------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLG 435
Cdd:cd05930 121 LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLErrPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTE-TCDDTNHEVLDRAQDGSRVPLGRAIAGVGVHV 514
Cdd:cd05930 201 ELE--LAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEaTVDATYYRVPPDDEEDGRVPIGRPIPNTRVYV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 515 VDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFR 594
Cdd:cd05930 279 LDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 595 VEIGEIEDRLLRLPGVREATVIV-AGAAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLTGNGK 671
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVVArEDGDGEKRLVAYVVPDEGGELDEeeLRAHLAERLPDYMVPSAFVVLDALPLTPNGK 438
|
....*.
gi 502993051 672 VDRKEL 677
Cdd:cd05930 439 VDRKAL 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
17-1005 |
2.39e-164 |
|
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: 518.26 E-value: 2.39e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 17 PRWATGLTGLAEHRFPLPAAVAD--------------TVLFAAHAVVLGALTGEP--VVTAVHDGRPRV----------- 69
Cdd:COG1020 229 PRPAVQSYRGARVSFRLPAELTAalralarrhgvtlfMVLLAAFALLLARYSGQDdvVVGTPVAGRPRPeleglvgffvn 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 70 -----VDL-GHRTWRELIAHV---------------------AGAPAVAAR----------CDTVVGEGELGGDAIVHIG 112
Cdd:COG1020 309 tlplrVDLsGDPSFAELLARVretllaayahqdlpferlveeLQPERDLSRnplfqvmfvlQNAPADELELPGLTLEPLE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 113 LD---------------GDALVVRC--RREWVDDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGA 175
Cdd:COG1020 389 LDsgtakfdltltvvetGDGLRLTLeyNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNAT 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 176 PRELP-DRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLK 254
Cdd:COG1020 469 AAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLK 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 255 AGGCYLPVEPHFPLERIAAMVTRSACGRALTDEvgaAVTDRLGGLvpGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIY 334
Cdd:COG1020 549 AGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS---ALAARLPEL--GVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 335 FTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAE 414
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAEL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 415 LDRSRVEVAQLVPSYVEVLLGHLerrPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTN-HEVLD 493
Cdd:COG1020 704 LARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTyYEVTP 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 494 RAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPL-FPGQRLYRSGDFGRW 572
Cdd:COG1020 781 PDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARW 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 573 TPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACY---SAAPSLAPGPLVEALARVL 649
Cdd:COG1020 861 LPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYvvpEAGAAAAAALLRLALALLL 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 650 PDYMVPRDWYWLDVLPLTGNGKVDRKELARitgGLHRAMTEDERPRPGAERRLAAAWATVLGVAPDRVGRTDDFFASGGS 729
Cdd:COG1020 941 PPYMVPAAVVLLLPLPLTGNGKLDRLALPA---PAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGL 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 730 SLSALQLVIELDRAVSLGDV--TAHPVLADLAGVLGTGATGTRPVLHRLTPPGRRTLVCFPYAGGNAVTYVPLAGELAAE 807
Cdd:COG1020 1018 LLLLALARAARLLLLLLLLLllFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLA 1097
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 808 GWAVYGVEPPGRDGNEAPVSVPELAELVAGELAALDAGPLTLWGHSTGVAAALATARLLRSRGHDVRRVLLGAQLPGDSG 887
Cdd:COG1020 1098 LLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLL 1177
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 888 ARRAQAAEVTALPDEAVVTALVESGRPELAEVGDAHRRLLADAYRHDVAAACGYLAEALDAGDRLDVPVTVVLAADDVPD 967
Cdd:COG1020 1178 ALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAA 1257
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 502993051 968 DLPGDPWDWSRLAGDVRVVELPDGGHYFAASRPASVAR 1005
Cdd:COG1020 1258 ALLALALALLALALLLLALALLLPALARARAARTARAL 1295
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
128-773 |
5.32e-140 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 465.40 E-value: 5.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 128 DDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELPDRRVHQLIADTAAARPDDVAVVAGLDQ 207
Cdd:PRK12467 458 EATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQV 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDE 287
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 VGAAVTDrlggLVPGLRARGVDEILR--GGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLG 365
Cdd:PRK12467 618 HLLAQLP----VPAGLRSLCLDEPADllCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQ 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 366 VRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGhlERRPRALP 445
Cdd:PRK12467 694 LAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPR 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 446 ALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH-EVLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPL 524
Cdd:PRK12467 772 PQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTyELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPV 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 525 GATGEIVFSGRCLARGYVNDPIRTALAFTASPLFP-GQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDR 603
Cdd:PRK12467 852 GVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 604 LLRLPGVREATVIVAGAAESARLVA-------CYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKE 676
Cdd:PRK12467 932 LLAQPGVREAVVLAQPGDAGLQLVAylvpaavADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKA 1011
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 677 LARITGGLHRAMTedERPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLVIE----LDRAVSLGDVTAH 752
Cdd:PRK12467 1012 LPKPDASAVQATF--VAPQTELEKRLAAIWADVLKV--ERVGLTDNFFELGGHSLLATQVISRvrqrLGIQVPLRTLFEH 1087
|
650 660
....*....|....*....|.
gi 502993051 753 PVLADLAGVLGTGATGTRPVL 773
Cdd:PRK12467 1088 QTLAGFAQAVAAQQQGAQPAL 1108
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
186-677 |
2.52e-139 |
|
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: 426.62 E-value: 2.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPH 265
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRSACGRALTDEvgaavtdRLGGLVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKG 345
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDR-------SLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEGMLNhmLAKIDD-LGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQ 424
Cdd:cd12117 154 VAVTHRGVVR--LVKNTNyVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LVPSyvevLLGHL-ERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTE-TCDDTNHEVLDRAQDGSRVP 502
Cdd:cd12117 232 LTAA----LFNQLaDEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnTTFTTSHVVTELDEVAGSIP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 503 LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSG 582
Cdd:cd12117 308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 583 RRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIV-AGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWL 661
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVrEDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVL 467
|
490
....*....|....*.
gi 502993051 662 DVLPLTGNGKVDRKEL 677
Cdd:cd12117 468 DELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
185-677 |
2.24e-136 |
|
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: 418.99 E-value: 2.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 185 HQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEP 264
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 HFPLERIAAMVTRSACGRALTDEvgaavtDRLGGLVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPK 344
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 345 GVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQ 424
Cdd:cd17646 155 GVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LVPSYVEVLLGhlERRPRALPALRCVSATGEALKAALVRRWFAvLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSRVPLG 504
Cdd:cd17646 235 FVPSMLRVFLA--EPAAGSCASLRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 505 RAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRR 584
Cdd:cd17646 312 RPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 585 DTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGA-AESARLVACYSAAPSLAPGP---LVEALARVLPDYMVPRDWYW 660
Cdd:cd17646 392 DDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApAGAARLVGYVVPAAGAAGPDtaaLRAHLAERLPEYMVPAAFVV 471
|
490
....*....|....*..
gi 502993051 661 LDVLPLTGNGKVDRKEL 677
Cdd:cd17646 472 LDALPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
124-952 |
1.31e-133 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 446.53 E-value: 1.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 124 REWVDDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELP-DRRVHQLIADTAAARPDDVAVV 202
Cdd:PRK12467 3036 RQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPsERLVHQLIEAQVARTPEAPALV 3115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 203 AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGR 282
Cdd:PRK12467 3116 FGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKL 3195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 283 ALTDevgAAVTDRLgGLVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKID 362
Cdd:PRK12467 3196 LLTQ---AHLLEQL-PAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAE 3271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 363 DLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQaLLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLErrPR 442
Cdd:PRK12467 3272 AYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND-LWDPEELWQAIHAHRISIACFPPAYLQQFAEDAG--GA 3348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 443 ALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH--EVLDRAQDGSRVPLGRAIAGVGVHVVDGNLM 520
Cdd:PRK12467 3349 DCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLN 3428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 521 PVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLF-PGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGE 599
Cdd:PRK12467 3429 PVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 3508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 600 IEDRLLRLPGVREATVIVAGAAESARLVA-CYSAAPSLAPGPLVEA-LARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGGKQLVAyVVPADPQGDWRETLRDhLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 678 ARITGGLHRAMTEderPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLVIELDRA----VSLGDVTAHP 753
Cdd:PRK12467 3589 PDPDAKGSREYVA---PRSEVEQQLAAIWADVLGV--EQVGVTDNFFELGGDSLLALQVLSRIRQSlglkLSLRDLMSAP 3663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 754 VLADLAGVLGTGATGTRPVLhrltPPGRRT-----LVCFPYAGGNAVTYVPLAGELaAEGWAVYGVEPPG-RDGNEAPVS 827
Cdd:PRK12467 3664 TIAELAGYSPLGDVPVNLLL----DLNRLEtgfpaLFCRHEGLGTVFDYEPLAVIL-EGDRHVLGLTCRHlLDDGWQDTS 3738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 828 VPELAELVAGELAALDA-GPLTLWGHSTGVAAALATARLLRSRGHDVRRV-LLGAQLPGDS--------GARRAQAAEVT 897
Cdd:PRK12467 3739 LQAMAVQYADYILWQQAkGPYGLLGWSLGGTLARLVAELLEREGESEAFLgLFDNTLPLPDefvpqaefLELLRQLGELI 3818
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 898 ALPDEaVVTALVESGRPELAEVGDAHRRLLADAYRHDVAAA--CGYLAEALDAGDRL 952
Cdd:PRK12467 3819 GRANR-LLRGLEEGGVGPDVLVGIAIQRCFDIAPLELYTPLldAGELAHIFDVAMRL 3874
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
128-765 |
1.55e-132 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 443.45 E-value: 1.55e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 128 DDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELPDRR-VHQLIADTAAARPDDVAVVAGLD 206
Cdd:PRK12467 1519 EASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARlVHQLIEDQAAATPEAVALVFGEQ 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTD 286
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 evgAAVTDRLgGLVPGLRARGVDEI--LRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDL 364
Cdd:PRK12467 1679 ---SHLQARL-PLPDGLRSLVLDQEddWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 365 GVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRAl 444
Cdd:PRK12467 1755 QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP- 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSR--VPLGRAIAGVGVHVVDGNLMPV 522
Cdd:PRK12467 1834 LSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsVPIGQPIANLSTYILDASLNPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 523 PLGATGEIVFSGRCLARGYVNDPIRTALAFTASPL-FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIE 601
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 602 DRLLRLPGVREATVIVAGAAESARLVA----------CYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGK 671
Cdd:PRK12467 1994 ARLREQGGVREAVVIAQDGANGKQLVAyvvptdpglvDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGK 2073
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 672 VDRKELARITGGLHRamTEDERPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLVielDRAVSLG---- 747
Cdd:PRK12467 2074 LDRKALPAPDASELQ--QAYVAPQSELEQRLAAIWQDVLGL--EQVGLHDNFFELGGDSIISIQVV---SRARQAGirft 2146
|
650 660
....*....|....*....|
gi 502993051 748 --DVTAHPVLADLAGVLGTG 765
Cdd:PRK12467 2147 pkDLFQHQTVQSLAAVAQEG 2166
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
186-677 |
2.27e-131 |
|
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: 405.94 E-value: 2.27e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPH 265
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRSACGRALTDEvgaavtdrlgGLVPGLRARGV-----DEILRGGHPSEVPgTPVVAGQLAYIYFTSGST 340
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQS----------HLQPPIAFIGLidlldEDTIYHEESENLE-PVSKSDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 341 GEPKGVMCEHEGmLNHMLAKIDDLGVRAGTV-VAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSR 419
Cdd:cd17655 150 GKPKGVMIEHRG-VVNLVEWANKVIYQGEHLrVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 420 VEVAQLVPSYVEVL--LGHLERRPralpaLRCVSATGEALKAALVRRWFAVLPE-VLLVNAYGLTETC-DDTNHEVLDRA 495
Cdd:cd17655 229 ITIIDLTPAHLKLLdaADDSEGLS-----LKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTvDASIYQYEPET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 496 QDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPD 575
Cdd:cd17655 304 DQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 576 GRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIV-AGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMV 654
Cdd:cd17655 384 GNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIArKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMI 463
|
490 500
....*....|....*....|...
gi 502993051 655 PRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd17655 464 PSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
128-737 |
4.72e-129 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 433.23 E-value: 4.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 128 DDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELPDRR-VHQLIADTAAARPDDVAVVAGLD 206
Cdd:PRK12316 456 EARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRgVHRLFEEQVERTPEAPALAFGEE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTD 286
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 EvgaavtdRLGGLVPglRARGVDEIL-------RGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLA 359
Cdd:PRK12316 616 S-------HLGRKLP--LAAGVQVLDldrpaawLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCW 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 360 KIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGhlER 439
Cdd:PRK12316 687 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DE 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 440 RPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLdRAQDGSRVPLGRAIAGVGVHVVDGNL 519
Cdd:PRK12316 765 DVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC-VEEGGDSVPIGRPIANLACYILDANL 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 520 MPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGE 599
Cdd:PRK12316 844 EPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 923
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 600 IEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLaPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:PRK12316 924 IEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW-REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 502993051 680 ITGGLHRAmtEDERPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLV 737
Cdd:PRK12316 1003 PEASVAQQ--GYVAPRNALERTLAAIWQDVLGV--ERVGLDDNFFELGGDSIVSIQVV 1056
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
188-677 |
8.95e-126 |
|
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: 391.32 E-value: 8.95e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFP 267
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 LERIAAMVTRSACGRALTDevgAAVTDRLGGlvpglRARGVDEILRGGHPSEVPGTPVV---AGQLAYIYFTSGSTGEPK 344
Cdd:cd17651 81 AERLAFMLADAGPVLVLTH---PALAGELAV-----ELVAVTLLDQPGAAAGADAEPDPaldADDLAYVIYTSGSTGRPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 345 GVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQ 424
Cdd:cd17651 153 GVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LVPSYVEVLLGHLERRPRALPALRCVSATGEALK-AALVRRWFAVLPEVLLVNAYGLTETCDDTNHEV-LDRAQDGSRVP 502
Cdd:cd17651 233 LPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLpGDPAAWPAPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 503 LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSG 582
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 583 RRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIV-AGAAESARLVACYSAAP--SLAPGPLVEALARVLPDYMVPRDWY 659
Cdd:cd17651 393 RADDQVKIRGFRIELGEIEAALARHPGVREAVVLArEDRPGEKRLVAYVVGDPeaPVDAAELRAALATHLPEYMVPSAFV 472
|
490
....*....|....*...
gi 502993051 660 WLDVLPLTGNGKVDRKEL 677
Cdd:cd17651 473 LLDALPLTPNGKLDRRAL 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
124-768 |
4.29e-125 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 421.67 E-value: 4.29e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 124 REWVDDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELPDRR-VHQLIADTAAARPDDVAVV 202
Cdd:PRK12316 4492 RGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRcVHQLVAERARMTPDAVAVV 4571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 203 AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGR 282
Cdd:PRK12316 4572 FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAAL 4651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 283 ALTDevgAAVTDRLgGLVPGLRARGVDEILR-GGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKI 361
Cdd:PRK12316 4652 LLTQ---SHLLQRL-PIPDGLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATG 4727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 362 DDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQaLLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRP 441
Cdd:PRK12316 4728 ERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDS-LWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG 4806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 442 RaLPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH-EVLDRAQDGSR-VPLGRAIAGVGVHVVDGNL 519
Cdd:PRK12316 4807 E-PPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLwKARDGDACGAAyMPIGTPLGNRSGYVLDGQL 4885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 520 MPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPL-FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIG 598
Cdd:PRK12316 4886 NPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELG 4965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 599 EIEDRLLRLPGVREATVIVAGAAESARLVA-CYSAAPSLAPGP---------LVEALARVLPDYMVPRDWYWLDVLPLTG 668
Cdd:PRK12316 4966 EIEARLREHPAVREAVVIAQEGAVGKQLVGyVVPQDPALADADeaqaelrdeLKAALRERLPEYMVPAHLVFLARMPLTP 5045
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 669 NGKVDRKELARITGG-LHRAMTEderPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLV----IELDRA 743
Cdd:PRK12316 5046 NGKLDRKALPQPDASlLQQAYVA---PRSELEQQVAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTsriqLELGLE 5120
|
650 660
....*....|....*....|....*
gi 502993051 744 VSLGDVTAHPVLADLAGVLGTGATG 768
Cdd:PRK12316 5121 LPLRELFQTPTLAAFVELAAAAGSG 5145
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
209-615 |
1.10e-124 |
|
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: 385.47 E-value: 1.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDE 287
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 VGAAVTDRLGgLVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:TIGR01733 81 ALASRLAGLV-LPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSR-VEVAQLVPSYVEVLlghLERRPRALPA 446
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALL---AAALPPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 LRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLDR--AQDGSRVPLGRAIAGVGVHVVDGNLMPVPL 524
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPddAPRESPVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 525 GATGEIVFSGRCLARGYVNDPIRTALAFTASPLFP--GQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIED 602
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
410
....*....|...
gi 502993051 603 RLLRLPGVREATV 615
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
128-927 |
1.88e-124 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 419.75 E-value: 1.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 128 DDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELP-DRRVHQLIADTAAARPDDVAVVAGLD 206
Cdd:PRK12316 1948 DAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPrGPGVHQRIAEQAARAPEAIAVVFGDQ 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTD 286
Cdd:PRK12316 2028 HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ 2107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 EvgaAVTDRLggLVP-GLRARGVDEILR-GGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDL 364
Cdd:PRK12316 2108 R---HLLERL--PLPaGVARLPLDRDAEwADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 365 GVRAGTVVAQTAPQCFDISLWQLLAPLITGGTvVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRAl 444
Cdd:PRK12316 2183 ELSPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRP- 2260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLDR--AQDGSRVPLGRAIAGVGVHVVDGNLMPV 522
Cdd:PRK12316 2261 PAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPqdPCGAAYVPIGRALGNRRAYILDADLNLL 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 523 PLGATGEIVFSGRCLARGYVNDPIRTALAFTASPL-FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIE 601
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 602 DRLLRLPGVREATVIVAGAAESARLVAcYSAAPSLA---PGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:PRK12316 2421 ARLQAHPAVREAVVVAQDGASGKQLVA-YVVPDDAAedlLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALP 2499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 679 RITGGLHRAMTedERPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLVIELDRA----VSLGDVTAHPV 754
Cdd:PRK12316 2500 KPDVSQLRQAY--VAPQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDlgleVPLRILFERPT 2575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 755 LADLAGVLGTGATGTRPVLHRLTPPgrrtlvcfpyaggnavtyVPLAGELAAE-GWAVYGVEPPGRDGNEAPVSVPELAE 833
Cdd:PRK12316 2576 LAAFAASLESGQTSRAPVLQKVTRV------------------QPLPLSHAQQrQWFLWQLEPESAAYHLPSALHLRGVL 2637
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 834 LVAGELAALDAGPLTLWGHSTGVAAALATARLLRSRGHDVRRVLLGAQLPGDSGARRAQAAEVTALPDEAVVTALvesgR 913
Cdd:PRK12316 2638 DQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLL----R 2713
|
810
....*....|....
gi 502993051 914 PELAEVGDAHRRLL 927
Cdd:PRK12316 2714 VRLLALDGQEHVLV 2727
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
129-989 |
6.62e-119 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 395.18 E-value: 6.62e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 129 DAYAAR--IADYHRTALRL------AAADPDAEHAGQCLLGAAElRHQLTAFSGAPRELPDRRVHQLIADTAAARPDDVA 200
Cdd:PRK10252 398 LANPQRydEATLIAHAERLkaliaqFAADPALLCGDVDILLPGE-YAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 201 VVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVtRSAC 280
Cdd:PRK10252 477 LADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML-EDAR 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 281 GRALTDEvgAAVTDRLGGlVPGLRARGVDEIL-RGGHPSEVPGTPvvaGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLA 359
Cdd:PRK10252 556 PSLLITT--ADQLPRFAD-VPDLTSLCYNAPLaPQGAAPLQLSQP---HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 360 KIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHL-- 437
Cdd:PRK10252 630 MQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLtp 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 438 ERRPRALPALRCVSATGEALKAALVRRWFAvLPEVLLVNAYGLTETCDDTNH-----EVLDrAQDGSRVPLGRAIAGVGV 512
Cdd:PRK10252 710 EGARQSCASLRQVFCSGEALPADLCREWQQ-LTGAPLHNLYGPTEAAVDVSWypafgEELA-AVRGSSVPIGYPVWNTGL 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 513 HVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRG 592
Cdd:PRK10252 788 RILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRG 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 593 FRVEIGEIEDRLLRLPGVREATVI-------VAGAAESARLVACYSAAPSLAP--GPLVEALARVLPDYMVPRDWYWLDV 663
Cdd:PRK10252 868 QRIELGEIDRAMQALPDVEQAVTHacvinqaAATGGDARQLVGYLVSQSGLPLdtSALQAQLRERLPPHMVPVVLLQLDQ 947
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 664 LPLTGNGKVDRK-----ELARITGGlhRAmtederPRPGAERRLAAAWATVLGVAPdrVGRTDDFFASGGSSLSALQLVI 738
Cdd:PRK10252 948 LPLSANGKLDRKalplpELKAQVPG--RA------PKTGTETIIAAAFSSLLGCDV--VDADADFFALGGHSLLAMKLAA 1017
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 739 ELD----RAVSLGDVTAHPVLADLAGVLGT-----GATGTRPVLhRLTPPGRRTLVCFPYAGGNAVTYVPLAGELAAEgW 809
Cdd:PRK10252 1018 QLSrqfaRQVTPGQVMVASTVAKLATLLDAeedesRRLGFGTIL-PLREGDGPTLFCFHPASGFAWQFSVLSRYLDPQ-W 1095
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 810 AVYGVEPPGRDGNEA-PVSVPELAE-LVAGELAALDAGPLTLWGHSTGVAAALATARLLRSRGHDVRRVLLGAQLPGDSG 887
Cdd:PRK10252 1096 SIYGIQSPRPDGPMQtATSLDEVCEaHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPETQ 1175
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 888 ARRAQAAevtALPDEAVVtALVESGRPELAEV--GDAHRRLLADAYRhDVAAACGYLAEALDAgdRLDVPVTVVLAADDV 965
Cdd:PRK10252 1176 NWREKEA---NGLDPEVL-AEIDREREAFLAAqqGSLSTELFTTIEG-NYADAVRLLTTAHSV--PFDGKATLFVAERTL 1248
|
890 900
....*....|....*....|....
gi 502993051 966 PDDlPGDPWDWSRLAGDVRVVELP 989
Cdd:PRK10252 1249 QEG-MSPEQAWSPWIAELDVYRQD 1271
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
196-677 |
1.08e-117 |
|
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: 368.12 E-value: 1.08e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALTdevgaavtdrlgglvpglrargvdeilrgghpsevpgtpvVAGQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd17652 81 ADARPALLLT----------------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLAN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLlg 435
Cdd:cd17652 121 LAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 hlerRPRALPALRCVSATGEALKAALVRRWfavLPEVLLVNAYGLTETCddTNHEVLDRAQDGSRVPLGRAIAGVGVHVV 515
Cdd:cd17652 199 ----PPDDLPDLRTLVVAGEACPAELVDRW---APGRRMINAYGPTETT--VCATMAGPLPGGGVPPIGRPVPGTRVYVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 516 DGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPL-FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFR 594
Cdd:cd17652 270 DARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 595 VEIGEIEDRLLRLPGVREATVIVAG-AAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLTGNGK 671
Cdd:cd17652 350 IELGEVEAALTEHPGVAEAVVVVRDdRPGDKRLVAYVVPAPGAAPTAaeLRAHLAERLPGYMVPAAFVVLDALPLTPNGK 429
|
....*.
gi 502993051 672 VDRKEL 677
Cdd:cd17652 430 LDRRAL 435
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
196-677 |
5.71e-117 |
|
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: 367.02 E-value: 5.71e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSAcgraltdevgaavtdrlgglvpglrargvdeilrgghPSEVPGTPvvaGQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd17643 81 ADSG-------------------------------------PSLLLTDP---DDLAYVIYTSGSTGRPKGVVVSHANVLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLG 435
Cdd:cd17643 121 LFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLERRPRALPALRCVSATGEALKAALVRRWFA--VLPEVLLVNAYGLTETCDDTNHEVLDRA--QDGSRVPLGRAIAGVG 511
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPLDAAdlPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 512 VHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLF-PGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKI 590
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 591 RGFRVEIGEIEDRLLRLPGVREATVIV-AGAAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLT 667
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDGAAADIaeLRALLKELLPDYMVPARYVPLDALPLT 440
|
490
....*....|
gi 502993051 668 GNGKVDRKEL 677
Cdd:cd17643 441 VNGKLDRAAL 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
159-747 |
4.57e-116 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 394.92 E-value: 4.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 159 LLGAAELRHQLTAFSGAPRELP-DRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAV 237
Cdd:PRK05691 3696 LLGEQERDFLLDGCNRSERDYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVAL 3775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 238 VSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRS---------AC---GRALTDEVGAAVTDRLggLVpglra 305
Cdd:PRK05691 3776 LAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSrtpvlvcsaACreqARALLDELGCANRPRL--LV----- 3848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 306 rgVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLW 385
Cdd:PRK05691 3849 --WEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVW 3926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 386 QLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEvllGHLERRPRALPALRCVSATGEALKAALVRRW 465
Cdd:PRK05691 3927 QFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQ---GMLAEDRQALDGLRWMLPTGEAMPPELARQW 4003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 466 FAVLPEVLLVNAYGLTETCDDTNHEVLDRAQ-DGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVND 544
Cdd:PRK05691 4004 LQRYPQIGLVNAYGPAECSDDVAFFRVDLAStRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGD 4083
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 545 PIRTALAFTASPL-FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAES 623
Cdd:PRK05691 4084 PLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG 4163
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 624 ARLVACYSAAPS-LAPGPLVEA----LARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARI-TGGLHRamTEDERPRPG 697
Cdd:PRK05691 4164 KHLVGYLVPHQTvLAQGALLERikqrLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALdIGQLQS--QAYLAPRNE 4241
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 502993051 698 AERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLVIELDRAVSLG 747
Cdd:PRK05691 4242 LEQTLATIWADVLKV--ERVGVHDNFFELGGHSLLATQIASRVQKALQRN 4289
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
196-677 |
1.32e-115 |
|
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: 363.92 E-value: 1.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALTDEVGAavtDRLGGLVPGLRARGvdeiLRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd12116 81 EDAEPALVLTDDALP---DRLPAGLPVLLLAL----AAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLG 435
Cdd:cd12116 154 FLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLERRPRALPALrcvsATGEALKAALVRRWFAVLPEvlLVNAYGLTETcddTNHEVLDRAQDGSR-VPLGRAIAGVGVHV 514
Cdd:cd12116 234 AGWQGRAGLTAL----CGGEALPPDLAARLLSRVGS--LWNLYGPTET---TIWSTAARVTAAAGpIPIGRPLANTQVYV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 515 VDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASP-LFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGF 593
Cdd:cd12116 305 LDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 594 RVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLTGNGK 671
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAaaLRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
....*.
gi 502993051 672 VDRKEL 677
Cdd:cd12116 465 LDRKAL 470
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
184-677 |
9.52e-115 |
|
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: 360.86 E-value: 9.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVE 263
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 264 PHFPLERIAAMVTRSACGRALTDevgaavtdrlgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEP 343
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTD----------------------------------------PDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 344 KGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVsqQALLDVEQFAAELDrsrVEVA 423
Cdd:cd12115 121 KGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLPAAAE---VTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 424 QLVPSYVEVLLGHlerrpRALPA-LRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTE-TCDDTNHEVldRAQDGSRV 501
Cdd:cd12115 196 NTVPSAAAELLRH-----DALPAsVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEdTTYSTVAPV--PPGASGEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 502 PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFS 581
Cdd:cd12115 269 SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 582 GRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAG-AAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDW 658
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAAGERRLVAYIVAEPGAAGLVedLRRHLGTRLPAYMVPSRF 428
|
490
....*....|....*....
gi 502993051 659 YWLDVLPLTGNGKVDRKEL 677
Cdd:cd12115 429 VRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
196-677 |
1.25e-112 |
|
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: 355.52 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGraltdevgaavtdrlgglvpglrargvdeILRGGHPSevpgtpvvagQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd17649 81 EDSGAG-----------------------------LLLTHHPR----------QLAYVIYTSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLG 435
Cdd:cd17649 122 HCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLERR-PRALPALRCVSATGEALKAALVRRWFAVlpEVLLVNAYGLTE-TCDDTNHEVLDRAQD-GSRVPLGRAIAGVGV 512
Cdd:cd17649 202 EADRTgDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEaTVTPLVWKCEAGAARaGASMPIGRPLGGRSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 513 HVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLF-PGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIR 591
Cdd:cd17649 280 YILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 592 GFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLAPGPLVE----ALARVLPDYMVPRDWYWLDVLPLT 667
Cdd:cd17649 360 GFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAqlrtALRASLPDYMVPAHLVFLARLPLT 439
|
490
....*....|
gi 502993051 668 GNGKVDRKEL 677
Cdd:cd17649 440 PNGKLDRKAL 449
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
186-679 |
1.32e-112 |
|
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: 354.69 E-value: 1.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPH 265
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRSACGRALTDevgAAVTDrlgglvpglrargvdeilrgghpsevpgtpvvagqLAYIYFTSGSTGEPKG 345
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTT---DSPDD-----------------------------------LAYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVivsqqaLLDVEQFAAELDRSrVEVAQL 425
Cdd:cd17653 123 VMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLV------LADPSDPFAHVART-VDALMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 426 VPSYVEVLlghlerRPRALPALRCVSATGEALKAALVRRWfavLPEVLLVNAYGLTE-TCDDTNHEVLDraqdGSRVPLG 504
Cdd:cd17653 196 TPSILSTL------SPQDFPNLKTIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTEcTISSTMTELLP----GQPVTIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 505 RAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRR 584
Cdd:cd17653 263 KPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 585 DTQVKIRGFRVEIGEIEDRLLRL-PGVREATVIVAgaaeSARLVACYSAApSLAPGPLVEALARVLPDYMVPRDWYWLDV 663
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVV----NGRLVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDS 417
|
490
....*....|....*.
gi 502993051 664 LPLTGNGKVDRKELAR 679
Cdd:cd17653 418 FPLTANGKVDRKALRE 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
125-737 |
8.42e-112 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 382.21 E-value: 8.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 125 EWVDDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAElRHQLTAFSGAPRELPDRRVHQLIADTAAARPDDVAVVAG 204
Cdd:PRK05691 1075 ELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAE-RAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIALVWD 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 205 LDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRAL 284
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 285 TDevgAAVTDRLGGlVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDL 364
Cdd:PRK05691 1234 TQ---SHLLERLPQ-AEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 365 GVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGhlERRPRAL 444
Cdd:PRK05691 1310 ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID--EPLAAAC 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLdRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPL 524
Cdd:PRK05691 1388 TSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQC-QAEDGERSPIGRPLGNVLCRVLDAELNLLPP 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 525 GATGEIVFSGRCLARGYVNDPIRTALAFTASPLF-PGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDR 603
Cdd:PRK05691 1467 GVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQAR 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 604 LLRLPGVREATVIVAGAAESARLVACYS--AAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARiT 681
Cdd:PRK05691 1547 LLAQPGVAQAAVLVREGAAGAQLVGYYTgeAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE-P 1625
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 682 GGLHRAMTEderPRPGAERRLAAAWATVLGVApdRVGRTDDFFASGGSSLSALQLV 737
Cdd:PRK05691 1626 VWQQREHVE---PRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIV 1676
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
124-766 |
2.11e-110 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 378.15 E-value: 2.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 124 REWVDDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELP-DRRVHQLIADTAAARPDDVAVV 202
Cdd:PRK12316 2998 TDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPlERGVHRLFEEQVERTPDAVALA 3077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 203 AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGR 282
Cdd:PRK12316 3078 FGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQL 3157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 283 ALTDEvgAAVTDRLGGLVPGLRARGVDeilrgGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKID 362
Cdd:PRK12316 3158 LLSQS--HLRLPLAQGVQVLDLDRGDE-----NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ 3230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 363 DLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGhlERRPR 442
Cdd:PRK12316 3231 AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE--EEDAH 3308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 443 ALPALRCVSATGEALKAALVRRWFAVLPevlLVNAYGLTETCDDTNHEVLDRAQDGSrVPLGRAIAGVGVHVVDGNLMPV 522
Cdd:PRK12316 3309 RCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEGKDA-VPIGRPIANRACYILDGSLEPV 3384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 523 PLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIED 602
Cdd:PRK12316 3385 PVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEA 3464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 603 RLLRLPGVREATVI-VAGAAESARLVAcySAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARIT 681
Cdd:PRK12316 3465 RLLEHPWVREAVVLaVDGRQLVAYVVP--EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPD 3542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 682 GGLHRamTEDERPRPGAERRLAAAWATVLGVApdRVGRTDDFFASGGSSLSALQLVIELDRA---VSLGDVTAHPVLADL 758
Cdd:PRK12316 3543 AALLQ--QDYVAPVNELERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAgirFTPKDLFQHQTIQGL 3618
|
....*...
gi 502993051 759 AGVLGTGA 766
Cdd:PRK12316 3619 ARVARVGG 3626
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
184-677 |
1.10e-107 |
|
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: 342.88 E-value: 1.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVE 263
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 264 PHFPLERIAAMvtrsacgraltdevgaavtdrlgglvpgLRARGVDEILRGGHpsevpgtpvvagQLAYIYFTSGSTGEP 343
Cdd:cd17644 82 PNYPQERLTYI----------------------------LEDAQISVLLTQPE------------NLAYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 344 KGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVA 423
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 424 QLVPSYVEVLLGHLERRPRALP-ALRCVSATGEALKAALVRRWF-AVLPEVLLVNAYGLTE-TCDDTNHEVLDRAQDGS- 499
Cdd:cd17644 202 SLPPAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQPELVRQWQkNVGNFIQLINVYGPTEaTIAATVCRLTQLTERNIt 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 500 RVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLF--PGQRLYRSGDFGRWTPDGR 577
Cdd:cd17644 282 SVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 578 LEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIV-AGAAESARLVAcYSAAP---SLAPGPLVEALARVLPDYM 653
Cdd:cd17644 362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVrEDQPGNKRLVA-YIVPHyeeSPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....
gi 502993051 654 VPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
192-677 |
1.18e-107 |
|
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: 342.30 E-value: 1.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERI 271
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 272 AAMVTRSACGRALTDEvgaavtdrlgglvpglrargvDEilrgghpsevpgtpvvagqLAYIYFTSGSTGEPKGVMCEHE 351
Cdd:cd05945 81 REILDAAKPALLIADG---------------------DD-------------------NAYIIFTSGSTGRPKGVQISHD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 352 GML---NHMLAkidDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPS 428
Cdd:cd05945 121 NLVsftNWMLS---DFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 429 YVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDD-TNHEVLDRAQDGS-RVPLGRA 506
Cdd:cd05945 198 FAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAvTYIEVTPEVLDGYdRLPIGYA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 507 IAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTaspLFPGQRLYRSGDFGRWTPDGRLEFSGRRDT 586
Cdd:cd05945 278 KPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 587 QVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESA-RLVACYSAAPSLAPGPLVE---ALARVLPDYMVPRDWYWLD 662
Cdd:cd05945 355 QVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtELIAFVVPKPGAEAGLTKAikaELAERLPPYMIPRRFVYLD 434
|
490
....*....|....*
gi 502993051 663 VLPLTGNGKVDRKEL 677
Cdd:cd05945 435 ELPLNANGKIDRKAL 449
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
196-677 |
2.54e-107 |
|
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: 342.33 E-value: 2.54e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALTDEVGAAVTDRLGGLVpglrargVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVL-------ILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLG 435
Cdd:cd12114 154 TILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTN-HEVLDRAQDGSRVPLGRAIAGVGVHV 514
Cdd:cd12114 234 VLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIyHPIDEVPPDWRSIPYGRPLANQRYRV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 515 VDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPlfPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFR 594
Cdd:cd12114 314 LDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 595 VEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSA---APSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGK 671
Cdd:cd12114 392 IELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPdndGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGK 471
|
....*.
gi 502993051 672 VDRKEL 677
Cdd:cd12114 472 VDRAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
184-680 |
1.83e-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: 340.29 E-value: 1.83e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAiPWL-VAVLGVLKAGGCYLPV 262
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKS-KWAvVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 263 EPHFPLERIAAMVTRSACGRALTDevgaavtdrlgglvpglrargvdeilrggHPSevpgtpvvagQLAYIYFTSGSTGE 342
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLTS-----------------------------SPS----------DAAYVIFTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 343 PKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDveQFAAELDRSRVEV 422
Cdd:cd05918 121 PKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 423 AQLVPSYVEVLlghlerRPRALPALRCVSATGEALKAALVRRWfavLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSRVp 502
Cdd:cd05918 199 AFLTPSVARLL------DPEDVPSLRTLVLGGEALTQSDVDTW---ADRVRLINAYGPAECTIAATVSPVVPSTDPRNI- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 503 lGRAIAGVgVHVVDGNLM--PVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLF-------PGQRLYRSGDFGRWT 573
Cdd:cd05918 269 -GRPLGAT-CWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWlkqegsgRGRRLYRTGDLVRYN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 574 PDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLR-LPGVREATVIV---AGAAESARLVACYSAAPSLAPGP--------- 640
Cdd:cd05918 347 PDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGdgdslflep 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502993051 641 ----------LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARI 680
Cdd:cd05918 427 sdefralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
196-677 |
1.47e-104 |
|
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: 334.05 E-value: 1.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALTDevgaavtdrlgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd17650 81 EDSGAKLLLTQ----------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRAGTVVA-QTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLL 434
Cdd:cd17650 121 AAHAWRREYELDSFPVRLlQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 435 GHLERRPRALPALRCVSATGEALKAalvrRWFAVLPEVL-----LVNAYGLTETCDDTNH--EVLDRAQDGSRVPLGRAI 507
Cdd:cd17650 201 AYVYRNGLDLSAMRLLIVGSDGCKA----QDFKTLAARFgqgmrIINSYGVTEATIDSTYyeEGRDPLGDSANVPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 508 AGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQ 587
Cdd:cd17650 277 PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 588 VKIRGFRVEIGEIEDRLLRLPGVREATVIV-AGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPL 666
Cdd:cd17650 357 VKIRGFRIELGEIESQLARHPAIDEAVVAVrEDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPL 436
|
490
....*....|.
gi 502993051 667 TGNGKVDRKEL 677
Cdd:cd17650 437 TPNGKVDRRAL 447
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
196-677 |
1.22e-100 |
|
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: 324.81 E-value: 1.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALT-DEVGAAVTDRLGGLVPglrargVDEILRGGHPSEVpGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGML 354
Cdd:cd17656 82 LDSGVRVVLTqRHLKSKLSFNKSTILL------EDPSISQEDTSNI-DYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 355 NHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLL 434
Cdd:cd17656 155 NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 435 GHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSRVPLGRAIAGVGVHV 514
Cdd:cd17656 235 SEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 515 VDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFR 594
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 595 VEIGEIEDRLLRLPGVREATVIVAGAAESAR-LVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKyLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
....
gi 502993051 674 RKEL 677
Cdd:cd17656 475 RKAL 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
185-677 |
5.91e-98 |
|
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: 316.03 E-value: 5.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 185 HQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEP 264
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 HFPLERIAAMVTRSACGRALTDevgaavtdrlgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEPK 344
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN----------------------------------------PDDLAYVIYTSGSTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 345 GVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQ 424
Cdd:cd17645 121 GVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LvPSYVEVLLGHLERRpralpALRCVSATGEALKAAlVRRWFAvlpevlLVNAYGLTE-TCDDTNHEVLDRAQDgsrVPL 503
Cdd:cd17645 201 L-PTGAAEQFMQLDNQ-----SLRVLLTGGDKLKKI-ERKGYK------LVNNYGPTEnTVVATSFEIDKPYAN---IPI 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 504 GRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGR 583
Cdd:cd17645 265 GKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 584 RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLAP-GPLVEALARVLPDYMVPRDWYWLD 662
Cdd:cd17645 345 LDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPhEELREWLKNDLPDYMIPTYFVHLK 424
|
490
....*....|....*
gi 502993051 663 VLPLTGNGKVDRKEL 677
Cdd:cd17645 425 ALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
124-774 |
1.57e-94 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 330.98 E-value: 1.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 124 REWVDDAYAARIADYHRTALRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELP-DRRVHQLIADTAAARPDDVAVV 202
Cdd:PRK05691 2129 RDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARlDQTLHGLFAAQAARTPQAPALT 2208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 203 AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGR 282
Cdd:PRK05691 2209 FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 283 ALTDevgAAVTDRLGGLVPGLrARGV---DEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLA 359
Cdd:PRK05691 2289 LLSD---RALFEALGELPAGV-ARWCledDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQA 2364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 360 KIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIvSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLER 439
Cdd:PRK05691 2365 VIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL-RAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAG 2443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 440 RPRALPALRCVSAtGEALKAALVRRWFAVLPEVLLVNAYGLTETCddtnheVLDRA--------QDGSRVPLGRAIAGVG 511
Cdd:PRK05691 2444 QGEQLPVRMCITG-GEALTGEHLQRIRQAFAPQLFFNAYGPTETV------VMPLAclapeqleEGAASVPIGRVVGARV 2516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 512 VHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFP-GQRLYRSGDFGRWTPDGRLEFSGRRDTQVKI 590
Cdd:PRK05691 2517 AYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKI 2596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 591 RGFRVEIGEIEDRLLRLPGVREAtVIVAGAAESARLVACYSAAPSLAPGPLVEALARV---------LPDYMVPRDWYWL 661
Cdd:PRK05691 2597 RGFRIELGEIESRLLEHPAVREA-VVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREalkahlkqqLPDYMVPAHLILL 2675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 662 DVLPLTGNGKVDRKELARITGGLHRamTEDERPRPGAERRLAAAWATVLGVapDRVGRTDDFFASGGSSLSALQLVielD 741
Cdd:PRK05691 2676 DSLPLTANGKLDRRALPAPDPELNR--QAYQAPRSELEQQLAQIWREVLNV--ERVGLGDNFFELGGDSILSIQVV---S 2748
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 502993051 742 RAVSLG------DVTAHPVLADLAGV------------LGTGATGTRPVLH 774
Cdd:PRK05691 2749 RARQLGihfsprDLFQHQTVQTLAAVathseaaqaeqgPLQGASGLTPIQH 2799
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
184-679 |
2.66e-94 |
|
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: 306.74 E-value: 2.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVE 263
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 264 PHFPLERIAAMVTRSacgraltdevGAAVtdrlgglvpglrargvdeilrgghpsevpgtpVVAgqlAYIYFTSGSTGEP 343
Cdd:COG0318 81 PRLTAEELAYILEDS----------GARA--------------------------------LVT---ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 344 KGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISL-WQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEV 422
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 423 AQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTETCDDTnHEVLDRAQDGSRVP 502
Cdd:COG0318 193 LFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVV-TVNPEDPGERRPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 503 LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTasplfpgQRLYRSGDFGRWTPDGRLEFSG 582
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 583 RRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALARVLPDYMVPRDWY 659
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgVPDEKWGERVVAFVVLRPgaELDAEELRAFLRERLARYKVPRRVE 423
|
490 500
....*....|....*....|
gi 502993051 660 WLDVLPLTGNGKVDRKELAR 679
Cdd:COG0318 424 FVDELPRTASGKIDRRALRE 443
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
196-677 |
6.46e-90 |
|
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: 295.08 E-value: 6.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADG-LAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAM 274
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 275 VTRSACGRALTDevgaaVTDrlgglvpglrargvdeilrgghpsevpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGML 354
Cdd:cd17648 81 LEDTGARVVITN-----STD-----------------------------------LAYAIYTSGTTGKPKGVLVEHGSVV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 355 NHM--LAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSyvev 432
Cdd:cd17648 121 NLRtsLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 433 LLGHLERRprALPALRCVSATGEALKAAL---VRRWFAVLpevlLVNAYGLTETCDdTNHEVLDRAQDGSRVPLGRAIAG 509
Cdd:cd17648 197 VLQQYDLA--RLPHLKRVDAAGEEFTAPVfekLRSRFAGL----IINAYGPTETTV-TNHKRFFPGDQRFDKSLGRPVRN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 510 VGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQ--------RLYRSGDFGRWTPDGRLEFS 581
Cdd:cd17648 270 TKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 582 GRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI------VAGAAESARLVACYSAAP-SLAPGPLVEALARVLPDYMV 654
Cdd:cd17648 350 GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasQAQSRIQKYLVGYYLPEPgHVPESDLLSFLRAKLPRYMV 429
|
490 500
....*....|....*....|...
gi 502993051 655 PRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd17648 430 PARLVRLEGIPVTINGKLDVRAL 452
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
188-591 |
2.75e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 289.21 E-value: 2.75e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQ-LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHF 266
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 267 PLERIAAMVTRSACGRALTDE-------VGAAVTDRLGGLV------PGLRARGVDEILRGGHPSEVPGTPVVAGQLAYI 333
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDalkleelLEALGKLEVVKLVlvldrdPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 334 YFTSGSTGEPKGVMCEHEGMLNHMLA----KIDDLGVRAGTVVAQTAPQCFDISL-WQLLAPLITGGTVVIVSQQALLDV 408
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 409 EQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVlLVNAYGLTETCDDTN 488
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 489 HEVLDRAQDGSRVPLGRAIAGVGVHVVDGNLM-PVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpgQRLYRSG 567
Cdd:pfam00501 320 TPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGePVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
|
410 420
....*....|....*....|....
gi 502993051 568 DFGRWTPDGRLEFSGRRDTQVKIR 591
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
188-678 |
4.30e-69 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 239.41 E-value: 4.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFP 267
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 LERIAaMVTRSACGRAL--TDEVGAAVTDrlgglVPGLRARGVDEILRGGhPSEVPGTPVVAGQLAYIYFTSGSTGEPKG 345
Cdd:PRK04813 88 AERIE-MIIEVAKPSLIiaTEELPLEILG-----IPVITLDELKDIFATG-NPYDFDHAVKGDDNYYIIFTSGTTGKPKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEGML---NHMlakIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEV 422
Cdd:PRK04813 161 VQISHDNLVsftNWM---LEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 423 AQLVPSYVEVLLGHLERRPRALPALR----CvsatGEALKAALVRRWFAVLPEVLLVNAYGLTETC--------DDtnhE 490
Cdd:PRK04813 238 WVSTPSFADMCLLDPSFNEEHLPNLThflfC----GEELPHKTAKKLLERFPSATIYNTYGPTEATvavtsieiTD---E 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 491 VLDRaqdGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplFPGQRLYRSGDFG 570
Cdd:PRK04813 311 MLDQ---YKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 571 RwTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATV---------------IVAGAAESARLVACYSAaps 635
Cdd:PRK04813 385 Y-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVvpynkdhkvqyliayVVPKEEDFEREFELTKA--- 460
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502993051 636 lapgpLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:PRK04813 461 -----IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALI 498
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
329-673 |
3.14e-64 |
|
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: 220.62 E-value: 3.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 329 QLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQallDV 408
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 409 EQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRwFAVLPEVLLVNAYGLTETCDDTN 488
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 489 HEVLDrAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFtasplfpGQRLYRSGD 568
Cdd:cd04433 157 TGPPD-DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 569 FGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPGP--LVEAL 645
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGERVVAVVVLRPGADLDAeeLRAHV 308
|
330 340
....*....|....*....|....*...
gi 502993051 646 ARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:cd04433 309 RERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
184-760 |
5.29e-55 |
|
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: 209.15 E-value: 5.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVV---------AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLK 254
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 255 AGGCYLPVEPHFPLER------IA---AMVTRSACGRaLTDEVGAAVTDRLG--GLVPGLRARGvDEILRGGHPSEvPGT 323
Cdd:TIGR03443 318 AGATFSVIDPAYPPARqtiylsVAkprALIVIEKAGT-LDQLVRDYIDKELElrTEIPALALQD-DGSLVGGSLEG-GET 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 324 PVVAGQLAY----------------IYFTSGSTGEPKGVMCEHEGMLNHM--LAKIDDLGVRAG-TVVAQTA--PQCFDI 382
Cdd:TIGR03443 395 DVLAPYQALkdtptgvvvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFpwMAKRFGLSENDKfTMLSGIAhdPIQRDM 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 383 slwqlLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERrprALPALRCVSATGEALKAALV 462
Cdd:TIGR03443 475 -----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATT---PIPSLHHAFFVGDILTKRDC 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 463 RRWFAVLPEVLLVNAYGLTETCDDTNH-EVLDRAQDGSR-------VPLGRAIAGVGVHVVDGN--LMPVPLGATGEIVF 532
Cdd:TIGR03443 547 LRLQTLAENVCIVNMYGTTETQRAVSYfEIPSRSSDSTFlknlkdvMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 533 SGRCLARGYVNDPIRTALAFT----ASP------------------LFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKI 590
Cdd:TIGR03443 627 RAGGLAEGYLGLPELNAEKFVnnwfVDPshwidldkennkperefwLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKI 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 591 RGFRVEIGEIEDRLLRLPGVREATVIV-----------------AGAAESARLVACYSAAPSLAP--------GPLV--- 642
Cdd:TIGR03443 707 RGFRIELGEIDTHLSQHPLVRENVTLVrrdkdeeptlvsyivpqDKSDELEEFKSEVDDEESSDPvvkglikyRKLIkdi 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 643 -EALARVLPDYMVPRDWYWLDVLPLTGNGKVDR--------KELArITGGLHRAMTEDERPRPgAERRLAAAWATVLGVA 713
Cdd:TIGR03443 787 rEYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKpalpfpdtAQLA-AVAKNRSASAADEEFTE-TEREIRDLWLELLPNR 864
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 502993051 714 PDRVGRTDDFFASGGSSLSALQLVIELDRA----VSLGDVTAHPVLADLAG 760
Cdd:TIGR03443 865 PATISPDDSFFDLGGHSILATRMIFELRKKlnveLPLGLIFKSPTIKGFAK 915
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
191-674 |
5.65e-53 |
|
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: 191.67 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 191 TAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPhfpler 270
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 271 iaamvtrsacgRALTDEVGAAVTDrlgglvpglrargvdeilrgghpsevPGTPVVAGQLAYIYFTSGSTGEPKGVMCEH 350
Cdd:cd17631 78 -----------RLTPPEVAYILAD--------------------------SGAKVLFDDLALLMYTSGTTGRPKGAMLTH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 351 EGMLNHMLAKIDDLGVRAGTVVAQTAP--QCFDISLWqLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPS 428
Cdd:cd17631 121 RNLLWNAVNALAALDLGPDDVLLVVAPlfHIGGLGVF-TLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 429 YVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVlpEVLLVNAYGLTETCddTNHEVLDRA-QDGSRVPLGRAI 507
Cdd:cd17631 197 MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETS--PGVTFLSPEdHRRKLGSAGRPV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 508 AGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQ 587
Cdd:cd17631 273 FFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-------WFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 588 VKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALARVLPDYMVPRDWYWLDVL 664
Cdd:cd17631 346 IISGGENVYPAEVEDVLYEHPAVAEVAVIgVPDEKWGEAVVAVVVPRPgaELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
490
....*....|
gi 502993051 665 PLTGNGKVDR 674
Cdd:cd17631 426 PRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
184-677 |
2.14e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 186.55 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVV---SERAipwLVAVLGVLKAGGCYL 260
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFdwnSHEY---LEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 261 PVEPHFPLERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLRARGVD---------------EILRGGHPSEVPGTPV 325
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEgdgpaaplapevgeyEELLAAASDTFDFPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 326 VAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDISLWQL-LAPLITGGTVVIVSQqa 404
Cdd:PRK06187 165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVP-MFHVHAWGLpYLALMAGAKQVIPRR-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 405 lLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTETC 484
Cdd:PRK06187 242 -FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 485 ----------DDTNHEVLDRAQdgsrvplGRAIAGVGVHVVDGNLMPVP--LGATGEIVFSGRCLARGYVNDPIRTALAF 552
Cdd:PRK06187 320 pvvsvlppedQLPGQWTKRRSA-------GRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 553 TASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYS 631
Cdd:PRK06187 393 DGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgVPDEKWGERPVAVVV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502993051 632 AAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK06187 466 LKPGATLDAkeLRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
186-677 |
1.13e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 178.56 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPH 265
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRS------ACGRAL-TDEVGAAVTDRLGGLV---------PGLRARGVDEILRGGHPSEVpGTPVVAGQ 329
Cdd:PRK07656 89 YTADEAAYILARGdakalfVLGLFLgVDYSATTRLPALEHVViceteeddpHTEKMKTFTDFLAAGDPAER-APEVDPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 330 LAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQ----CFDISLwqlLAPLITGGTVVIVSQQAL 405
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFfhvfGYKAGV---NAPLMRGATILPLPVFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 406 LDVEQFAAEldrSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCD 485
Cdd:PRK07656 245 DEVFRLIET---ERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 486 DTNHEVLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLfpgqrLYr 565
Cdd:PRK07656 322 VTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW-----LH- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 566 SGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAA---PSLAPGPLV 642
Cdd:PRK07656 396 TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLkpgAELTEEELI 475
|
490 500 510
....*....|....*....|....*....|....*
gi 502993051 643 EALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK07656 476 AYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
192-690 |
1.40e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 179.54 E-value: 1.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLD-----QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVephF 266
Cdd:COG0365 19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV---F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 267 PL-------ERIA-----AMVT-----RSACGRALTDEVGAA-----------VTDRLGGLVPGLRARGVDEILRGgHPS 318
Cdd:COG0365 96 PGfgaealaDRIEdaeakVLITadgglRGGKVIDLKEKVDEAleelpslehviVVGRTGADVPMEGDLDWDELLAA-ASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 319 EVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDD-LGVRAGTVVAQTApqcfDISlWQ------LLAPL 391
Cdd:COG0365 175 EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTA----DIG-WAtghsyiVYGPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 392 ITGGTVVIV-SQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRA--LPALRCVSATGEALKAALVRRWFAV 468
Cdd:COG0365 250 LNGATVVLYeGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydLSSLRLLGSAGEPLNPEVWEWWYEA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 469 LpEVLLVNAYGLTETCddtnHEVLDRAQDGSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRC--LARGYVND 544
Cdd:COG0365 330 V-GVPIVDGWGQTETG----GIFISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWND 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 545 PIRTALAFTASplFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAES 623
Cdd:COG0365 405 PERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVgVPDEIRG 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993051 624 ARLVACYSAAPSLAPGP-----LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARITGGLHRAMTE 690
Cdd:COG0365 481 QVVKAFVVLKPGVEPSDelakeLQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDTS 552
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-678 |
4.38e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 175.32 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 215 ERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGC----YLPVEPHFPLERIAAMVTRSACGRALTDevgA 290
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLAD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 291 AVTDRLGGLVPGLRARG----VDEILRGGHPseVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGV 366
Cdd:cd05922 78 GAADRLRDALPASPDPGtvldADGIRAARAS--APAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 367 RAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIvSQQALLDvEQFAAELDRSRVEVAQLVPSYVEVLLgHLERRPRALPA 446
Cdd:cd05922 156 TADDRALTVLPLSYDYGLSVLNTHLLRGATLVL-TNDGVLD-DAFWEDLREHGATGLAGVPSTYAMLT-RLGFDPAKLPS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 LRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTN----HEVLDRAqdGSrvpLGRAIAGVGVHVVDGNLMPV 522
Cdd:cd05922 233 LRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTylppERILEKP--GS---IGLAIPGGEFEILDDDGTPT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 523 PLGATGEIVFSGRCLARGYVNDPirtalAFTASPLFPGQRLYrSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIED 602
Cdd:cd05922 308 PPGEPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 603 RLLRLPGVREATVIVAGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:cd05922 382 AARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
186-677 |
6.97e-42 |
|
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: 160.42 E-value: 6.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPH 265
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRSacgraltdevGAAVtdrlgglvpGLRARGVDEILRGGHPsEVPGTPVVAGQLAYIYFTSGSTGEPKG 345
Cdd:cd05936 83 YTPRELEHILNDS----------GAKA---------LIVAVSFTDLLAAGAP-LGERVALTPEDVAVLQYTSGTTGVPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEGMLNHMLAKIDDLGV--RAGTVV----------AQTApqcfdislwQLLAPLITGGTVVIVSQqalLDVEQFAA 413
Cdd:cd05936 143 AMLTHRNLVANALQIKAWLEDllEGDDVVlaalplfhvfGLTV---------ALLLPLALGATIVLIPR---FRPIGVLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 414 ELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTETCDDT--NHev 491
Cdd:cd05936 211 EIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVavNP-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 492 ldraQDGSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLfpgqrlyRSGDF 569
Cdd:cd05936 288 ----LDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 570 GRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVAcysAAPSLAPGP------LVE 643
Cdd:cd05936 357 GYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVK---AFVVLKEGAslteeeIIA 433
|
490 500 510
....*....|....*....|....*....|....
gi 502993051 644 ALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05936 434 FCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
206-672 |
3.06e-41 |
|
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: 158.92 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 206 DQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALT 285
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 D----EVGAAVTDRLG---------GLVPGLRARG-VDEILRGGHPSEVPGTPVVAG-QLAYIYFTSGSTGEPKGVMCEH 350
Cdd:cd05911 89 DpdglEKVKEAAKELGpkdkiivldDKPDGVLSIEdLLSPTLGEEDEDLPPPLKDGKdDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 351 EGMLNHMLAKIDDLGVRAGTVVAQTAPQCFD-IS-LWQLLAPLITGGTVVIVSQQallDVEQFAAELDRSRVEVAQLVPS 428
Cdd:cd05911 169 RNLIANLSQVQTFLYGNDGSNDVILGFLPLYhIYgLFTTLASLLNGATVIIMPKF---DSELFLDLIEKYKITFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 429 YVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSrvpLGRAIA 508
Cdd:cd05911 246 IAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGS---VGRLLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 509 GVGVHVVDGNLMP-VPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpgQRLYRSGDFGRWTPDGRLEFSGRRDTQ 587
Cdd:cd05911 323 NVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYLYIVDRKKEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 588 VKIRGFRVEIGEIEDRLLRLPGVREATVI---VAGAAESARlvacysAAPSLAPGPLVEALArvLPDYMVPR--DWYWL- 661
Cdd:cd05911 397 IKYKGFQVAPAELEAVLLEHPGVADAAVIgipDEVSGELPR------AYVVRKPGEKLTEKE--VKDYVAKKvaSYKQLr 468
|
490
....*....|....*..
gi 502993051 662 ------DVLPLTGNGKV 672
Cdd:cd05911 469 ggvvfvDEIPKSASGKI 485
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
209-677 |
3.91e-41 |
|
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: 159.22 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLER--IAAMVTRSAcgraltd 286
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARqnIYLGVAKPR------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 evgaavtdrlgGLVpGLRARGVdeiLRGghPSEVPGtpvvagqlayIYFTSGSTGEPKGVMCEHEGM---LNHM-----L 358
Cdd:cd17647 95 -----------GLI-VIRAAGV---VVG--PDSNPT----------LSFTSGSEGIPKGVLGRHFSLayyFPWMakrfnL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 359 AKIDDLGVRAGtvVAQTAPQcfdislWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLE 438
Cdd:cd17647 148 SENDKFTMLSG--IAHDPIQ------RDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQAT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 439 RrprALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH-EVLDRAQDGSR-------VPLGRAIAGV 510
Cdd:cd17647 220 T---PFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYfEVPSRSSDPTFlknlkdvMPAGRGMLNV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 511 GVHVVDGN--LMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAS-----------------P-----LFPGQRLYRS 566
Cdd:cd17647 297 QLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnePwrqfwLGPRDRLYRT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 567 GDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACY-----------SAAPS 635
Cdd:cd17647 377 GDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYivprfdkpddeSFAQE 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993051 636 LAPG-----PLVEALARV--------------LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd17647 457 DVPKevstdPIVKGLIGYrklikdireflkkrLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
208-677 |
1.35e-40 |
|
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: 156.09 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDE 287
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 VgaavtdrlgglvpglrargVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd17654 97 E-------------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELD-RSRVEVAQLVPSYVEVLLGHL--ERRPRAL 444
Cdd:cd17654 158 SEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFkRHRITVLQATPTLFRRFGSQSikSTVLSAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEAL-KAALVRRWFAVLPEVLLVNAYGLTET-CDDTNHEVLDraqDGSRVPLGRAIAGVGVHVVDGNLMPV 522
Cdd:cd17654 238 SSLRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVsCWALAYKVPE---EDSPVQLGSPLLGTVIEVRDQNGSEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 523 plgaTGEiVF----SGRCLARGYVNDPIRTalaftasplfpgqrLYRSGDFGRWTpDGRLEFSGRRDTQVKIRGFRVEIG 598
Cdd:cd17654 315 ----TGQ-VFlgglNRVCILDDEVTVPKGT--------------MRATGDFVTVK-DGELFFLGRKDSQIKRRGKRINLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 599 EIEDRLLRLPGVrEATVIVAGAAEsaRLVACYSAAPSLAPG----PLVEALARVLPDYMVprdwyWLDVLPLTGNGKVDR 674
Cdd:cd17654 375 LIQQVIESCLGV-ESCAVTLSDQQ--RLIAFIVGESSSSRIhkelQLTLLSSHAIPDTFV-----QIDKLPLTSHGKVDK 446
|
...
gi 502993051 675 KEL 677
Cdd:cd17654 447 SEL 449
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
208-677 |
7.54e-40 |
|
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: 153.69 E-value: 7.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVePHFPLERIAAMVTRSACGRALtde 287
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI-LPFFREHELAFILRRAKAKVF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 vgaavtdrlggLVPGLrargvdeiLRGGHPSEVPGtpvvagQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd05903 78 -----------VVPER--------FRQFDPAAMPD------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTAPQCFDI-SLWQLLAPLITGGTVVIvsqQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPA 446
Cdd:cd05903 133 PGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 LRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTETCDDTNHEVLDRAQDGSRVPlGRAIAGVGVHVVDGNLMPVPLGA 526
Cdd:cd05903 210 LRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD-GRPLPGVEIKVVDDTGATLAPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 527 TGEIVFSGRCLARGYVNDPIRTALAFTasplfpgQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLR 606
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAP-------EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993051 607 LPGVREATVIvagAAESARLVACYSAAPSLAPG--PLVEALARVLPDYMVPRdWYW------LDVLPLTGNGKVDRKEL 677
Cdd:cd05903 361 HPGVIEAAVV---ALPDERLGERACAVVVTKSGalLTFDELVAYLDRQGVAK-QYWperlvhVDDLPRTPSGKVQKFRL 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
192-673 |
1.76e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 154.66 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGC-------YLPVEP 264
Cdd:PRK07798 13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVpvnvnyrYVEDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 HFPLE--RIAAMVTrsacGRALTDEVgAAVTDRLGGL----------VPGLRARGVD--EILRGGHPSEVPGTPvvAGQL 330
Cdd:PRK07798 93 RYLLDdsDAVALVY----EREFAPRV-AEVLPRLPKLrtlvvvedgsGNDLLPGAVDyeDALAAGSPERDFGER--SPDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHE-------GMLNHMLAK-IDDLGVRAGTVVAQTAPQCFDIS-------LWQLLAPLITGG 395
Cdd:PRK07798 166 LYLLYTGGTTGMPKGVMWRQEdifrvllGGRDFATGEpIEDEEELAKRAAAGPGMRRFPAPplmhgagQWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 396 TVVIVSQQAlLDVEQFAAELDRSRVEVAQLV-PSYVEVLLGHLE-RRPRALPALRCVSATGEALKAALVRRWFAVLPEVL 473
Cdd:PRK07798 246 TVVLLPDVR-FDADEVWRTIEREKVNVITIVgDAMARPLLDALEaRGPYDLSSLFAIASGGALFSPSVKEALLELLPNVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 474 LVNAYGLTETCDDTNHEVLDRAQ--DGSRVPLGRaiagvGVHVVDGNLMPVPLG--ATGEIVFSGRcLARGYVNDPIRTA 549
Cdd:PRK07798 325 LTDSIGSSETGFGGSGTVAKGAVhtGGPRFTIGP-----RTVVLDEDGNPVEPGsgEIGWIARRGH-IPLGYYKDPEKTA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 550 LAFtasPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVreATVIVAGAAeSARLVAC 629
Cdd:PRK07798 399 ETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV--ADALVVGVP-DERWGQE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502993051 630 YSAAPSLAPGP------LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:PRK07798 473 VVAVVQLREGArpdlaeLRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-677 |
5.37e-38 |
|
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: 147.82 E-value: 5.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 206 DQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALT 285
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 DevgaavtdrlgglvpglrargvdeilrgghpsevpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLG 365
Cdd:cd05934 82 D-------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 366 VRAGTVvAQTAPQCFDIS--LWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRA 443
Cdd:cd05934 119 LGEDDV-YLTVLPLFHINaqAVSVLAALSVGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 444 LPALRCV--SATGEALKAALVRRWfavlpEVLLVNAYGLTETCddtnHEVLdRAQDGSRVP--LGRAIAGVGVHVVDGNL 519
Cdd:cd05934 195 AHRLRAAygAPNPPELHEEFEERF-----GVRLLEGYGMTETI----VGVI-GPRDEPRRPgsIGRPAPGYEVRIVDDDG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 520 MPVPLGATGEIV---FSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVE 596
Cdd:cd05934 265 QELPAGEPGELVirgLRGWGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 597 IGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAP---SLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:cd05934 338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgeTLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417
|
....
gi 502993051 674 RKEL 677
Cdd:cd05934 418 KAQL 421
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
189-682 |
7.86e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 143.73 E-value: 7.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 189 ADTAAARPDDVAVVAGLD-QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFp 267
Cdd:PRK06087 30 QQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 leRIAAMV-TRSACGR-------------------ALTDEV----GAAVTDRLGglvPGLRARGVDEILRGGHPSEVPgT 323
Cdd:PRK06087 109 --REAELVwVLNKCQAkmffaptlfkqtrpvdlilPLQNQLpqlqQIVGVDKLA---PATSSLSLSQIIADYEPLTTA-I 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 324 PVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQ-LLAPLITGGTVVIvsq 402
Cdd:PRK06087 183 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGARSVL--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 403 QALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRwfAVLPEVLLVNAYGLTE 482
Cdd:PRK06087 260 LDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARE--CQQRGIKLLSVYGSTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 483 TCDdtnHEVLDRAQDGSRV--PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpg 560
Cdd:PRK06087 338 SSP---HAVVNLDDPLSRFmhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 561 QRLYRSGDFGRWTPDGRLEFSGRRdTQVKIRGFR-VEIGEIEDRLLRLPGVREATVIvagAAESARL--VACYSAAP--- 634
Cdd:PRK06087 409 EGWYYSGDLCRMDEAGYIKITGRK-KDIIVRGGEnISSREVEDILLQHPKIHDACVV---AMPDERLgeRSCAYVVLkap 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502993051 635 --SLAPGPLVEALARV-LPDYMVPRDWYWLDVLPLTGNGKVD----RKELARITG 682
Cdd:PRK06087 485 hhSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQkfllRKDIMRRLT 539
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
196-678 |
1.26e-35 |
|
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: 142.45 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLD--QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLER--- 270
Cdd:cd05926 1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEfef 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 271 ----------IAAMVTRSACGRALTDEVGAAVtdRLGGLVPGLRARGVDEILRG---GHPSEVPGTPVVAGQLAYIYFTS 337
Cdd:cd05926 81 yladlgsklvLTPKGELGPASRAASKLGLAIL--ELALDVGVLIRAPSAESLSNllaDKKNAKSEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 338 GSTGEPKGVMCEHEGMLN--HMLAKIDDLGVRAGTVVaqTAPqCFDIS--LWQLLAPLITGGTVVIvsqQALLDVEQFAA 413
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAAsaTNITNTYKLTPDDRTLV--VMP-LFHVHglVASLLSTLAAGGSVVL---PPRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 414 ELDRSRVEVAQLVPSYVEVLLGHLERRPR-ALPALRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTETCddtnHEVL 492
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPEsPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAA----HQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 493 DRAQDGSRVPLGRAIAGVGVHVV----DGNlmPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGD 568
Cdd:cd05926 308 SNPLPPGPRKPGSVGKPVGVEVRildeDGE--ILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWF------RTGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 569 FGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACY---SAAPSLAPGPLVEAL 645
Cdd:cd05926 380 LGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAvvlREGASVTEEELRAFC 459
|
490 500 510
....*....|....*....|....*....|...
gi 502993051 646 ARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:cd05926 460 RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
192-677 |
4.67e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 141.72 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHF----- 266
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFrehel 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 267 -------------PLERIAAMV--TRSACG------RALTDEVGAAVTDRLGGLV--PGLRARGVDEILRG--GHPSEVP 321
Cdd:PRK06178 123 syelndagaevllALDQLAPVVeqVRAETSlrhvivTSLADVLPAEPTLPLPDSLraPRLAAAGAIDLLPAlrACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 322 GTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLnHMLAKIDDLGVRAGT--VVAQTAPQcfdisLW------QLLAPLIT 393
Cdd:PRK06178 203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGGEdsVFLSFLPE-----FWiagenfGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 394 GGTVVIVsqqALLDVEQFAAELDRSRVEV-AQLVPSYVEvLLGHLERRPRALPALRCVSATGEALK--AALVRRWFAVLP 470
Cdd:PRK06178 277 GATLVLL---ARWDAVAFMAAVERYRVTRtVMLVDNAVE-LMDHPRFAEYDLSSLRQVRVVSFVKKlnPDYRQRWRALTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 471 EVLLVNAYGLTE--TCDD--TNHEVLDRAQDGSRVPLGRAIAGVGVHVVDGNL-MPVPLGATGEIVFSGRCLARGYVNDP 545
Cdd:PRK06178 353 SVLAEAAWGMTEthTCDTftAGFQDDDFDLLSQPVFVGLPVPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNKP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 546 IRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAAESAR 625
Cdd:PRK06178 433 EATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV--GRPDPDK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 626 ---LVACYSAAP--SLAPGPLVEALARVLPDYMVPrDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK06178 504 gqvPVAFVQLKPgaDLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
181-677 |
7.07e-35 |
|
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: 139.77 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 181 DRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYL 260
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 261 PVEPHFPLERIAAMVtrsacgrALTDEVGAAVTDRLGGLVPGLRARGVDEilrgghpsEVPgtpvvagQLAYIYFTSGST 340
Cdd:cd05920 94 LALPSHRRSELSAFC-------AHAEAVAYIVPDRHAGFDHRALARELAE--------SIP-------EVALFLLSGGTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 341 GEPKGVMCEHEGMLNHMLAKIDDLGVRAGTV--VAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVeqFAAeLDRS 418
Cdd:cd05920 152 GTPKLIPRTHNDYAYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAA--FPL-IERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 419 RVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRwfavLPEVL---LVNAYGLTE-----TCDDTNHE 490
Cdd:cd05920 229 GVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARR----VPPVLgctLQQVFGMAEgllnyTRLDDPDE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 491 VLDRAQdgsrvplGRAI-AGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpgQRLYRSGDF 569
Cdd:cd05920 305 VIIHTQ-------GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP------DGFYRTGDL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 570 GRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAE----SARLVACYSAAPSLApgPLVEAL 645
Cdd:cd05920 372 VRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlgerSCAFVVLRDPPPSAA--QLRRFL 449
|
490 500 510
....*....|....*....|....*....|...
gi 502993051 646 -ARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05920 450 rERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
209-677 |
4.74e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 136.41 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDEv 288
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 289 gaavtdrlgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHM--LAKIDDLGV 366
Cdd:cd05971 87 --------------------------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLpgVQFPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 367 RAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPA 446
Cdd:cd05971 129 RDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 LRCVSATGEALKAALV---RRWFAVLpevllVN-AYGLTET-CDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMP 521
Cdd:cd05971 209 LRAIATGGESLGEELLgwaREQFGVE-----VNeFYGQTECnLVIGNCSALFPIKPGS---MGKPIPGHRVAIVDDNGTP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 522 VPLGATGEIvfsgrCLAR-------GYVNDPIRTALAFTASPLfpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFR 594
Cdd:cd05971 281 LPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 595 VEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAapsLAPGPL-VEALARVLPDYM--------VPRDWYWLDVLP 665
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV---LNPGETpSDALAREIQELVktrlaaheYPREIEFVNELP 425
|
490
....*....|..
gi 502993051 666 LTGNGKVDRKEL 677
Cdd:cd05971 426 RTATGKIRRREL 437
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
208-677 |
2.90e-33 |
|
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: 134.00 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVephFPLERIAAMVTRSACGRAltde 287
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL---TTLLGPKDIEYRLEAAGA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 vGAAVTDrlgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd05972 74 -KAIVTD--------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTAPQCFDISLW-QLLAPLITGGTVViVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLgHLERRPRALPA 446
Cdd:cd05972 121 PDDIHWNIADPGWAKGAWsSFFGPWLLGATVF-VYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI-KQDLSSYKFSH 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 LRCVSATGEALKAALVRRWFAVLPEVLLvNAYGLTETcddTNHEVLDRAQD---GSrvpLGRAIAGVGVHVVDGNLMPVP 523
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWRAATGLPIR-DGYGQTET---GLTVGNFPDMPvkpGS---MGRPTPGYDVAIIDDDGRELP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 524 LGATGEIVF--SGRCLARGYVNDPIRTALAFtasplfpGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIE 601
Cdd:cd05972 272 PGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 602 DRLLRLPGVREATVIvaGAAESAR---------LVACYSAAPSLAPgPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKV 672
Cdd:cd05972 345 SALLEHPAVAEAAVV--GSPDPVRgevvkafvvLTSGYEPSEELAE-ELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*
gi 502993051 673 DRKEL 677
Cdd:cd05972 422 RRVEL 426
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
181-679 |
5.98e-33 |
|
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: 134.89 E-value: 5.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 181 DRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGcyL 260
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 261 PV---EPHFPLErIAAMVTRS-ACGRALTDEVG----AAVTDRLGGLVPGLR----------ARGVDEILRGGHPSEVPG 322
Cdd:COG1021 102 PVfalPAHRRAE-ISHFAEQSeAVAYIIPDRHRgfdyRALARELQAEVPSLRhvlvvgdageFTSLDALLAAPADLSEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 323 TPvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQC--FDISLWQLLAPLITGGTVVIV 400
Cdd:COG1021 181 PD--PDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 401 SQQALLDVeqFAAeLDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRwfavLPEVL---LVNA 477
Cdd:COG1021 259 PDPSPDTA--FPL-IERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARR----VRPALgctLQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 478 YGLTE-----TCDDTNHEVLDRAQdgsrvplGRAI-AGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALA 551
Cdd:COG1021 332 FGMAEglvnyTRLDDPEEVILTTQ-------GRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 552 FTAsplfpgQRLYRSGDFGRWTPDGRLEFSGRRDTQVkIRGfrveiGE------IEDRLLRLPGVREATVIvagAAESAR 625
Cdd:COG1021 405 FTP------DGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVHDAAVV---AMPDEY 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 626 L----VACYSAA-PSLAPGPLVEAL-ARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:COG1021 470 LgersCAFVVPRgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
191-677 |
1.02e-32 |
|
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: 133.65 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 191 TAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLER 270
Cdd:cd05959 13 LNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 271 IAAMVTRSAC-----GRALTDEVGAAVTDRLGGLV--------PGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTS 337
Cdd:cd05959 93 YAYYLEDSRArvvvvSGELAPVLAAALTKSEHTLVvlivsggaGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 338 GSTGEPKGVMCEHEGM---LNHMLAKIddLGVRAGTVVAQTAPQCFDISLWQ-LLAPLITGGTVVIVSQQALLDVeqFAA 413
Cdd:cd05959 173 GSTGRPKGVVHLHADIywtAELYARNV--LGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMPERPTPAA--VFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 414 ELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALR-CVSAtGEALKAALVRRWFAvLPEVLLVNAYGLTETCddtnHEVL 492
Cdd:cd05959 249 RIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRlCVSA-GEALPAEVGERWKA-RFGLDILDGIGSTEML----HIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 493 DRAQDGSRV-PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGR 571
Cdd:cd05959 323 SNRPGRVRYgTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-------WTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 572 WTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAAESARL---VACY-----SAAPSLAPGPLVE 643
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVV--GVEDEDGLtkpKAFVvlrpgYEDSEALEEELKE 473
|
490 500 510
....*....|....*....|....*....|....
gi 502993051 644 ALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05959 474 FVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
182-677 |
4.26e-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: 131.86 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 182 RRVHQLIADTAAARPDDVAVV--AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCY 259
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 260 LPVEPHFPLERIAAMVTRsacgraltDEVGAAVTDRLGGLVPGLRARGVDEILRGGHPSE---------VPGTPVVAGQL 330
Cdd:cd05923 81 ALINPRLKAAELAELIER--------GEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLgepesagplIEDPPREPEQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR--AGTVVAQTAPQCFDISLWQLL-APLITGGTVVIVSQqalLD 407
Cdd:cd05923 153 AFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEE---FD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 408 VEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPeVLLVNAYGLTETcddT 487
Cdd:cd05923 230 PADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP-GEKVNIYGTTEA---M 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 488 NHEVLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVF--SGRCLARGYVNDPIRTALAFTasplfpgQRLYR 565
Cdd:cd05923 306 NSLYMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ-------DGWYR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 566 SGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPGPLVEA 644
Cdd:cd05923 379 TGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACVVPREGTLSADELDQ 458
|
490 500 510
....*....|....*....|....*....|....*
gi 502993051 645 LARV--LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05923 459 FCRAseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
198-677 |
5.09e-32 |
|
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: 130.27 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 198 DVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGcyLPVephfpleriaamvtr 277
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGA--IAV--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 278 sacgraltdevgaavtdrlgGLVPGLRARGVDEILRGGHPSEVPgtpVVAGQLAYIYFTSGSTGEPKGVMCEHEGML--- 354
Cdd:cd05919 64 --------------------VINPLLHPDDYAYIARDCEARLVV---TSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfa 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 355 NHMLAKIddLGVRAGTVVAQTAPQCFDISLWQ-LLAPLITGGTVVIVSqqALLDVEQFAAELDRSRVEVAQLVPSYVEVL 433
Cdd:cd05919 121 DAMAREA--LGLTPGDRVFSSAKMFFGYGLGNsLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 434 LGHLERRPRALPALRCVSATGEALKAALVRRWFAvlpevllvnaYGLTETCD-----DTNHEVLDRAQDGSRV-PLGRAI 507
Cdd:cd05919 197 LDSCAGSPDALRSLRLCVSAGEALPRGLGERWME----------HFGGPILDgigatEVGHIFLSNRPGAWRLgSTGRPV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 508 AGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSgdfgrwtPDGRLEFSGRRDTQ 587
Cdd:cd05919 267 PGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRD-------ADGWYTHAGRADDM 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 588 VKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAP-GPLVEALAR----VLPDYMVPRDWYWL 661
Cdd:cd05919 340 LKVGGQWVSPVEVESLIIQHPAVAEAAVVaVPESTGLSRLTAFVVLKSPAAPqESLARDIHRhlleRLSAHKVPRRIAFV 419
|
490
....*....|....*.
gi 502993051 662 DVLPLTGNGKVDRKEL 677
Cdd:cd05919 420 DELPRTATGKLQRFKL 435
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
187-680 |
1.62e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 130.82 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 187 LIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHF 266
Cdd:PRK07788 54 LVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 267 PLERIAAMVTRSACGRALTDEvgaAVTDRLGGL---VPGLRA---------------RGVDEILRGGHPSEVPGTPVVAG 328
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDD---EFTDLLSALppdLGRLRAwggnpdddepsgstdETLDDLIAGSSTAPLPKPPKPGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 329 QlayIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIvsqQALLDV 408
Cdd:PRK07788 211 I---VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVL---RRRFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 409 EQFAAELDRSRVEVAQLVPSYVEVLLGHLE--RRPRALPALRCVSATGEALKAALVRRWFAVLPEVlLVNAYGLTETCDD 486
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAFA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 487 TnhevLDRAQDGSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRtalaftasplfpgQR-- 562
Cdd:PRK07788 364 T----IATPEDLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDK-------------QIid 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 563 -LYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPGP 640
Cdd:PRK07788 427 gLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQRLRAFVVKAPGAALDE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502993051 641 ------LVEALARvlpdYMVPRDWYWLDVLPLTGNGKVDRKELARI 680
Cdd:PRK07788 507 daikdyVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
204-677 |
4.84e-31 |
|
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: 128.90 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 204 GLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIA----------- 272
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAyiinhaedrvv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 273 -------AMVTRSAcGRALTDEVGAAVTDRLGGLVPGL-RARGVDEILRGGHPSEvpGTPVVAGQLAY-IYFTSGSTGEP 343
Cdd:cd12119 102 fvdrdflPLLEAIA-PRLPTVEHVVVMTDDAAMPEPAGvGVLAYEELLAAESPEY--DWPDFDENTAAaICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 344 KGVMCEHEGMLNHMLAKI--DDLGVRAGTVVAQTAPQcFDISLWQL-LAPLITGGTVVIvsQQALLDVEQFAAELDRSRV 420
Cdd:cd12119 179 KGVVYSHRSLVLHAMAALltDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 421 EVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVllVNAYGLTETCD-------DTNHEVLD 493
Cdd:cd12119 256 TFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRV--IHAWGMTETSPlgtvarpPSEHSNLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 494 RAQDGS-RVPLGRAIAGVGVHVVD--GNLMPVPLGATGEIVFSGRCLARGYVNDPiRTALAFTASPLFpgqrlyRSGDFG 570
Cdd:cd12119 334 EDEQLAlRAKQGRPVPGVELRIVDddGRELPWDGKAVGELQVRGPWVTKSYYKND-EESEALTEDGWL------RTGDVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 571 RWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALAR 647
Cdd:cd12119 407 TIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIgVPHPKWGERPLAVVVLKEgaTVTAEELLEFLAD 486
|
490 500 510
....*....|....*....|....*....|
gi 502993051 648 VLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd12119 487 KVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
184-616 |
7.64e-31 |
|
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: 128.12 E-value: 7.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVVAGL--DQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLP 261
Cdd:cd05904 7 LDSVSFLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 262 VEPHFPLERIAAMVTRSACGRALTDevgAAVTDRLGGLVPGL--------RARGVDEILRGGHPSEVPGTPVVAGQLAYI 333
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAKLAFTT---AELAEKLASLALPVvlldsaefDSLSFSDLLFEADEAEPPVVVIKQDDVAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 334 YFTSGSTGEPKGVMCEHEGmLNHMLAKIDDLGVRAGT---VVAQTAPQCFDISL-WQLLAPLITGGTVVIVSQqalLDVE 409
Cdd:cd05904 164 LYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGSNSDsedVFLCVLPMFHIYGLsSFALGLLRLGATVVVMPR---FDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 410 QFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH 489
Cdd:cd05904 240 ELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 490 EVLDRAQDGSRVPLGRAIAGVGVHVVDGN-LMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTasplfpGQRLYRSGD 568
Cdd:cd05904 320 CFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 502993051 569 FGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI 616
Cdd:cd05904 394 LCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
180-683 |
7.73e-31 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 128.63 E-value: 7.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 180 PDRRVHQLIADTAAARPDDVAVVA------GLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVL 253
Cdd:PRK13295 22 HDRTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 254 KAGGCYLPVEPHFPLERIAAMVTRSACGRALTDEV-----GAAVTDRLGGLVPGLR---------ARGVDEILRGGHPSE 319
Cdd:PRK13295 102 RIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdHAAMARRLRPELPALRhvvvvggdgADSFEALLITPAWEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 320 VPGTPVV-------AGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDIS-LWQLLAPL 391
Cdd:PRK13295 182 EPDAPAIlarlrpgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 392 ITGGTVVIvsqQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLpE 471
Cdd:PRK13295 262 MLGATAVL---QDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-G 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 472 VLLVNAYGLTETCDDTNHEvLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALA 551
Cdd:PRK13295 338 AKIVSAWGMTENGAVTLTK-LDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 552 FtasplfpgQRLYRSGDFGRWTPDGRLEFSGrRDTQVKIRGFR-VEIGEIEDRLLRLPGVREATVIvagAAESARL--VA 628
Cdd:PRK13295 417 A--------DGWFDTGDLARIDADGYIRISG-RSKDVIIRGGEnIPVVEIEALLYRHPAIAQVAIV---AYPDERLgeRA 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993051 629 CYSAAPSLAPGPLVEALARVLPDYMVPRDwYW------LDVLPLTGNGKVDRKELARITGG 683
Cdd:PRK13295 485 CAFVVPRPGQSLDFEEMVEFLKAQKVAKQ-YIperlvvRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
188-672 |
1.11e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 128.15 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAAR-PDDVAVVAGLDQLTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPH 265
Cdd:PRK08314 15 NLEVSARRyPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRSA-----CGRALTDEVGAAVTD-RLGGLV--------------------------PGLRARGV---DE 310
Cdd:PRK08314 95 NREEELAHYVTDSGarvaiVGSELAPKVAPAVGNlRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVvawKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 311 ILRGGHPsevPGtPVVAG--QLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDISLWQ-- 386
Cdd:PRK08314 175 ALAAGLA---PP-PHTAGpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLP-LFHVTGMVhs 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 387 LLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWF 466
Cdd:PRK08314 250 MNAPIYAGATVVLMPR---WDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 467 AvLPEVLLVNAYGLTETCDDTNHEVLDRAQdgsRVPLGRAIAGVGVHVVD-GNLMPVPLGATGEIVFSGRCLARGYVNDP 545
Cdd:PRK08314 327 E-LTGLDYVEGYGLTETMAQTHSNPPDRPK---LQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 546 IRTALAFTAsplFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAA---E 622
Cdd:PRK08314 403 EATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPrrgE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993051 623 SAR-LVACYSAAPSLAPGPLVEALAR-VLPDYMVPRDWYWLDVLPLTGNGKV 672
Cdd:PRK08314 480 TVKaVVVLRPEARGKTTEEEIIAWAReHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
188-677 |
1.46e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 127.31 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFP 267
Cdd:PRK06145 8 IAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 LERIAAMVTRSACGRALTD-EVGAAVTDRLGGLVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGV 346
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVDeEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 347 MCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDISLWQL--LAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQ 424
Cdd:PRK06145 168 MHSYGNLHWKSIDHVIALGLTASERLLVVGP-LYHVGAFDLpgIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCD-DTNHEV---LDRAqdGSR 500
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSgDTLMEAgreIEKI--GST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 501 vplGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEF 580
Cdd:PRK06145 322 ---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-------WFRSGDVGYLDEEGFLYL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 581 SGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAA---ESARLVACYSAAPSLAPGPLVEALARVLPDYMVPRD 657
Cdd:PRK06145 392 TDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDrwgERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQ 471
|
490 500
....*....|....*....|
gi 502993051 658 WYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK06145 472 LKVRDELPRNPSGKVLKRVL 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
207-677 |
1.54e-30 |
|
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: 125.67 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSAcgrALTD 286
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSG---AKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 EVGAAVTDrlgglvpglrargvdeilrgghpsevpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGV 366
Cdd:cd05935 78 VVGSELDD-----------------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 367 RAGTVVAQTAPqCFDISLWQ--LLAPLITGGTVVIVsqqALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRAL 444
Cdd:cd05935 123 TPSDVILACLP-LFHVTGFVgsLNTAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRWFAvLPEVLLVNAYGLTETCDDTNhevLDRAQDGSRVPLGRAIAGVGVHVVD-GNLMPVP 523
Cdd:cd05935 199 SSLKVLTGGGAPMPPAVAEKLLK-LTGLRFVEGYGLTETMSQTH---TNPPLRPKLQCLGIP*FGVDARVIDiETGRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 524 LGATGEIVFSGRCLARGYVNDPIRTALAFTAsplFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDR 603
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993051 604 LLRLPGVREATVIVAGAAESARLVACY-----SAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05935 352 LYKHPAI*EVCVISVPDERVGEEVKAFivlrpEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
173-680 |
2.58e-30 |
|
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: 127.01 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 173 SGAPRELPDrrvhqLIADTAAARPDD----VAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVA 248
Cdd:cd05906 6 EGAPRTLLE-----LLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 249 VLGVLKAGG--CYLPVEPHFP--------LERIAAMVTRSAC--GRALTDEVGAAVTDRLgglVPGLRARGVDEILRggH 316
Cdd:cd05906 81 FWACVLAGFvpAPLTVPPTYDepnarlrkLRHIWQLLGSPVVltDAELVAEFAGLETLSG---LPGIRVLSIEELLD--T 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 317 PSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIddlgvragtVVAQTAPQcfDISL-W-QL------- 387
Cdd:cd05906 156 AADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKI---------QHNGLTPQ--DVFLnWvPLdhvgglv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 388 ---LAPLITGGTVVIVSQQALL-DVEQFAAELDRSRVEVAqLVPSYVEVLLG-HLERRPRA---LPALRCVSATGEALKA 459
Cdd:cd05906 225 elhLRAVYLGCQQVHVPTEEILaDPLRWLDLIDRYRVTIT-WAPNFAFALLNdLLEEIEDGtwdLSSLRYLVNAGEAVVA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 460 ALVRRWFAVL-----PEVLLVNAYGLTETC----DDTNHEVLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEI 530
Cdd:cd05906 304 KTIRRLLRLLepyglPPDAIRPAFGMTETCsgviYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 531 VFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGrWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGV 610
Cdd:cd05906 384 QVRGPVVTKGYYNNPEANAEAFTEDGWF------RTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 611 RE----ATVIVAGAAESARLVACY--SAAPSLAPGPLVEALARVL-------PDYMVPRDwywLDVLPLTGNGKVDRKEL 677
Cdd:cd05906 457 EPsftaAFAVRDPGAETEELAIFFvpEYDLQDALSETLRAIRSVVsrevgvsPAYLIPLP---KEEIPKTSLGKIQRSKL 533
|
...
gi 502993051 678 ARI 680
Cdd:cd05906 534 KAA 536
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
197-679 |
7.16e-30 |
|
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: 123.94 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 197 DDVAVVAGLDQLTYRQLDERANQVAHALLA-DGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLAlGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSAcgraltdevgaavtdrlgglvpglrargVDEILRGghpsevpgtpvvagqlAYIYFTSGSTGEPKGVMCEHEGMLN 355
Cdd:cd05941 81 TDSE----------------------------PSLVLDP----------------ALILYTSGTTGRPKGVVLTHANLAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 356 HMLAKIDDLGVRA--------------GTVVAqtapqcfdislwqLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVE 421
Cdd:cd05941 117 NVRALVDAWRWTEddvllhvlplhhvhGLVNA-------------LLCPLFAGASVEFLPK---FDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 422 VAQLVP-------SYVEVLLGHLERRPRALPA-LRCVSATGEALKAALVRRWFAVLPEVLLvNAYGLTETCDDTNHEVld 493
Cdd:cd05941 181 VFMGVPtiytrllQYYEAHFTDPQFARAAAAErLRLMVSGSAALPVPTLEEWEAITGHTLL-ERYGMTEIGMALSNPL-- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 494 raqDGSRVP--LGRAIAGVGVHVVD-GNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFG 570
Cdd:cd05941 258 ---DGERRPgtVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWF------KTGDLG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 571 RWTPDGRLEFSGR-RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACY---SAAPSLAPGPLVEAL 645
Cdd:cd05941 329 VVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgVPDPDWGERVVAVVvlrAGAAALSLEELKEWA 408
|
490 500 510
....*....|....*....|....*....|....
gi 502993051 646 ARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:cd05941 409 KQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
199-678 |
1.04e-29 |
|
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: 123.36 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 199 VAVVAGLDQLTYRQLDERANQVAHALLADGlaaedvVAVVSERAI------PWLVAV-LGVLKAGGcylpvephfplerI 271
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVLVGEL------GIVPGNRVLlrgsnsPELVACwFGIQKAGA-------------I 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 272 AAmvtrsacgraltdevgaavtdrlgGLVPGLRARGVDEILRGGHPSEVpgtpVVAGQL------AYIYFTSGSTGEPKG 345
Cdd:cd05958 63 AV------------------------ATMPLLRPKELAYILDKARITVA----LCAHALtasddiCILAFTSGTTGAPKA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEGMLNHM-LAKIDDLGVRAGTVVAQTAPQCFDISL-WQLLAPLITGGTVVIVSQQALLDVeqfAAELDRSRVEVA 423
Cdd:cd05958 115 TMHFHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEEATPDLL---LSAIARYKPTVL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 424 QLVPSYVEVLLGHLERRPRALPALR-CVSAtGEALKAALVRRWFAVLpEVLLVNAYGLTETCddtnHEVLDRAQDGSRV- 501
Cdd:cd05958 192 FTAPTAYRAMLAHPDAAGPDLSSLRkCVSA-GEALPAALHRAWKEAT-GIPIIDGIGSTEMF----HIFISARPGDARPg 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 502 PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTalaftaspLFPGQRLYrSGDFGRWTPDGRLEFS 581
Cdd:cd05958 266 ATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRT--------YVQGGWNI-TGDTYSRDPDGYFRHQ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 582 GRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAAESARLV---ACYSAAPSLAPGP-LVEAL----ARVLPDYM 653
Cdd:cd05958 337 GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVV--GHPDESRGVvvkAFVVLRPGVIPGPvLARELqdhaKAHIAPYK 414
|
490 500
....*....|....*....|....*
gi 502993051 654 VPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:cd05958 415 YPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
186-677 |
1.15e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 124.66 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADT---AAAR-PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLP 261
Cdd:PRK08316 11 QTIGDIlrrSARRyPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 262 VEPHFPLERIA---------------AMVTRSACGRALTDEVGAAVTDRLGGLVPGLRARGVDEILRGGhPSEVPGTPVV 326
Cdd:PRK08316 91 VNFMLTGEELAyildhsgaraflvdpALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAG-SVAEPDVELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 327 AGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLI-TGGTVVIVSQQal 405
Cdd:PRK08316 170 DDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLyVGATNVILDAP-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 406 lDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCd 485
Cdd:PRK08316 248 -DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIA- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 486 dTNHEVLdRAQDGSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrL 563
Cdd:PRK08316 326 -PLATVL-GPEEHLRRPgsAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG-------W 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 564 YRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvagAAESARLVACYSAAPSLAPGPLV- 642
Cdd:PRK08316 397 FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI---GLPDPKWIEAVTAVVVPKAGATVt 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502993051 643 --EALARV---LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK08316 474 edELIAHCrarLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
208-677 |
2.38e-29 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 122.61 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDE 287
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 VGAAVTDrlgglvpglrargvdeilrgghpsevPGTPvvagqlAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd05969 81 ELYERTD--------------------------PEDP------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTA-PQCFDISLWQLLAPLITGGTVVIVsqQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRA--L 444
Cdd:cd05969 129 PDDIYWCTAdPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRrWFAVLPEVLLVNAYGLTETCDD--TNHEVLDrAQDGSrvpLGRAIAGVGVHVVDGNLMPV 522
Cdd:cd05969 207 SSLRFIHSVGEPLNPEAIR-WGMEVFGVPIHDTWWQTETGSImiANYPCMP-IKPGS---MGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 523 PLGATGEIVFSGR--CLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEI 600
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 601 EDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPG-PLVEAL---ARV-LPDYMVPRDWYWLDVLPLTGNGKVDR 674
Cdd:cd05969 355 ESALMEHPAVAEAGVIgKPDPLRGEIIKAFISLKEGFEPSdELKEEIinfVRQkLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
...
gi 502993051 675 KEL 677
Cdd:cd05969 435 RVL 437
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
777-1010 |
3.18e-29 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 116.88 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 777 TPPGRRTLVCFPYAGGNAVTYVPLAGELAAeGWAVYGVEPPGRDG--NEAPV-SVPELAELVAGELAALDAGPLTLWGHS 853
Cdd:COG3208 2 RPDARLRLFCFPYAGGSASAYRPWAAALPP-DIEVLAVQLPGRGDrlGEPPLtSLEELADDLAEELAPLLDRPFALFGHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 854 TGVAAALATARLLRSRGHDVRRVLL--GAQLPGdsgaRRAQAAEVTALPDEAVVTALVE-SGRPELAEVGDAHRRLLADA 930
Cdd:COG3208 81 MGALLAFELARRLERRGRPLPAHLFvsGRRAPH----LPRRRRPLHDLSDAELLAELRRlGGTPEEVLADPELLELFLPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 931 YRHDVAAACGYLAealDAGDRLDVPVTVVLAADDvPDDLPGDPWDWSRLA-GDVRVVELPdGGHYFAASRPASVARVIAG 1009
Cdd:COG3208 157 LRADFRLLETYRY---TPGPPLDCPITALGGDDD-PLVSPEELAAWREHTtGPFRLRVFP-GGHFFLRDHPAELLALIRA 231
|
.
gi 502993051 1010 T 1010
Cdd:COG3208 232 A 232
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
329-679 |
6.55e-29 |
|
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: 118.59 E-value: 6.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 329 QLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDIS-LWQLLAPLITGGTVVIVSQQALLd 407
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGgLAILVRSLLAGAELVLLERNQAL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 408 veqfAAELDRSRVEVAQLVPSYVEVLLGHLERRPrALPALRCVSATGEALKAALVRRwfAVLPEVLLVNAYGLTETCDDT 487
Cdd:cd17630 79 ----AEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 488 NHEVLDRAQDGSrvpLGRAIAGVGVHVVDGnlmpvplgatGEIVFSGRCLARGYVNDPIRtalaftasPLFPGQRLYRSG 567
Cdd:cd17630 152 ATKRPDGFGRGG---VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV--------PEFNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 568 DFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPGPLVEALA 646
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDEELGQRPVAVIVGRGPADPAELRAWLK 290
|
330 340 350
....*....|....*....|....*....|...
gi 502993051 647 RVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:cd17630 291 DKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
333-674 |
7.65e-29 |
|
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: 118.90 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 333 IYFTSGSTGEPKGVMCEHEGM---LNHMLakIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLdvE 409
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFfavPDILQ--KEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY--K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 410 QFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRrWFAVLPEVLLVNAYGLTET----CD 485
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVR-FIEATGLTNTAQVYGLSETgtalCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 486 DTNHEVLDRAQDGSRVPlgraiaGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTasplfpGQRLYr 565
Cdd:cd17635 161 PTDDDSIEINAVGRPYP------GVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI------DGWVN- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 566 SGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSL----APGPL 641
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEldenAIRAL 307
|
330 340 350
....*....|....*....|....*....|...
gi 502993051 642 VEALARVLPDYMVPRDWYWLDVLPLTGNGKVDR 674
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
333-672 |
1.56e-28 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 117.60 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 333 IYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAP--QCFDISLwQLLAPLITGGTVVivsQQALLDVEQ 410
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPffHTFGYKA-GIVACLLTGATVV---PVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 411 FAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRcVSATGEA-LKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH 489
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLR-AAVTGAAtVPVELVRRMRSELGFETVLTAYGLTEAGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 490 EVLDRAQDGSRVpLGRAIAGVGVHVVDgnlmpvplgaTGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDF 569
Cdd:cd17638 160 RPGDDAETVATT-CGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWL------HTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 570 GRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAAESaRLVACYSAAPSLAPGPLVEALARV- 648
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVI--GVPDE-RMGEVGKAFVVARPGVTLTEEDVIa 299
|
330 340
....*....|....*....|....*....
gi 502993051 649 -----LPDYMVPRDWYWLDVLPLTGNGKV 672
Cdd:cd17638 300 wcrerLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
187-677 |
1.69e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 121.39 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 187 LIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHF 266
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 267 PLERIAAMVTRSACG----------------------RALTDEVGAAVTDRLGGLVPGlRARGVDEILRGGH-PSEVPGT 323
Cdd:PRK06164 95 RSHEVAHILGRGRARwlvvwpgfkgidfaailaavppDALPPLRAIAVVDDAADATPA-PAPGARVQLFALPdPAPPAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 324 PVVAGQ---LAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIv 400
Cdd:PRK06164 174 GERAADpdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVC- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 401 sqQALLDVEQFAAELDRSRVEVAqLVPSYVEVLLGHLERRPRALPALRCVSAtgealkAALVRRWFAVLPEVL-----LV 475
Cdd:PRK06164 253 --EPVFDAARTARALRRHRVTHT-FGNDEMLRRILDTAGERADFPSARLFGF------ASFAPALGELAALARargvpLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 476 NAYGLTE-----TCDDTNHEVLDRAQDGSRVPLGRAIAGVgVHVVDGNLMPVplGATGEIVFSGRCLARGYVNDPIRTAL 550
Cdd:PRK06164 324 GLYGSSEvqalvALQPATDPVSVRIEGGGRPASPEARVRA-RDPQDGALLPD--GESGEIEIRAPSLMRGYLDNPDATAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 551 AFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVA-- 628
Cdd:PRK06164 401 ALTDDGYF------RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAfv 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993051 629 CYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLT--GNG-KVDRKEL 677
Cdd:PRK06164 475 IPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
182-677 |
1.05e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 119.11 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 182 RRVH--QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCY 259
Cdd:PRK07786 15 RRQNwvNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 260 LPVEPHFPLERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLR------------ARGVDEILRGGHPSEVPgTPVVA 327
Cdd:PRK07786 95 VPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLStvvvaggssddsVLGYEDLLAEAGPAHAP-VDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 328 GQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDIS-LWQLLAPLITGGTVVIVSQQALl 406
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAgIGSMLPGLLLGAPTVIYPLGAF- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 407 DVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALpALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTE---- 482
Cdd:PRK07786 253 DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEmspv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 483 TCddtnheVLDrAQDGSRV--PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpg 560
Cdd:PRK07786 332 TC------MLL-GEDAIRKlgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGG----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 561 qrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAAES------ARLVACYSAAP 634
Cdd:PRK07786 400 --WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI--GRADEkwgevpVAVAAVRNDDA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502993051 635 SLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK07786 476 ALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
199-677 |
1.62e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 118.08 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 199 VAVVAGLDQ-LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTR 277
Cdd:PRK08276 2 AVIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 278 S------------ACGRALTDEVGAAVTDRL--GGLVPGLRARgvdEILRGGHPsEVPGTPVVAGQ-LAYiyfTSGSTGE 342
Cdd:PRK08276 82 SgakvlivsaalaDTAAELAAELPAGVPLLLvvAGPVPGFRSY---EEALAAQP-DTPIADETAGAdMLY---SSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 343 PKGVMCEHEG-----MLNHMLAKID-DLGVRAGTVVA------QTAPQCFDISLWQLlaplitGGTVVIVSQqalLDVEQ 410
Cdd:PRK08276 155 PKGIKRPLPGldpdeAPGMMLALLGfGMYGGPDSVYLspaplyHTAPLRFGMSALAL------GGTVVVMEK---FDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 411 FAAELDRSRVEVAQLVPS-YVEVLlgHLERRPRA---LPALRCVSATG----EALKAALVRRWFAVLPEVllvnaYGLTE 482
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTmFVRML--KLPEEVRArydVSSLRVAIHAAapcpVEVKRAMIDWWGPIIHEY-----YASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 483 TCDDTnheVLDrAQDGSRVP--LGRAIAGVgVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTasplfpG 560
Cdd:PRK08276 299 GGGVT---VIT-SEDWLAHPgsVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------P 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 561 QRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAE-SARLVACYSAAPSLAPG 639
Cdd:PRK08276 368 HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEmGERVKAVVQPADGADAG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502993051 640 P-----LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK08276 448 DalaaeLIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
207-616 |
5.97e-27 |
|
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: 115.39 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACgraltd 286
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 evgaavtdrlgglvpglrargvdEILRGGHPSEvpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGV 366
Cdd:cd05907 79 -----------------------KALFVEDPDD----------LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 367 RAGTVVAQTAPQC--FDISLWQlLAPLITGGTVVIVSqqallDVEQFAAELDRSRVEVAQLVPSYVE--------VLLGH 436
Cdd:cd05907 126 TEGDRHLSFLPLAhvFERRAGL-YVPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWEkvyaaikvKAVPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 437 LERRP---RALPALRCVSATGEALKAALVRRWFAV-LPevlLVNAYGLTETCDDTNHEVLDRAQDGSrvpLGRAIAGVGV 512
Cdd:cd05907 200 LKRKLfdlAVGGRLRFAASGGAPLPAELLHFFRALgIP---VYEGYGLTETSAVVTLNPPGDNRIGT---VGKPLPGVEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 513 HVVDgnlmpvplgaTGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGR-RDTQVKIR 591
Cdd:cd05907 274 RIAD----------DGEILVRGPNVMLGYYKNPEATAEALDADGWL------HTGDLGEIDEDGFLHITGRkKDLIITSG 337
|
410 420
....*....|....*....|....*
gi 502993051 592 GFRVEIGEIEDRLLRLPGVREATVI 616
Cdd:cd05907 338 GKNISPEPIENALKASPLISQAVVI 362
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
333-678 |
2.15e-26 |
|
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: 111.60 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 333 IYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAP--QCFDISLwQLLAPLITGGTVVIVSqqALLDVEQ 410
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPlfHCFGSVL-GVLACLTHGATMVFPS--PSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 411 FAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHE 490
Cdd:cd05917 84 VLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 491 VLDRAQDGSRVPLGRAIAGVGVHVVD--GNLMPvPLGATGEIVFSGRCLARGYVNDPIRTALAFTasplfpGQRLYRSGD 568
Cdd:cd05917 164 RTDDSIEKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEAID------GDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 569 FGRWTPDGRLEFSGR-RDtqVKIRGfrveiG------EIEDRLLRLPGVREATVIvagAAESARL--VACysAAPSLAPG 639
Cdd:cd05917 237 LAVMDEDGYCRIVGRiKD--MIIRG-----GeniyprEIEEFLHTHPKVSDVQVV---GVPDERYgeEVC--AWIRLKEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 502993051 640 P------LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:cd05917 305 AelteedIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
188-651 |
3.31e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 114.61 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAG----------LDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAG- 256
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPggrgadgklaYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 257 ---------------GCYLPVEPH----FPLERIAAMVTRSACG---RALTdeVGaavtdrlGGLVPGlrARGVDEILRG 314
Cdd:PRK09274 92 vpvlvdpgmgiknlkQCLAEAQPDafigIPKAHLARRLFGWGKPsvrRLVT--VG-------GRLLWG--GTTLATLLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 315 GHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHeGMLNHMLAKI-DDLGVRAGTVVAQTAPqcfdisLWQLLAPLIT 393
Cdd:PRK09274 161 GAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTH-GMFEAQIEALrEDYGIEPGEIDLPTFP------LFALFGPALG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 394 GGTVV---IVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLP 470
Cdd:PRK09274 234 MTSVIpdmDPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 471 E-VLLVNAYGLTET---CDDTNHEVLDRAQDGSR----VPLGRAIAGVGVHVVD---------GNLMPVPLGATGEIVFS 533
Cdd:PRK09274 314 PdAEILTPYGATEAlpiSSIESREILFATRAATDngagICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 534 GRCLARGYVNDPIRTALAFTASPLfpGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREA 613
Cdd:PRK09274 394 GPMVTRSYYNRPEATRLAKIPDGQ--GDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
|
490 500 510
....*....|....*....|....*....|....*...
gi 502993051 614 TVIVAGAAESARLVACYSAAPSLAPGPlvEALARVLPD 651
Cdd:PRK09274 472 ALVGVGVPGAQRPVLCVELEPGVACSK--SALYQELRA 507
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
190-592 |
7.50e-26 |
|
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: 113.49 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 190 DTAAARPDDVAVV------AGLDQLTYRQLDERANQVAHALLADGLAAeDVVAVVSERAIPWLVAVLGVLKAGGC----Y 259
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPG-DRVLLLAPPGLDFVAAFLGCLYAGAIavplP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 260 LPVEPHfPLERIAAMVTRSACGRALT-----DEVGAAVTDRLGGLVPGLRargVDEILRGGHPSEVPGTPVVAGQLAYIY 334
Cdd:cd05931 80 PPTPGR-HAERLAAILADAGPRVVLTtaaalAAVRAFAASRPAAGTPRLL---VVDLLPDTSAADWPPPSPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 335 FTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQ-LLAPLITGGTVVIVSQQALL-DVEQFA 412
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGgLLTPLYSGGPSVLMSPAAFLrRPLRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 413 AELDRSRVEVA-------QLVPSYVEVllghLERRPRALPALRCVSATGEALKAALVRRWFAV-----LPEVLLVNAYGL 480
Cdd:cd05931 236 RLISRYRATISaapnfayDLCVRRVRD----EDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfapfgFRPEAFRPSYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 481 TETC-----------------DDT---NHEVLDRAQDGSRVPL---GRAIAGVGVHVVDGN-LMPVPLGATGEIVFSGRC 536
Cdd:cd05931 312 AEATlfvsggppgtgpvvlrvDRDalaGRAVAVAADDPAARELvscGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPS 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 537 LARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTpDGRLEFSGRRDTQVKIRG 592
Cdd:cd05931 392 VASGYWGRPEATAETFGALAATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRG 446
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-678 |
7.91e-26 |
|
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: 112.17 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAaEDVVAVVSERAIPWLVAVLGVLKAGGCyLPVephfpleriaamvtrsacgraLTD 286
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIR-RGMRAVLMVPPGPDFFALTFALFKAGA-VPV---------------------LID 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 evgaavtdrlgglvPGLRARGVDEILRGGHPSEVPGTPVvAGQLAYIYFTSGSTGEPKGVMCEHeGMLNHMLAKI-DDLG 365
Cdd:cd05910 59 --------------PGMGRKNLKQCLQEAEPDAFIGIPK-ADEPAAILFTSGSTGTPKGVVYRH-GTFAAQIDALrQLYG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 366 VRAGTVVAQTAPqcfdisLWQLLAPLItGGTVVI----VSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRP 441
Cdd:cd05910 123 IRPGEVDLATFP------LFALFGPAL-GLTSVIpdmdPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 442 RALPALRCVSATGEALKAALVRRWFAVL-PEVLLVNAYGLTET---CDDTNHEVLDRAQD----GSRVPLGRAIAGVGVH 513
Cdd:cd05910 196 ITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvSSIGSRELLATTTAatsgGAGTCVGRPIPGVRVR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 514 VVD---------GNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAftASPLFPGQRLYRSGDFGRWTPDGRLEFSGRR 584
Cdd:cd05910 276 IIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALA--KIDDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 585 DTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLAP--GPLVEALARVLPDYmvPRDWYWLD 662
Cdd:cd05910 354 AHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITprARLEQELRALAKDY--PHTQRIGR 431
|
490 500
....*....|....*....|...
gi 502993051 663 VLPLTG-------NGKVDRKELA 678
Cdd:cd05910 432 FLIHPSfpvdirhNAKIFREKLA 454
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
166-677 |
1.03e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 112.93 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 166 RHQLTAFSGAPRELP--DRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAI 243
Cdd:PRK06155 3 PLGAGLAARAVDPLPpsERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 244 PWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSAcGRALTDEvgAAVTDRLGGLVPGLRARG----VDEILRGGHPSE 319
Cdd:PRK06155 83 EFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSG-ARLLVVE--AALLAALEAADPGDLPLPavwlLDAPASVSVPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 320 ------------VPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQL 387
Cdd:PRK06155 160 wstaplppldapAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 388 LAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCvsATGEALKAALVRRWFA 467
Cdd:PRK06155 240 FQALLAGATYVLEPR---FSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRV--ALGPGVPAALHAAFRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 468 VLpEVLLVNAYGLTEtcddTNHEVLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGR---CLARGYVND 544
Cdd:PRK06155 315 RF-GVDLLDGYGSTE----TNFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 545 PIRTALAFtasplfpgQRL-YRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAES 623
Cdd:PRK06155 390 PEKTVEAW--------RNLwFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELG 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 624 ARLVAcysAAPSLAPGPLVEALARV------LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK06155 462 EDEVM---AAVVLRDGTALEPVALVrhceprLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
187-677 |
1.71e-25 |
|
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: 111.62 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 187 LIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSeRAIPWLV-AVLGVLKAGGCYLPVEPH 265
Cdd:cd12118 9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLA-PNTPAMYeLHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 266 FPLERIAAMVTRSACGRALTDevgaavtdrlgglvpglRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKG 345
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVD-----------------REFEYEDLLAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEG-MLNhMLAKIDDLGVRAGTVVAQTAPQ------CFdisLWQLLApliTGGTVVI---VSQQALLD------VE 409
Cdd:cd12118 151 VVYHHRGaYLN-ALANILEWEMKQHPVYLWTLPMfhcngwCF---PWTVAA---VGGTNVClrkVDAKAIYDliekhkVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 410 QFAAeldrsrvevaqlVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVrrwFAVLPEVLLVN-AYGLTET----- 483
Cdd:cd12118 224 HFCG------------APTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVL---AKMEELGFDVThVYGLTETygpat 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 484 -C---DDTNHEVLD-----RAQDGSRVplgraIAGVGVHVVDGNLM-PVPL-GAT-GEIVFSGRCLARGYVNDPIRTALA 551
Cdd:cd12118 289 vCawkPEWDELPTEerarlKARQGVRY-----VGLEEVDVLDPETMkPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 552 FTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATViVAGAAESARLVACys 631
Cdd:cd12118 364 FRGG-------WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV-VARPDEKWGEVPC-- 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993051 632 AAPSLAPG------PLVEALARVLPDYMVPRDWYWLDvLPLTGNGKVDRKEL 677
Cdd:cd12118 434 AFVELKEGakvteeEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
182-677 |
3.53e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 110.90 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 182 RRVHQL---IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGC 258
Cdd:PRK07470 4 RRVMNLahfLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 259 YLPVEPHFPLERIAAMVTRSA-----CGRALTDEVGA--AVTDRLGGLVPGLRARG---VDEILRGGHPSEVPGTPVVAG 328
Cdd:PRK07470 84 WVPTNFRQTPDEVAYLAEASGaramiCHADFPEHAAAvrAASPDLTHVVAIGGARAgldYEALVARHLGARVANAAVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 329 QLAYIYFTSGSTGEPKGVMCEHEGM----LNHMLAKIDDLGVRAGTVVaqTAPQCFDISLWQLLAPLITGGTVVIVSQQa 404
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQMafviTNHLADLMPGTTEQDASLV--VAPLSHGAGIHQLCQVARGAATVLLPSER- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 405 lLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVlLVNAYGLTETC 484
Cdd:PRK07470 241 -FDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 485 DdtNHEVL----DRAQDGSRV---PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASpl 557
Cdd:PRK07470 319 G--NITVLppalHDAEDGPDArigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 558 fpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGAAESARLVAcySA 632
Cdd:PRK07470 395 -----WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLgvpdpVWGEVGVAVCVA--RD 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502993051 633 APSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK07470 468 GAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
191-679 |
5.87e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 110.62 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 191 TAAAR-PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLE 269
Cdd:PRK13382 51 IAAQRcPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 270 RIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGlRARGVD----------EILRGGHPSEVPGTPVVAGQLayIYFTSGS 339
Cdd:PRK13382 131 ALAEVVTREGVDTVIYDEEFSATVDRALADCPQ-ATRIVAwtdedhdltvEVLIAAHAGQRPEPTGRKGRV--ILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 340 TGEPKGVmcEHEGMLNHMLAK--IDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIvsqQALLDVEQFAAELDR 417
Cdd:PRK13382 208 TGTPKGA--RRSGPGGIGTLKaiLDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVT---RRRFDPEATLDLIDR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 418 SRVEVAQLVPSYVEVLLGHLE--RRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLvNAYGLTET--CDDTNHEVLD 493
Cdd:PRK13382 283 HRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIY-NNYNATEAgmIATATPADLR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 494 RAQDGSrvplGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDpirTALAFTASplfpgqrLYRSGDFGRWT 573
Cdd:PRK13382 362 AAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHDG-------FMASGDVGYLD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 574 PDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALARVLP 650
Cdd:PRK13382 428 ENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDEQYGQRLAAFVVLKPgaSATPETLKQHVRDNLA 507
|
490 500
....*....|....*....|....*....
gi 502993051 651 DYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:PRK13382 508 NYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
186-687 |
1.06e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 109.69 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVS-ERAIPWLVAVLGVLkAGGCYLPVEP 264
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSlNRPEVLMAIGAAQL-AGLRRTALHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 HFPLERiAAMVTRSACGRALTDEvGAAVTDRLGGL---VPGLRA--------RGVD---EILRGGHPSEVPGTpvVAGQL 330
Cdd:PRK06188 95 LGSLDD-HAYVLEDAGISTLIVD-PAPFVERALALlarVPSLKHvltlgpvpDGVDllaAAAKFGPAPLVAAA--LPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqcfdIS--LWQLLAP-LITGGTVVIVSQqalLD 407
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTP----LShaGGAFFLPtLLRGGTVIVLAK---FD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 408 VEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLlVNAYGLTE----- 482
Cdd:PRK06188 244 PAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIF-AQYYGQTEapmvi 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 483 -TCDDTNHevlDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLfpgq 561
Cdd:PRK06188 323 tYLRKRDH---DPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWL---- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 562 rlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVA-----GAAESARLVACYSAAPSl 636
Cdd:PRK06188 396 ---HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpdekwGEAVTAVVVLRPGAAVD- 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993051 637 aPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL-ARITGGLHRA 687
Cdd:PRK06188 472 -AAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALrARYWEGRGRA 522
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
192-677 |
3.39e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 107.85 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVV-AGLDQ-LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLE 269
Cdd:PRK13391 7 AQTTPDKPAVImASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 270 RIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLRAR----GVDEILRGGHPSEV----PGTPV---VAGQLayIYFTSG 338
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRlvldGDGELEGFVGYAEAvaglPATPIadeSLGTD--MLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 339 STGEPKGVMCE-------HEGMLNHMLAKIddLGVRAGTV------VAQTAPQCFDISLWQLlaplitGGTVVIVSQqal 405
Cdd:PRK13391 165 TTGRPKGIKRPlpeqppdTPLPLTAFLQRL--WGFRSDMVylspapLYHSAPQRAVMLVIRL------GGTVIVMEH--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 406 LDVEQFAAELDRSRVEVAQLVPS-YVEVLLGHLERRPR-ALPALRcVSATGEA-----LKAALVRRWFAVLPEVllvnaY 478
Cdd:PRK13391 234 FDAEQYLALIEEYGVTHTQLVPTmFSRMLKLPEEVRDKyDLSSLE-VAIHAAApcppqVKEQMIDWWGPIIHEY-----Y 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 479 GLTE---TCDDTNHEVLDRaqdgsRVPLGRAIAGVgVHVVDGNLMPVPLGATGEIVFSGRcLARGYVNDPIRTALAFTAS 555
Cdd:PRK13391 308 AATEglgFTACDSEEWLAH-----PGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGG-RPFEYLNDPAKTAEARHPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 556 PlfpgqRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLV-ACYSAAP 634
Cdd:PRK13391 381 G-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVkAVVQPVD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502993051 635 SLAPGP-----LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK13391 456 GVDPGPalaaeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
191-679 |
2.06e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 105.34 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 191 TAAARPDDVAV-VAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLE 269
Cdd:PRK07514 11 AAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 270 RI---------AAMVTRSACGRALtdevgAAVTDRLG-GLVPGLRARGVDEILRG--GHPSEVPGTPVVAGQLAYIYFTS 337
Cdd:PRK07514 91 ELdyfigdaepALVVCDPANFAWL-----SKIAAAAGaPHVETLDADGTGSLLEAaaAAPDDFETVPRGADDLAAILYTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 338 GSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAP-----QCFDISLWQLLAplitGGTVVIVSQqalLDVEQFA 412
Cdd:PRK07514 166 GTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPifhthGLFVATNVALLA----GASMIFLPK---FDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 413 AELDRSRVEVAqlVPSYVEVLLGHLERRPRALPALR-CVSatGEA-LKAALVRRWFAVLPEVLLvNAYGLTETCDDTNHE 490
Cdd:PRK07514 239 ALMPRATVMMG--VPTFYTRLLQEPRLTREAAAHMRlFIS--GSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSNP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 491 VldraqDGSRVP--LGRAIAGVGVHVVD-GNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSG 567
Cdd:PRK07514 314 Y-----DGERRAgtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFF------ITG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 568 DFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVA-----GAAESARLVAcySAAPSLAPGPLV 642
Cdd:PRK07514 383 DLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVphpdfGEGVTAVVVP--KPGAALDEAAIL 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 502993051 643 EALARVLPDYMVPRDWYWLDVLPLTGNGKVdRKELAR 679
Cdd:PRK07514 461 AALKGRLARFKQPKRVFFVDELPRNTMGKV-QKNLLR 496
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
168-674 |
7.77e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 104.08 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 168 QLTAFSGAPRE-LPDRRVHQLIADTAAARPDDVAVVAGLDQL--TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIP 244
Cdd:PRK12583 3 QPSYYQGGGDKpLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 245 WLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACgRALTDEVGAAVTDR---LGGLVPGLRARGVDEI-------LRG 314
Cdd:PRK12583 83 WLLTQFATARIGAILVNINPAYRASELEYALGQSGV-RWVICADAFKTSDYhamLQELLPGLAEGQPGALacerlpeLRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 315 G---HPSEVPGTPVVAGQLAY-----------------------IYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRA 368
Cdd:PRK12583 162 VvslAPAPPPGFLAWHELQARgetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 369 GTVVAQTAP--QCFDISLWQLLAplITGGTVVIVSQQAL--LDVEQFAAEldrSRVEVAQLVPSYVEVLLGHLERRPRAL 444
Cdd:PRK12583 242 HDRLCVPVPlyHCFGMVLANLGC--MTVGACLVYPNEAFdpLATLQAVEE---ERCTALYGVPTMFIAELDHPQRGNFDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRWFAVL--PEVLLvnAYGLTETCDDTNhevldraQDGSRVPLGRAIAGVG-------VHVV 515
Cdd:PRK12583 317 SSLRTGIMAGAPCPIEVMRRVMDEMhmAEVQI--AYGMTETSPVSL-------QTTAADDLERRVETVGrtqphleVKVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 516 DGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRV 595
Cdd:PRK12583 388 DPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWM------HTGDLATMDEQGYVRIVGRSKDMIIRGGENI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 596 EIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKV 672
Cdd:PRK12583 462 YPREIEEFLFTHPAVADVQVFgVPDEKYGEEIVAWVRLHPghAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
..
gi 502993051 673 DR 674
Cdd:PRK12583 542 QK 543
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
188-681 |
7.80e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 103.40 E-value: 7.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPV---- 262
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLnirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 263 ---EPHFPLERIAamvTRSACGRALTDEVGAAVTDRLgGLVPGLRARGVDEILRGGHPSEVPGTpvvaGQLAYIY-FTSG 338
Cdd:PRK06839 88 tenELIFQLKDSG---TTVLFVEKTFQNMALSMQKVS-YVQRVISITSLKEIEDRKIDNFVEKN----ESASFIIcYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 339 STGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDISLWQLLA-PLITGGTVVIVSQQalLDVEQFAAELDR 417
Cdd:PRK06839 160 TTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLP-LFHIGGIGLFAfPTLFAGGVIIVPRK--FEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 418 SRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWfaVLPEVLLVNAYGLTETCDDTnheVLDRAQD 497
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREF--IDRGFLFGQGFGMTETSPTV---FMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 498 GSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyrSGDFGRWTPD 575
Cdd:PRK06839 312 ARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 576 GRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVA-----GAAESARLVACYSAapSLAPGPLVEALARVLP 650
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRqhvkwGEIPIAFIVKKSSS--VLIEKDVIEHCRLFLA 462
|
490 500 510
....*....|....*....|....*....|.
gi 502993051 651 DYMVPRDWYWLDVLPLTGNGKVDRKELARIT 681
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
183-683 |
1.42e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 103.04 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 183 RVHQLIADTAAARPDDVAVVAGLDQ--LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYL 260
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 261 PVEPHFPlerIAAMVTRSACGRA---LTDEVGaaVTDRLGGLV---PGLRARGVDEILRGGHPS-----EVPGTPVVAGQ 329
Cdd:PRK05852 97 PLDPALP---IAEQRVRSQAAGArvvLIDADG--PHDRAEPTTrwwPLTVNVGGDSGPSGGTLSvhldaATEPTPATSTP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 330 L------AYIYFTSGSTGEPKGVMCEHEGMLNHMLAKID--DLGVRAGTVVAQTAPQCFDIsLWQLLAPLITGGTVVIVS 401
Cdd:PRK05852 172 EglrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITgyRLSPRDATVAVMPLYHGHGL-IAALLATLASGGAVLLPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 402 QqALLDVEQFAAELDRSRVEVAQLVPSYVEVLL--GHLERRPRALPALRCV---SATGEALKAALVRRWFAVLpevlLVN 476
Cdd:PRK05852 251 R-GRFSAHTFWDDIKAVGATWYTAVPTIHQILLerAATEPSGRKPAALRFIrscSAPLTAETAQALQTEFAAP----VVC 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 477 AYGLTETcddtNHEVLDRAQDG---------SRVPLGRAiAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIR 547
Cdd:PRK05852 326 AFGMTEA----THQVTTTQIEGigqtenpvvSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 548 TALAFTASPLfpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGAAE 622
Cdd:PRK05852 401 TAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFgvpdqLYGEAV 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993051 623 SARLVACYSAAPSlaPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARITGG 683
Cdd:PRK05852 474 AAVIVPRESAPPT--AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGH 532
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
332-674 |
1.69e-22 |
|
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: 99.79 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 332 YIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQqalLDVEQF 411
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK---FNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 412 AAELDRSRVEVAQLVPSYVEVLLGHLErrprALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETcddtnHEV 491
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLE----PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL-----SFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 492 LDRAQDGSRVPL--GRAIAGVGVHVVDGNLmpvplGATGEI------VFSGRCLARGYVNDpirtalaftasplfpgqRL 563
Cdd:cd17633 152 TYNFNQESRPPNsvGRPFPNVEIEIRNADG-----GEIGKIfvksemVFSGYVRGGFSNPD-----------------GW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 564 YRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSaAPSLAPGPLV 642
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgIPDARFGEIAVALYS-GDKLTYKQLK 288
|
330 340 350
....*....|....*....|....*....|..
gi 502993051 643 EALARVLPDYMVPRDWYWLDVLPLTGNGKVDR 674
Cdd:cd17633 289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
209-672 |
1.69e-22 |
|
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: 103.04 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAA---------MVT--- 276
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGriidsssrlLITadg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 277 -----RSACGRALTDEVGAA---------VTDRLGGLVPGLRARGV--DEILRGGHPSEVPgTPVVAGQLAYIYFTSGST 340
Cdd:cd17634 166 gvragRSVPLKKNVDDALNPnvtsvehviVLKRTGSDIDWQEGRDLwwRDLIAKASPEHQP-EAMNAEDPLFILYTSGTT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 341 GEPKGVMCEHEGMLNHM---LAKIDDLGvrAGTVVAQTApqcfDISL-----WQLLAPLITGGTVVIVSQQALL-DVEQF 411
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAattMKYVFDYG--PGDIYWCTA----DVGWvtghsYLLYGPLACGATTLLYEGVPNWpTPARM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 412 AAELDRSRVEVAQLVPSYVEVLLGH----LERRPRAlpALRCVSATGEALKAAlVRRWFAvlpEVL------LVNAYGLT 481
Cdd:cd17634 319 WQVVDKHGVNILYTAPTAIRALMAAgddaIEGTDRS--SLRILGSVGEPINPE-AYEWYW---KKIgkekcpVVDTWWQT 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 482 ETCDD--TNHEVLDRAQDGSRVplgRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRC--LARGYVNDPIRTALAFTASpl 557
Cdd:cd17634 393 ETGGFmiTPLPGAIELKAGSAT---RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWpgQTRTLFGDHERFEQTYFST-- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 558 FPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSL 636
Cdd:cd17634 468 FKG--MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgIPHAIKGQAPYAYVVLNHGV 545
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502993051 637 APGP-----LVEALARVLPDYMVPRDWYWLDVLPLTGNGKV 672
Cdd:cd17634 546 EPSPelyaeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
192-677 |
2.33e-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: 102.19 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLDQ-----LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLP----V 262
Cdd:cd05970 27 AKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 263 EPHFPLERIAA----MVTRSAcGRALTDEVGAAVTD--------RLGGLVPglraRG---VDEILRGGHPS-EVPGTPVV 326
Cdd:cd05970 107 TAKDIVYRIESadikMIVAIA-EDNIPEEIEKAAPEcpskpklvWVGDPVP----EGwidFRKLIKNASPDfERPTANSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 327 AG--QLAYIYFTSGSTGEPKgvMCEHEGM--LNHMLAKIDDLGVRAGTVVAQTAPQCFDISLW-QLLAPLITGGTVVIvs 401
Cdd:cd05970 182 PCgeDILLVYFSSGTTGMPK--MVEHDFTypLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFV-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 402 qqalLDVEQFAAE--LDR-SRVEVAQL-VPSYVEVLLGHLERRPRALPALR-CVSAtGEALKAALVRRWFAvLPEVLLVN 476
Cdd:cd05970 258 ----YDYDKFDPKalLEKlSKYGVTTFcAPPTIYRFLIREDLSRYDLSSLRyCTTA-GEALNPEVFNTFKE-KTGIKLME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 477 AYGLTETCDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVF---SGRCLA--RGYVNDPIRTALA 551
Cdd:cd05970 332 GFGQTETTLTIATFPWMEPKPGS---MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEKTAEV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 552 FtasplFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGAAESARL 626
Cdd:cd05970 409 W-----HDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTgvpdpIRGQVVKATI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502993051 627 V--ACYSAAPSLAPgPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05970 482 VlaKGYEPSEELKK-ELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
332-673 |
3.26e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 99.76 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 332 YIYFTSGSTGEPKGVMCEHE-------GMLNHM---LAKIDDLGVRA----GTVVAQTAPQCFDISLWQLLAPLITGGTV 397
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdifrmlmGGADFGtgeFTPSEDAHKAAaaaaGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 398 VIVSQQalLDVEQFAAELDRSRVEVAQLV-PSYVEVLLGHLER-RPRALPALRCVSATGEALKAALVRRWFAVLPEVLLV 475
Cdd:cd05924 87 VLPDDR--FDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDaGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 476 NAYGLTETCDDTNHEVldRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRcLARGYVNDPIRTALAFtas 555
Cdd:cd05924 165 DAFGSSETGFTGSGHS--AGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGH-IPLGYYGDEAKTAETF--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 556 PLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREatVIVAGAAES---ARLVACYSA 632
Cdd:cd05924 239 PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYD--VLVVGRPDErwgQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502993051 633 APSLAP--GPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:cd05924 317 REGAGVdlEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
185-678 |
5.04e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 101.23 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 185 HQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEP 264
Cdd:PRK13383 38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 HFPLERIAAMVTRSACGRALTDEvgaAVTDRLGGlvPGLRARGVDEILRGGHpsEVPGTPVVAGQLAYIYFTSGSTGEPK 344
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADN---EFAERIAG--ADDAVAVIDPATAGAE--ESGGRPAVAAPGRIVLLTSGTTGKPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 345 GV--MCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEV 422
Cdd:PRK13383 191 GVprAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRH---FDAEAALAQASLHRADA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 423 AQLVPSYVEVLLgHLERRPRA---LPALRCVSATGEALKAALVRRWFAVLPEVLLvNAYGLTET---CDDTNHEVLDRAQ 496
Cdd:PRK13383 268 FTAVPVVLARIL-ELPPRVRArnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILY-NGYGSTEVgigALATPADLRDAPE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 497 DgsrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrlyrSGDFGRWTPDG 576
Cdd:PRK13383 346 T-----VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAVVDGMTS----------TGDMGYLDNAG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 577 RLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALARVLPDYM 653
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIgVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKDRVSRFE 490
|
490 500
....*....|....*....|....*
gi 502993051 654 VPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
207-616 |
6.11e-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: 100.51 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGgcylpvephfpleriAAMVTRSAcgRALTD 286
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG---------------AVDVVRGS--DSSVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 EVGAAVTDrlgglvpglrARGVDEILRGgHPSEvpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGMLNHM--LAKIDDL 364
Cdd:cd17640 68 ELLYILNH----------SESVALVVEN-DSDD----------LATIIYTSGTTGNPKGVMLTHANLLHQIrsLSDIVPP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 365 GVraGTVVAQTAPqcfdisLW---QLLAP--LITGGTVvivsqQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLER 439
Cdd:cd17640 127 QP--GDRFLSILP------IWhsyERSAEyfIFACGCS-----QAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 440 RPRALPALRCVSA----TGEALKAAL---------VRRWFAVLpEVLLVNAYGLTETCDDTNHEVLDRAQDGSrvpLGRA 506
Cdd:cd17640 194 QVSKSSPIKQFLFlfflSGGIFKFGIsgggalpphVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNVRGS---VGRP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 507 IAGVGVHVVD--GNlMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGR- 583
Cdd:cd17640 270 LPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWF------NTGDLGWLTCGGELVLTGRa 342
|
410 420 430
....*....|....*....|....*....|...
gi 502993051 584 RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI 616
Cdd:cd17640 343 KDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
189-679 |
6.25e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 100.45 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 189 ADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHalladGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHF-P 267
Cdd:PRK07787 7 AAVAAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSgV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 LERiaamvtrsacGRALTDEVGAAVTDRLGGLVPGLRARGVDEILRGGHPSEVPGtpvvAGQLAYIYFTSGSTGEPKGVM 347
Cdd:PRK07787 82 AER----------RHILADSGAQAWLGPAPDDPAGLPHVPVRLHARSWHRYPEPD----PDAPALIVYTSGTTGPPKGVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 348 CEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDIS--LWQLLAPLITGGTVVIVSQQAlldVEQFAAELDRSrvevAQL 425
Cdd:PRK07787 148 LSRRAIAADLDALAEAWQWTADDVLVHGLP-LFHVHglVLGVLGPLRIGNRFVHTGRPT---PEAYAQALSEG----GTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 426 ---VPSYVEVLLGHLERrPRALPALRCVSATGEALKAALVRRwFAVLPEVLLVNAYGLTETCDDTNhevlDRAqDGSRVP 502
Cdd:PRK07787 220 yfgVPTVWSRIAADPEA-ARALRGARLLVSGSAALPVPVFDR-LAALTGHRPVERYGMTETLITLS----TRA-DGERRP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 503 --LGRAIAGVGVHVVDGNLMPVPLG--ATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRL 578
Cdd:PRK07787 293 gwVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGWF------RTGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 579 EFSGRRDTQ-VKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMVPR 656
Cdd:PRK07787 367 RIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVgVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPR 446
|
490 500
....*....|....*....|...
gi 502993051 657 DWYWLDVLPLTGNGKVDRKELAR 679
Cdd:PRK07787 447 EVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
291-680 |
6.28e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 101.05 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 291 AVTDRLGGLVPGLR---ARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHML---AKIDDL 364
Cdd:PRK12492 167 TVVDKVKKMVPAYHlpqAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLqvrACLSQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 365 GVRAGTVVAQ-----TAPqcfdISLWQLLA-------PLITGGTVVIVSQQAllDVEQFAAELDRSRVEVAQLVPSYVEV 432
Cdd:PRK12492 247 GPDGQPLMKEgqevmIAP----LPLYHIYAftancmcMMVSGNHNVLITNPR--DIPGFIKELGKWRFSALLGLNTLFVA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 433 LLGHLERRPRALPALRCVSATGEALKAALVRRWfAVLPEVLLVNAYGLTETcddtnHEVLDRAQDGSRVPLGRA---IAG 509
Cdd:PRK12492 321 LMDHPGFKDLDFSALKLTNSGGTALVKATAERW-EQLTGCTIVEGYGLTET-----SPVASTNPYGELARLGTVgipVPG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 510 VGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVK 589
Cdd:PRK12492 395 TALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWF------KTGDIAVIDPDGFVRIVDRKKDLII 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 590 IRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPslAPGPLVEALARV----LPDYMVPRDWYWLDVLP 665
Cdd:PRK12492 469 VSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR--DPGLSVEELKAYckenFTGYKVPKHIVLRDSLP 546
|
410
....*....|....*
gi 502993051 666 LTGNGKVDRKELARI 680
Cdd:PRK12492 547 MTPVGKILRRELRDI 561
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
329-678 |
7.74e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 102.31 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 329 QLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAP--QCFDISLWQLLaPLITGGTVVIVSQQalL 406
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPffHSFGLTVTLWL-PLLEGIKVVYHPDP--T 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 407 DVEQFAAELDRSRVEVAQLVPSYvevlLGHLERRPRALPA----LRCVSATGEALKAAlVRRWFAVLPEVLLVNAYGLTE 482
Cdd:PRK08633 860 DALGIAKLVAKHRATILLGTPTF----LRLYLRNKKLHPLmfasLRLVVAGAEKLKPE-VADAFEEKFGIRILEGYGATE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 483 T-------CDDTNhEVLDRAQDGSRV-PLGRAIAGVGVHVVD-GNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFT 553
Cdd:PRK08633 935 TspvasvnLPDVL-AADFKRQTGSKEgSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIK 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 554 aspLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAG---AAESARLVACY 630
Cdd:PRK08633 1014 ---DIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAvpdEKKGEKLVVLH 1090
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502993051 631 SaAPSLAPGPLVEALARV-LPDYMVPRDWYWLDVLPLTGNGKVD---RKELA 678
Cdd:PRK08633 1091 T-CGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDlkgLKELA 1141
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
331-677 |
2.51e-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: 97.80 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDIS-LWQLLAPLITGGTVVIVSQqalLDVE 409
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALP-LFHISgLSILMRSVIYGMTVYLVDK---FDAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 410 QFAAELDRSRVEVAQLVPSYVEVLlghLERRPRALPA-LRCVSATGEALKAALVRRwfAVLPEVLLVNAYGLTETCDD-- 486
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRL---LEILGEGYPNnLRCILLGGGPAPKPLLEQ--CKEKGIPVYQSYGMTETCSQiv 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 487 --TNHEVLDRAqdGSrvpLGRAIAGVGVHVVDGNlmpVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLY 564
Cdd:cd05912 231 tlSPEDALNKI--GS---AGKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENG-------WF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 565 RSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAE-SARLVACYSAAPSLAPGPLVE 643
Cdd:cd05912 296 KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVVSERPISEEELIA 375
|
330 340 350
....*....|....*....|....*....|....
gi 502993051 644 ALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05912 376 YCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
324-677 |
2.52e-21 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 98.56 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 324 PVVAGQLAYIYFTSGSTGEPKGVMCEHEGML-------NHMLAKIDDlgvragtVVAQTAP--QCF--DISLWqllAPLI 392
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanveqitAIFDPNPED-------VVFGALPffHSFglTGCLW---LPLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 393 TGGTVVIVSQQalLDVEQFAAELDRSRVEVAQLVPsyveVLLGHLERR--PRALPALRCVSATGEALKAALvRRWFAVLP 470
Cdd:cd05909 213 SGIKVVFHPNP--LDYKKIPELIYDKKATILLGTP----TFLRGYARAahPEDFSSLRLVVAGAEKLKDTL-RQEFQEKF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 471 EVLLVNAYGLTETCD--DTNHEVLDRaQDGSrvpLGRAIAGVGVHVVD-GNLMPVPLGATGEIVFSGRCLARGYVNDPIR 547
Cdd:cd05909 286 GIRILEGYGTTECSPviSVNTPQSPN-KEGT---VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 548 TALAFtasplfpGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLL-RLPG-VREATVIVAGAAESAR 625
Cdd:cd05909 362 TSFAF-------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeILPEdNEVAVVSVPDGRKGEK 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502993051 626 LVACYSaAPSLAPGPLVEALARV-LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05909 435 IVLLTT-TTDTDPSSLNDILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
208-677 |
2.54e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 99.18 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHF-PLERIAAMVTRSACGRALT 285
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYtPRELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 DEVGAAVTDRLGG--------------------------------LVPGLRARGV---DEILRGGHPSEVPGTPVVAGQL 330
Cdd:PRK08751 131 DNFGTTVQQVIADtpvkqvittglgdmlgfpkaalvnfvvkyvkkLVPEYRINGAirfREALALGRKHSMPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGV----RAGTVVAQTAPQCFDIslWQLLAP----LITGGTVVIVSQ 402
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGtgklEEGCEVVITALPLYHI--FALTANglvfMKIGGCNHLISN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 403 QAllDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVlPEVLLVNAYGLTE 482
Cdd:PRK08751 289 PR--DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQV-TGLTLVEAYGLTE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 483 TCDDTNHEVLD-RAQDGSrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgq 561
Cdd:PRK08751 366 TSPAACINPLTlKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWL--- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 562 rlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLV--ACYSAAPSLApG 639
Cdd:PRK08751 440 ---HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVkvVIVKKDPALT-A 515
|
490 500 510
....*....|....*....|....*....|....*....
gi 502993051 640 PLVEALARV-LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK08751 516 EDVKAHARAnLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
208-679 |
3.60e-21 |
|
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: 97.59 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDe 287
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 vgAAVTDRLgglvpglrargvdeilrgghpsevpgtpvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd05973 80 --AANRHKL------------------------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTAPQCFDISLW-QLLAPLITGGTVVIVsqQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPA 446
Cdd:cd05973 128 PEDSFWNAADPGWAYGLYyAITGPLALGHPTILL--EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 -LRCVSATGEALKAALVRrWFAVLPEVLLVNAYGLTET-CDDTNHEVLDR-AQDGSrvpLGRAIAGVGVHVVDGNLMPVP 523
Cdd:cd05973 206 rLRRVSSAGEPLTPEVIR-WFDAALGVPIHDHYGQTELgMVLANHHALEHpVHAGS---AGRAMPGWRVAVLDDDGDELG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 524 LGATGeivfsgrclargyvndpiRTALAFTASPL--FPGQ----------RLYRSGDFGRWTPDGRLEFSGRRDTQVKIR 591
Cdd:cd05973 282 PGEPG------------------RLAIDIANSPLmwFRGYqlpdtpaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 592 GFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSA-APSLAPGP-LVEALARV----LPDYMVPRDWYWLDVLP 665
Cdd:cd05973 344 GYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGHEGTPaLADELQLHvkkrLSAHAYPRTIHFVDELP 423
|
490
....*....|....
gi 502993051 666 LTGNGKVDRKELAR 679
Cdd:cd05973 424 KTPSGKIQRFLLRR 437
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
180-616 |
5.14e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 98.63 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 180 PDRRVHQLIADTAAARPDDVAV---VAGLDQ-LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKA 255
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALrekEDGIWQsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 256 GGCYLPVEPHFPLERIAAMVTRSAC------GRALTDEVgAAVTDRL-----------GGLVPGLRARGVDEILRGG--- 315
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAkvlfveDQEQLDKL-LEVRDELpslrhivvldpRGLRDDPRLLSLDELLALGrev 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 316 -HPSEVPGTP--VVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVV------AQTAPQCFDISLwq 386
Cdd:COG1022 168 aDPAELEARRaaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTlsflplAHVFERTVSYYA-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 387 llapLITGGTVVIVSqqallDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALR------CVSA-------- 452
Cdd:COG1022 246 ----LAAGATVAFAE-----SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKrklfrwALAVgrryarar 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 453 -------TGEALKAALVRRW--------------FAV-----LPE----------VLLVNAYGLTETCDDTNHEVLDRAQ 496
Cdd:COG1022 317 lagkspsLLLRLKHALADKLvfsklrealggrlrFAVsggaaLGPelarffralgIPVLEGYGLTETSPVITVNRPGDNR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 497 DGSrvpLGRAIAGVGVHvvdgnlmpvpLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfPGQrlYRSGDFGRWTPDG 576
Cdd:COG1022 397 IGT---VGPPLPGVEVK----------IAEDGEILVRGPNVMKGYYKNPEATAEAFDA----DGW--LHTGDIGELDEDG 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502993051 577 RLEFSGR-RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI 616
Cdd:COG1022 458 FLRITGRkKDLIVTSGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
191-677 |
1.93e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 96.21 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 191 TAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAV----VSEraipWLVAVLGVLKAGgcYLPVEP-- 264
Cdd:PRK10946 32 TRHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVqlgnVAE----FYITFFALLKLG--VAPVNAlf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 -HFPLERIA-------AMVTRSACGRALTDEvgaAVTDRLGGLVPGLR---------ARGVDEILRggHPSE-VPGTPVV 326
Cdd:PRK10946 106 sHQRSELNAyasqiepALLIADRQHALFSDD---DFLNTLVAEHSSLRvvlllnddgEHSLDDAIN--HPAEdFTATPSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 327 AGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGT--VVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQA 404
Cdd:PRK10946 181 ADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTryLCALPAAHNYPMSSPGALGVFLAGGTVVLAPDPS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 405 LLDVeqFAAeLDRSRVEVAQLVPSYVEVLLGHLERRPR--ALPALRCVSATGEALKAALVRRwfavLPEVL---LVNAYG 479
Cdd:PRK10946 261 ATLC--FPL-IEKHQVNVTALVPPAVSLWLQAIAEGGSraQLASLKLLQVGGARLSETLARR----IPAELgcqLQQVFG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 480 LTETCddTNHEVLDRAQDGSRVPLGRAIAGVG-VHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplf 558
Cdd:PRK10946 334 MAEGL--VNYTRLDDSDERIFTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDA---- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 559 pgQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvagAAESARL----VACYSAAP 634
Cdd:PRK10946 408 --NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALV---SMEDELMgeksCAFLVVKE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502993051 635 SLAPGPLVEAL-ARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK10946 483 PLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
178-676 |
2.71e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 96.22 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 178 ELPDRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGG 257
Cdd:PRK05605 28 DYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 258 cyLPVEpHFPL---------------------ERIAAMVTRSACGRALTDEVGAAVTD------RLGGLVPGLRARGVDE 310
Cdd:PRK05605 108 --VVVE-HNPLytahelehpfedhgarvaivwDKVAPTVERLRRTTPLETIVSVNMIAampllqRLALRLPIPALRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 311 ILRGGHPSEVPGTPVVAGQL-----------------AYIYFTSGSTGEPKGVMCEHEGMLNHML---AKIDDLGVRAGT 370
Cdd:PRK05605 185 ALTGPAPGTVPWETLVDAAIggdgsdvshprptpddvALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGLGDGPER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 371 VVAqTAP--QCFDISLWQLLAPLItGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALR 448
Cdd:PRK05605 265 VLA-ALPmfHAYGLTLCLTLAVSI-GGELVLLPA---PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 449 CVSATGEALKAALVRRWFAvLPEVLLVNAYGLTETcddtnhevldraqdgSRVPLG------RAIAGVGV-------HVV 515
Cdd:PRK05605 340 NAFSGAMALPVSTVELWEK-LTGGLLVEGYGLTET---------------SPIIVGnpmsddRRPGYVGVpfpdtevRIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 516 D----GNLMPVplGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIR 591
Cdd:PRK05605 404 DpedpDETMPD--GEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 592 GFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAP--SLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTG 668
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVgLPREDGSEEVVAAVVLEPgaALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQ 554
|
....*...
gi 502993051 669 NGKVDRKE 676
Cdd:PRK05605 555 LGKVRRRE 562
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
182-855 |
6.06e-20 |
|
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: 95.93 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 182 RRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLP 261
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 262 VEPHFPLERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTG 341
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 342 EPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVE 421
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 422 VAQLVPsyveVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSRV 501
Cdd:COG3319 241 LLLLAA----LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 502 PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFS 581
Cdd:COG3319 317 PIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 582 GRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWL 661
Cdd:COG3319 397 GLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPAL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 662 DVLPLTGNGKVDRKELARITGGLHRAMTEDERPRPGAERRLAAAWATVLGVAPDRVGRTDDFFASGGSSLSALQLVIELD 741
Cdd:COG3319 477 LLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 742 RAVSLGDVTAHPVLADLAGVL-----GTGATGTRPVLHRLTPPGRRTLVCFPYAGGNAVTYVPLAGELAAEgWAVYGVEP 816
Cdd:COG3319 557 LLLRLLLLLALLLAPTLAALAaalaaAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPD-RPVYGLQA 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 502993051 817 PGRDGNEAP-VSVPELAELVAGELAALDA-GPLTLWGHSTG 855
Cdd:COG3319 636 PGLDGGEPPpASVEEMAARYVEAIRAVQPeGPYHLLGWSFG 676
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
189-677 |
6.90e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 94.31 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 189 ADTAAARPDDVAVVAGlDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPL 268
Cdd:PRK13390 7 AQIAPDRPAVIVAETG-EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 269 ERI--------AAMVTRSACGRALTDEVGAAVTDRL--GGLVPGLRArgVDEILRGGHPsevPGTPVVAGqlAYIYFTSG 338
Cdd:PRK13390 86 PEAdyivgdsgARVLVASAALDGLAAKVGADLPLRLsfGGEIDGFGS--FEAALAGAGP---RLTEQPCG--AVMLYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 339 STGEPKGVMCEHEGMlnhmlaKIDdlgvRAGTVVAQTAPQCFDISLWQLL---------APL-------ITGGTVVIVSQ 402
Cdd:PRK13390 159 TTGFPKGIQPDLPGR------DVD----APGDPIVAIARAFYDISESDIYyssapiyhaAPLrwcsmvhALGGTVVLAKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 403 qalLDVEQFAAELDRSRVEVAQLVPS-YVEVLLGHLERRPR-ALPALRCVSATGEA----LKAALVrRWFAvlpeVLLVN 476
Cdd:PRK13390 229 ---FDAQATLGHVERYRITVTQMVPTmFVRLLKLDADVRTRyDVSSLRAVIHAAAPcpvdVKHAMI-DWLG----PIVYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 477 AYGLTETCDDTnheVLDRAQ----DGSrvpLGRAIAGVgVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALA- 551
Cdd:PRK13390 301 YYSSTEAHGMT---FIDSPDwlahPGS---VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAq 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 552 FTASPLFPgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLV-ACY 630
Cdd:PRK13390 374 HPAHPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVkAVI 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502993051 631 SAAPSLAPGplvEALARVLPDYM--------VPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK13390 449 QLVEGIRGS---DELARELIDYTrsriahykAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
191-677 |
8.42e-20 |
|
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: 93.98 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 191 TAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLER 270
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 271 IAAMVTRSACGRALTDEVGAAVTDRLGGLVPGlrargvdeilRGGHPsEVPGTPVVAGQlaYIYFTSGSTGEPKGVMCEH 350
Cdd:cd05929 81 ACAIIEIKAAALVCGLFTGGGALDGLEDYEAA----------EGGSP-ETPIEDEAAGW--KMLYSGGTTGRPKGIKRGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 351 EGMLNHMLAKID---DLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVP 427
Cdd:cd05929 148 PGGPPDNDTLMAaalGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK---FDPEEFLRLIERYRVTFAQFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 428 SYVEVLLgHLERRPRA---LPALRCVSATGEALKAALVRRWFAVLPEVLlVNAYGLTE----TCDDTNHEVLDRaqdGSr 500
Cdd:cd05929 225 TMFVRLL-KLPEAVRNaydLSSLKRVIHAAAPCPPWVKEQWIDWGGPII-WEYYGGTEgqglTIINGEEWLTHP---GS- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 501 vpLGRAIAGvGVHVVDGNLMPVPLGATGEIVFSGRClARGYVNDPIRTALAFTAsplfpgqRLYRS-GDFGRWTPDGRLE 579
Cdd:cd05929 299 --VGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNE-------GGWSTlGDVGYLDEDGYLY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 580 FSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAE-SARLVACYSAAPSLAPGP-LVEALARVLPDYM---- 653
Cdd:cd05929 368 LTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEElGQRVHAVVQPAPGADAGTaLAEELIAFLRDRLsryk 447
|
490 500
....*....|....*....|....
gi 502993051 654 VPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05929 448 CPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
304-683 |
9.25e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 92.03 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 304 RARGVDEILRGGHPSEVPGTPVVAgqlayiyfTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTApqcFDIS 383
Cdd:PRK07824 19 RAALLRDALRVGEPIDDDVALVVA--------TSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLALPA---HHIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 384 LWQ-LLAPLITGGTVVIVSQQALLDVEQFA---AELDRSRVeVAQLVPSYVEVLLGHLErRPRALPALRCVSATGEALKA 459
Cdd:PRK07824 88 GLQvLVRSVIAGSEPVELDVSAGFDPTALPravAELGGGRR-YTSLVPMQLAKALDDPA-ATAALAELDAVLVGGGPAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 460 ALVRRwfAVLPEVLLVNAYGLTETCddtnhevldraqdGSRVPLGRAIAGVGVHVVDgnlmpvplgatGEIVFSGRCLAR 539
Cdd:PRK07824 166 PVLDA--AAAAGINVVRTYGMSETS-------------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 540 GYVNDPIRTALAftasplFPGqrLYRSGDFGRWTpDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VA 618
Cdd:PRK07824 220 GYRNPVDPDPFA------EPG--WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFgLP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 619 GAAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARITGG 683
Cdd:PRK07824 291 DDRLGQRVVAAVVGDGGPAPTLeaLRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
174-677 |
9.31e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 94.32 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 174 GAPRELPD---RRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVL 250
Cdd:PRK07059 12 GVPAEIDAsqyPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 251 GVLKAGGCYLPVEP--------H----------FPLERIAAMVTRSACGRALTDEVGAAVTDRLG--GLVPGLRARGV-- 308
Cdd:PRK07059 92 AVLRAGYVVVNVNPlytpreleHqlkdsgaeaiVVLENFATTVQQVLAKTAVKHVVVASMGDLLGfkGHIVNFVVRRVkk 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 309 -------------DEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHML-------------AKID 362
Cdd:PRK07059 172 mvpawslpghvrfNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeawlqpafekkPRPD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 363 DLGvragTVVAQTAPQCFDISLWQLLApLITGGTVVIVSQQalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPR 442
Cdd:PRK07059 252 QLN----FVCALPLYHIFALTVCGLLG-MRTGGRNILIPNP--RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 443 ALPALRCVSATGEALKAALVRRWFAVL--PevlLVNAYGLTET-----CDDTNhevlDRAQDGSrvpLGRAIAGVGVHVV 515
Cdd:PRK07059 325 DFSKLIVANGGGMAVQRPVAERWLEMTgcP---ITEGYGLSETspvatCNPVD----ATEFSGT---IGLPLPSTEVSIR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 516 DGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRV 595
Cdd:PRK07059 395 DDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFF------RTGDVGVMDERGYTKIVDRKKDMILVSGFNV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 596 EIGEIEDRLLRLPGVREATVIVAGAAESARLVACY--SAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:PRK07059 469 YPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFvvKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKIL 548
|
....
gi 502993051 674 RKEL 677
Cdd:PRK07059 549 RREL 552
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
182-679 |
1.72e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 93.71 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 182 RRVH--QLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVV---SERAIPWLVAVLGVlkaG 256
Cdd:PLN02860 5 SQAHicQCLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAalnSDLYLEWLLAVACA---G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 257 GCYLPVEPHFPLERIAAMVTRSACGRALTDEVGAAVTDRL-GGLVPGLRAR------------------GVDEIL-RGGH 316
Cdd:PLN02860 82 GIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELqNDRLPSLMWQvflespsssvfiflnsflTTEMLKqRALG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 317 PSEVpgTPVVAGQ-LAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGG 395
Cdd:PLN02860 162 TTEL--DYAWAPDdAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 396 TVVIVSQ---QALLDVeqfaaeLDRSRVEVAQLVPSYVEVLL--GHLERRPRALPALRCVSATGEALKAALVRRWFAVLP 470
Cdd:PLN02860 240 CHVLLPKfdaKAALQA------IKQHNVTSMITVPAMMADLIslTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 471 EVLLVNAYGLTETC---------DDTNHEVLDRAQDGSRVPLGRAIAGVGV-------HVVDGNLMPVPlGATGEIVFSG 534
Cdd:PLN02860 314 NAKLFSAYGMTEACssltfmtlhDPTLESPKQTLQTVNQTKSSSVHQPQGVcvgkpapHVELKIGLDES-SRVGRILTRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 535 RCLARGYVNDPIRTALAFTASPLFPgqrlyrSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVreAT 614
Cdd:PLN02860 393 PHVMLGYWGQNSETASVLSNDGWLD------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGV--AS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 615 VIVAGAAEsARL----VACYS---------AAPSLAPGPLV---EAL-----ARVLPDYMVPRDWY-WLDVLPLTGNGKV 672
Cdd:PLN02860 465 VVVVGVPD-SRLtemvVACVRlrdgwiwsdNEKENAKKNLTlssETLrhhcrEKNLSRFKIPKLFVqWRKPFPLTTTGKI 543
|
....*..
gi 502993051 673 DRKELAR 679
Cdd:PLN02860 544 RRDEVRR 550
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
188-677 |
2.16e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 92.56 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVV--AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIpWLVAV-LGVLKAGGCYLPVEP 264
Cdd:PRK09088 1 IAFHARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSV-WLVALhFACARVGAIYVPLNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 265 HFPLERIAAMVTRSACGRALTDEVGAAvtdrlGGLVPGLRARGVDEIlRGGHPSEVPGTPvvAGQLAYIYFTSGSTGEPK 344
Cdd:PRK09088 80 RLSASELDALLQDAEPRLLLGDDAVAA-----GRTDVEDLAAFIASA-DALEPADTPSIP--PERVSLILFTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 345 GVMCEhEGMLNHMLAKIDDLG-VRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSqqalldvEQFAAELDRSRVEVA 423
Cdd:PRK09088 152 GVMLS-ERNLQQTAHNFGVLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVS-------NGFEPKRTLGRLGDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 424 QL-------VPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAvlPEVLLVNAYGLTETcddtnHEVLDRAQ 496
Cdd:PRK09088 224 ALgithyfcVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD--DGIPMVDGFGMSEA-----GTVFGMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 497 DGSRV-----PLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGR 571
Cdd:PRK09088 297 DCDVIrakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWF------RTGDIAR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 572 WTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGA--AESARLVACYSAAPSLAPGPLVEALARV 648
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgMADAqwGEVGYLAIVPADGAPLDLERIRSHLSTR 450
|
490 500
....*....|....*....|....*....
gi 502993051 649 LPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK09088 451 LAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
782-1007 |
3.81e-19 |
|
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: 87.44 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 782 RTLVCFPYAGGNAVTYVPLAGELAAEgWAVYGVEPPGRDGNEAPV-SVPELAELVAGEL-AALDAGPLTLWGHSTGVAAA 859
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPP-AEVLAVQYPGRGRGEPPLnSIEALADEYAEALrQIQPEGPYALFGHSMGGMLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 860 LATARLLRSRGHDVRRVLLgaqlpGDSGARRAQAAEVTALPDEAVVTAL--VESGRPELAEVGDAHRRLLADAYRHDVAA 937
Cdd:pfam00975 80 FEVARRLERQGEAVRSLFL-----SDASAPHTVRYEASRAPDDDEVVAEftDEGGTPEELLEDEELLSMLLPALRADYRA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502993051 938 ACGYLAEALDAGDRLdvpvtvVLAADDVP----DDLPGDPWDWSRLAGDVRVVelpDGGHYFAASRPASVARVI 1007
Cdd:pfam00975 155 LESYSCPPLDAQSAT------LFYGSDDPlhdaDDLAEWVRDHTPGEFDVHVF---DGDHFYLIEHLEAVLEII 219
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
197-677 |
2.60e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 89.65 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 197 DDVAVVAGL--DQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAM 274
Cdd:PLN02330 43 DKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 275 VTRSACGRALTDEVGAAVTDRLG------GLVPGLRARGVDEILRGGHPS--EVPGTPVVAGQLAYIYFTSGSTGEPKGV 346
Cdd:PLN02330 123 AEAAGAKLIVTNDTNYGKVKGLGlpvivlGEEKIEGAVNWKELLEAADRAgdTSDNEEILQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 347 MCEHEGMLNHMLAKIddLGVRA---GTVVAQTAPQCFDIS--LWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVE 421
Cdd:PLN02330 203 MLTHRNLVANLCSSL--FSVGPemiGQVVTLGLIPFFHIYgiTGICCATLRNKGKVVVMSR---FELRTFLNALITQEVS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 422 VAQLVPSYVEVLLGH--LERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTE-TCDDTNHEVLDRAQD- 497
Cdd:PLN02330 278 FAPIVPPIILNLVKNpiVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEhSCITLTHGDPEKGHGi 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 498 GSRVPLGRAIAGVGVHVVD-GNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpgQRLYRSGDFGRWTPDG 576
Cdd:PLN02330 358 AKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDE------DGWLHTGDIGYIDDDG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 577 RLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARL-VACYSAAPSLAPGP--LVEALARVLPDYM 653
Cdd:PLN02330 432 DIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIpAACVVINPKAKESEedILNFVAANVAHYK 511
|
490 500
....*....|....*....|....
gi 502993051 654 VPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PLN02330 512 KVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
195-677 |
3.35e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 88.87 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 195 RPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAM 274
Cdd:PRK03640 15 TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 275 VTRSACGRALTDEVGAAvtdrlgGLVPGLRARgVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEgml 354
Cdd:PRK03640 95 LDDAEVKCLITDDDFEA------KLIPGISVK-FAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYG--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 355 NHMLAKID---DLGVragtvvaqTAPQC-------FDIS-LWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVA 423
Cdd:PRK03640 165 NHWWSAVGsalNLGL--------TEDDCwlaavpiFHISgLSILMRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 424 QLVPSYVEVLLGHLERRpRALPALRCV-SATGEALKAAL---VRRWFAVlpevllVNAYGLTETC--------DDTNHEV 491
Cdd:PRK03640 234 SVVSTMLQRLLERLGEG-TYPSSFRCMlLGGGPAPKPLLeqcKEKGIPV------YQSYGMTETAsqivtlspEDALTKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 492 ldraqdGSrvpLGRAIAGVGVHVVDgNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTasplfpgQRLYRSGDFGR 571
Cdd:PRK03640 307 ------GS---AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-------DGWFKTGDIGY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 572 WTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGAAESARLVAcySAAPSLApgPLVEALA 646
Cdd:PRK03640 370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgvpddKWGQVPVAFVVK--SGEVTEE--ELRHFCE 445
|
490 500 510
....*....|....*....|....*....|.
gi 502993051 647 RVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK03640 446 EKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
207-677 |
4.49e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.97 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACG----- 281
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASllvts 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 282 -------RALTDEVGAAVTDRLGGLVPGLRARGVDEI--LRGGHPSEV-PGTPVVAGQLAYIYFTSGSTGEPKGVMCEHE 351
Cdd:PRK08008 117 aqfypmyRQIQQEDATPLRHICLTRVALPADDGVSSFtqLKAQQPATLcYAPPLSTDDTAEILFTSGTTSRPKGVVITHY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 352 GMLNHMLAKIDDLGVRAGTVVAQTAPQC-FDISLWQLLAPLITGGTVVIVSQQAlldVEQFAAELDRSRVEVAQLVPSYV 430
Cdd:PRK08008 197 NLRFAGYYSAWQCALRDDDVYLTVMPAFhIDCQCTAAMAAFSAGATFVLLEKYS---ARAFWGQVCKYRATITECIPMMI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 431 EVLLGHLERRPRALPALRCVS---ATGEALKAALVRRWfavlpEVLLVNAYGLTETCDDTnheVLDRAQDGSRVP-LGRA 506
Cdd:PRK08008 274 RTLMVQPPSANDRQHCLREVMfylNLSDQEKDAFEERF-----GVRLLTSYGMTETIVGI---IGDRPGDKRRWPsIGRP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 507 IAGVGVHVVDGNLMPVPLGATGEIVFSG---RCLARGYVNDPIRTALAFTasplfPGQRLYrSGDFGRWTPDGRLEFSGR 583
Cdd:PRK08008 346 GFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLE-----ADGWLH-TGDTGYVDEEGFFYFVDR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 584 RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAAESARLVAC-----YSAAPSLAPGPLVEALARVLPDYMVPRDW 658
Cdd:PRK08008 420 RCNMIKRGGENVSCVELENIIATHPKIQDIVVV--GIKDSIRDEAIkafvvLNEGETLSEEEFFAFCEQNMAKFKVPSYL 497
|
490
....*....|....*....
gi 502993051 659 YWLDVLPLTGNGKVDRKEL 677
Cdd:PRK08008 498 EIRKDLPRNCSGKIIKKNL 516
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
209-677 |
4.59e-18 |
|
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: 88.68 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALL-ADGLAAEDVVAVVSERaIP--WLVAVlGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALT 285
Cdd:cd05928 43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPR-VPewWLVNV-ACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 DEVGAAVTDRLGGLVPGLRAR------------GVDEILRGGHPSEvpgTPVVAGQL--AYIYFTSGSTGEPKgvMCEHE 351
Cdd:cd05928 121 SDELAPEVDSVASECPSLKTKllvseksrdgwlNFKELLNEASTEH---HCVETGSQepMAIYFTSGTTGSPK--MAEHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 352 GMLNHMLAKIDD---LGVRAGTVVAQTAPQCFDIS-LWQLLAPLITGGTVvIVSQQALLDVEQFAAELDRSRVEVAQLVP 427
Cdd:cd05928 196 HSSLGLGLKVNGrywLDLTASDIMWNTSDTGWIKSaWSSLFEPWIQGACV-FVHHLPRFDPLVILKTLSSYPITTFCGAP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 428 SYVEVLLGHLERRPRaLPALR-CVSAtGEALKAALVRRWfAVLPEVLLVNAYGLTET---CDDTNHEvldRAQDGSrvpL 503
Cdd:cd05928 275 TVYRMLVQQDLSSYK-FPSLQhCVTG-GEPLNPEVLEKW-KAQTGLDIYEGYGQTETgliCANFKGM---KIKPGS---M 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 504 GRAIAGVGVHVVDGNLMPVPLGATGEI---VFSGR--CLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRL 578
Cdd:cd05928 346 GKASPPYDVQIIDDNGNVLPPGTEGDIgirVKPIRpfGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 579 EFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGAAESARLV---ACYSAAPSLAPGPLVEALARVLP 650
Cdd:cd05928 419 WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVsspdpIRGEVVKAFVVlapQFLSHDPEQLTKELQQHVKSVTA 498
|
490 500
....*....|....*....|....*..
gi 502993051 651 DYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05928 499 PYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
207-619 |
9.72e-18 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 87.52 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACG----- 281
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKalfvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 282 -----RALTDEVGAAVTDRLGGLVPGLRA-RGVDEILRGGHPSEvpGTPV-VAGQLAYIYFTSGSTGEPKGVMCEHEGML 354
Cdd:cd05932 86 klddwKAMAPGVPEGLISISLPPPSAANCqYQWDDLIAQHPPLE--ERPTrFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 355 NHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQalldVEQFAAELDRSRVEVAQLVPS-YVEVL 433
Cdd:cd05932 164 WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES----LDTFVEDVQRARPTLFFSVPRlWTKFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 434 LGHLERRPRA-LPALRCVSATGealkaALVRRWF----------------AVLPEVLL----------VNAYGLTETCDD 486
Cdd:cd05932 240 QGVQDKIPQQkLNLLLKIPVVN-----SLVKRKVlkglgldqcrlagcgsAPVPPALLewyrslglniLEAYGMTENFAY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 487 TNHEVLDRAQDGSrvpLGRAIAGVGVHVVDgnlmpvplgaTGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRS 566
Cdd:cd05932 315 SHLNYPGRDKIGT---VGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEATAEAFTADGFL------RT 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 502993051 567 GDFGRWTPDGRLEFSGR-RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAG 619
Cdd:cd05932 376 GDKGELDADGNLTITGRvKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
291-677 |
1.48e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.51 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 291 AVTDRLGGLVPGL---RARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:PRK05677 167 AVVKHVKKMVPAYhlpQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSN 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AG----TVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQAllDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRA 443
Cdd:PRK05677 247 LNegceILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPR--DLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLD 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 444 LPALRCVSATGEALKAALVRRWFAVLPEVLLvNAYGLTETCDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMPVP 523
Cdd:PRK05677 325 FSALKLTLSGGMALQLATAERWKEVTGCAIC-EGYGMTETSPVVSVNPSQAIQVGT---IGIPVPSTLCKVIDDDGNELP 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 524 LGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDR 603
Cdd:PRK05677 401 LGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 604 LLRLPGVREATVI---VAGAAESARLVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK05677 475 LAALPGVLQCAAIgvpDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
171-616 |
1.72e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 87.26 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 171 AFSGAPR-------ELPDRRVHQLIADTAAARPDDVAVVaglDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERaI 243
Cdd:PRK04319 33 EFSWLETgkvniayEAIDRHADGGRKDKVALRYLDASRK---EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPR-I 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 244 PWL-VAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSAcGRALTdevgaaVTDRLgglvpgLRARGVDE-------ILRGG 315
Cdd:PRK04319 109 PELyFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLI------TTPAL------LERKPADDlpslkhvLLVGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 316 HPSEVPGT-----------------PVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTA-P 377
Cdd:PRK04319 176 DVEEGPGTldfnalmeqasdefdieWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVYWCTAdP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 378 QCFDISLWQLLAPLITGGTVVIvsqqallDVEQFAAE-----LDRSRVEVAQLVPSYVEVLLGHLE--RRPRALPALRCV 450
Cdd:PRK04319 256 GWVTGTSYGIFAPWLNGATNVI-------DGGRFSPErwyriLEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDLSSLRHI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 451 SATGEALKaalvrrwfavlPEVLL--VNAYGL--------TET-----CddtNHEVLDrAQDGSrvpLGRAIAGVGVHVV 515
Cdd:PRK04319 329 LSVGEPLN-----------PEVVRwgMKVFGLpihdnwwmTETggimiA---NYPAMD-IKPGS---MGKPLPGIEAAIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 516 DGNLMPVPLGATGEivfsgrcLA---------RGYVNDPIRTALAFtasplFPGqrLYRSGDFGRWTPDGRLEFSGRRDT 586
Cdd:PRK04319 391 DDQGNELPPNRMGN-------LAikkgwpsmmRGIWNNPEKYESYF-----AGD--WYVSGDSAYMDEDGYFWFQGRVDD 456
|
490 500 510
....*....|....*....|....*....|
gi 502993051 587 QVKIRGFRVEIGEIEDRLLRLPGVREATVI 616
Cdd:PRK04319 457 VIKTSGERVGPFEVESKLMEHPAVAEAGVI 486
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
196-692 |
2.72e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.61 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV 275
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALTDEVGAAVTDRLGGLVPG------LRARGVDEI----------------LRGGHPsevpgTPVVAGQLAYI 333
Cdd:PLN03102 108 RHAKPKILFVDRSFEPLAREVLHLLSSedsnlnLPVIFIHEIdfpkrpsseeldyeclIQRGEP-----TPSLVARMFRI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 334 Y---------FTSGSTGEPKGVMCEHEGMLNHMLAKIddLGVRAGT--VVAQTAPQcFDISLWQLL-APLITGGTVVIVS 401
Cdd:PLN03102 183 QdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAI--IGWEMGTcpVYLWTLPM-FHCNGWTFTwGTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 402 QqalLDVEQFAAELDRSRVEVAQLVPSYVEVLL--GHLERRPRALPALrcVSATGEALKAALVRRWFAVLPEVLlvNAYG 479
Cdd:PLN03102 260 H---VTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVH--VLTGGSPPPAALVKKVQRLGFQVM--HAYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 480 LTET------CD--------DTNHEVLDRAQDGSRVpLGraIAGVGVHVVDgNLMPVPL-GAT-GEIVFSGRCLARGYVN 543
Cdd:PLN03102 333 LTEAtgpvlfCEwqdewnrlPENQQMELKARQGVSI-LG--LADVDVKNKE-TQESVPRdGKTmGEIVIKGSSIMKGYLK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 544 DPIRTALAFTASPLfpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVA----- 618
Cdd:PLN03102 409 NPKATSEAFKHGWL-------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMphptw 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 619 GAAESARLVACYSAAPSLAP--------GPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARITGGLhraMTE 690
Cdd:PLN03102 482 GETPCAFVVLEKGETTKEDRvdklvtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGL---VVE 558
|
..
gi 502993051 691 DE 692
Cdd:PLN03102 559 DE 560
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
207-679 |
7.72e-17 |
|
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: 84.33 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGcylpvephfplerIAAMVTRSACGRALTD 286
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA-------------VAALINYNLRGESLAH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 EVGaavtdrlgglvpglrargvdeILRGGHpsevpgtpVVAGQLAYIYfTSGSTGEPKGVMCEHEGMLNhMLAKIDDLGV 366
Cdd:cd05940 70 CLN---------------------VSSAKH--------LVVDAALYIY-TSGTTGLPKAAIISHRRAWR-GGAFFAGSGG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 367 RAGTVVAQTAPQCFDIS--LWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQlvpsYVEVLLGHLERRPRAL 444
Cdd:cd05940 119 ALPSDVLYTCLPLYHSTalIVGWSACLASGATLVIRKK---FSASNFWDDIRKYQATIFQ----YIGELCRYLLNQPPKP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 P----ALRCVSATGeaLKAALVRRW---FAVlPEVLlvNAYGLTE-TCDDTNHEVLDRA--QDGSRVPLGRAIAGVGVHV 514
Cdd:cd05940 192 TerkhKVRMIFGNG--LRPDIWEEFkerFGV-PRIA--EFYAATEgNSGFINFFGKPGAigRNPSLLRKVAPLALVKYDL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 515 --------VDGNLMPVPLGATGEIVFSGRCLAR--GYVnDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRR 584
Cdd:cd05940 267 esgepirdAEGRCIKVPRGEPGLLISRINPLEPfdGYT-DPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 585 DTQVKIRGFRVEIGEIEDRLLRLPGVREATVI------VAGAAESARLVACYSAAPSLApgPLVEALARVLPDYMVPRDW 658
Cdd:cd05940 346 GDTFRWKGENVSTTEVAAVLGAFPGVEEANVYgvqvpgTDGRAGMAAIVLQPNEEFDLS--ALAAHLEKNLPGYARPLFL 423
|
490 500
....*....|....*....|.
gi 502993051 659 YWLDVLPLTGNGKVDRKELAR 679
Cdd:cd05940 424 RLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
200-677 |
1.07e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 84.36 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 200 AVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSA 279
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 280 CG---------RALTDEVGAAVTDRLGGLVPGLRAR-GVDEILRGGHP-----------SEVPGTPVVAGQLAYIYfTSG 338
Cdd:PRK12406 84 ARvliahadllHGLASALPAGVTVLSVPTPPEIAAAyRISPALLTPPAgaidwegwlaqQEPYDGPPVPQPQSMIY-TSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 339 STGEPKGV-----MCEHEGMLNHMLAKIddLGVRAGTVVAQT------APQCFDISLWQLlaplitGGTVVIvsqQALLD 407
Cdd:PRK12406 163 TTGHPKGVrraapTPEQAAAAEQMRALI--YGLKPGIRALLTgplyhsAPNAYGLRAGRL------GGVLVL---QPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 408 VEQFAAELDRSRVEVAQLVPS-YVEVLLGHLERRPR-ALPALRCVSATGEA----LKAALVRRWFAVLPEVllvnaYGLT 481
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTmFIRLLKLPEEVRAKyDVSSLRHVIHAAAPcpadVKRAMIEWWGPVIYEY-----YGST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 482 ETCDDTNHEvldrAQDGSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVfsgrCLARG-----YVNDPIRTALAFTA 554
Cdd:PRK12406 307 ESGAVTFAT----SEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIY----SRIAGnpdftYHNKPEKRAEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 555 SplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVAcysAAP 634
Cdd:PRK12406 379 G-------FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALM---AVV 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502993051 635 SLAPGPLVEA------LARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK12406 449 EPQPGATLDEadiraqLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
173-677 |
1.21e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 84.34 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 173 SGAPRELPDRRVHQLIA--DTAAAR-PDDVAVVAGLDQLTYRQLDERANQVAhALLADGLAAE--DVVAVVSERAIPWLV 247
Cdd:PRK08974 11 ADVPAEINPDRYQSLVDmfEQAVARyADQPAFINMGEVMTFRKLEERSRAFA-AYLQNGLGLKkgDRVALMMPNLLQYPI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 248 AVLGVLKAGGCYLPVEPHF-PLER--------IAAMVTRSACGRALTD-----EVGAAVTDRLG---------------- 297
Cdd:PRK08974 90 ALFGILRAGMIVVNVNPLYtPRELehqlndsgAKAIVIVSNFAHTLEKvvfktPVKHVILTRMGdqlstakgtlvnfvvk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 298 ---GLVPGLR---ARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGML-NHMLAK-IDDLGVRAG 369
Cdd:PRK08974 170 yikRLVPKYHlpdAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKaAYGPLLHPG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 370 TVVAQTApqcfdISLWQLLAPLITGGTVVIVSQQALL-----DVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRAL 444
Cdd:PRK08974 250 KELVVTA-----LPLYHIFALTVNCLLFIELGGQNLLitnprDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRWfAVLPEVLLVNAYGLTE-----TCDDTNhevLDRaQDGSrvpLGRAIAGVGVHVVDGNL 519
Cdd:PRK08974 325 SSLKLSVGGGMAVQQAVAERW-VKLTGQYLLEGYGLTEcsplvSVNPYD---LDY-YSGS---IGLPVPSTEIKLVDDDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 520 MPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLfpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGE 599
Cdd:PRK08974 397 NEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWL-------ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 600 IEDRLLRLPGVREATVIVAGAAESARLVACYSAA--PSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK08974 470 IEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKkdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
208-681 |
1.76e-16 |
|
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: 83.00 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDE 287
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 VGAAVtdrlgglvpglrargvDEILrgghpsevpgtpvvagqlayIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd05974 81 NTHAD----------------DPML--------------------LYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVVAQTAPQCFDISLWQ-LLAPLITGGTVVIVSQqALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGhlERRPRALPA 446
Cdd:cd05974 125 PGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNY-ARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ--QDLASFDVK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 447 LRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTETCDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMPVPLGA 526
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNSPGQPVKAGS---MGRPLPGYRVALLDPDGAPATEGE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 527 TGEIVFSGR--CLARGYVNDPIRTALAFtasplfpGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRL 604
Cdd:cd05974 278 VALDLGDTRpvGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 605 LRLPGVREATVIVAGAAESAR-------LVACYSAAPSLAPGPLVEALARVLPDYMVPRdwYWLDVLPLTGNGKVDRKEL 677
Cdd:cd05974 351 IEHPAVAEAAVVPSPDPVRLSvpkafivLRAGYEPSPETALEIFRFSRERLAPYKRIRR--LEFAELPKTISGKIRRVEL 428
|
....
gi 502993051 678 ARIT 681
Cdd:cd05974 429 RRRE 432
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
333-674 |
2.42e-16 |
|
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: 81.55 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 333 IYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDIS-LWQLLAPLITGGTVVIVSQqalLDVEQF 411
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLP-LFHIAgLNLALATFHAGGANVVMEK---FDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 412 AAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSAtgeaLKA-ALVRRWFAVLPEVLLVnAYGLTET-CDDTNH 489
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLG----LDApETIQRFEETTGATFWS-LYGQTETsGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 490 EVLDRaqDGSrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDF 569
Cdd:cd17637 156 PYRER--PGS---AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 570 GRWTPDGRLEFSGRRDTQ--VKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGA--AESARLVACYSAAPSLAPGPLVEA 644
Cdd:cd17637 224 GRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIgVPDPkwGEGIKAVCVLKPGATLTADELIEF 303
|
330 340 350
....*....|....*....|....*....|
gi 502993051 645 LARVLPDYMVPRDWYWLDVLPLTGNGKVDR 674
Cdd:cd17637 304 VGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
175-679 |
4.61e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.70 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 175 APRELPDRrVHQLIADTAAARPDDVAVVAGLD--------QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWL 246
Cdd:PRK07529 19 AARDLPAS-TYELLSRAAARHPDAPALSFLLDadpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 247 VAVLGVlKAGGCYLPVEPHFPLERIAAMVTRS--------------------ACGRALTDEVGAAVTDRLGGLVPGLRAR 306
Cdd:PRK07529 98 FALWGG-EAAGIANPINPLLEPEQIAELLRAAgakvlvtlgpfpgtdiwqkvAEVLAALPELRTVVEVDLARYLPGPKRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 307 GVDEILRGGH---------------PSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGML-NHMLAKIDDLGVRAGT 370
Cdd:PRK07529 177 AVPLIRRKAHarildfdaelarqpgDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVaNAWLGALLLGLGPGDT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 371 VVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLD---VEQFAAELDRSRVEVAQLVPSYVEVLLghleRRP---RAL 444
Cdd:PRK07529 257 VFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALL----QVPvdgHDI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 445 PALRCVSATGEALKAALVRRwFAVLPEVLLVNAYGLTE-TCDDTNHEVLDRAQDGS---RVPLGRaiagVGVHVVDGN-- 518
Cdd:PRK07529 333 SSLRYALCGAAPLPVEVFRR-FEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSvglRLPYQR----VRVVILDDAgr 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 519 -LMPVPLGATGEIVFSGRCLARGYVNdpirtalAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVkIR-GFRVE 596
Cdd:PRK07529 408 yLRDCAVDEVGVLCIAGPNVFSGYLE-------AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNID 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 597 IGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAapsLAPGPLVE-------ALARVLPDYMVPRDWYWLDVLPLTGN 669
Cdd:PRK07529 480 PAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQ---LKPGASATeaellafARDHIAERAAVPKHVRILDALPKTAV 556
|
570
....*....|
gi 502993051 670 GKVDRKELAR 679
Cdd:PRK07529 557 GKIFKPALRR 566
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
188-677 |
9.35e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 81.36 E-value: 9.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGlAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFP 267
Cdd:PRK07638 7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 LERIAAMVTRSACGRALTDEVgaAVTDRLGGLVPGLRARGVDEILRGGHPSEVPGTPVvagQLAYIY--FTSGSTGEPKG 345
Cdd:PRK07638 86 QDELKERLAISNADMIVTERY--KLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENV---QNAPFYmgFTSGSTGKPKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 346 VMCEHEGMLNHMLAKIDDLGVR-------AGTVVAQtapqcfdISLWQLLAPLITGGTVVIVSQQALLDVEQfaaELDRS 418
Cdd:PRK07638 161 FLRAQQSWLHSFDCNVHDFHMKredsvliAGTLVHS-------LFLYGAISTLYVGQTVHLMRKFIPNQVLD---KLETE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 419 RVEVAQLVPSYVEVLLghlerRPRALP--ALRCVSaTGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDT--NHEvldr 494
Cdd:PRK07638 231 NISVMYTVPTMLESLY-----KENRVIenKMKIIS-SGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTalVDE---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 495 aqDGSRVP--LGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTalaftasPLFPGQRLYRSGDFGRW 572
Cdd:PRK07638 301 --ESERRPnsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLA-------RELNADGWMTVRDVGYE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 573 TPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI--------------VAGAAESARLVAcysaapslap 638
Cdd:PRK07638 372 DEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIgvpdsywgekpvaiIKGSATKQQLKS---------- 441
|
490 500 510
....*....|....*....|....*....|....*....
gi 502993051 639 gplveALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK07638 442 -----FCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
193-680 |
3.26e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.89 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 193 AARPDDVAVVAGLD--QLTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLE 269
Cdd:PLN02574 50 HNHNGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 270 RIAAMVTRSACGRALTdevgaaVTDRLGGLVP-GLRARGVDE---------------ILRGGHPSEVPGTPVVAGQLAYI 333
Cdd:PLN02574 130 EIKKRVVDCSVGLAFT------SPENVEKLSPlGVPVIGVPEnydfdskriefpkfyELIKEDFDFVPKPVIKQDDVAAI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 334 YFTSGSTGEPKGVMCEHEGMLNHMlakidDLGVR----------AGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQ 403
Cdd:PLN02574 204 MYSSGTTGASKGVVLTHRNLIAMV-----ELFVRfeasqyeypgSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 404 alLDVEQFAAELDRSRVEVAQLVPSyvevLLGHLERRPRA-----LPALRCVSATGEALKAALVRRWFAVLPEVLLVNAY 478
Cdd:PLN02574 279 --FDASDMVKVIDRFKVTHFPVVPP----ILMALTKKAKGvcgevLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 479 GLTE-TCDDT---NHEVLDR-AQDGSRVPLGRAIAgvgVHVVDGNLMPvPlGATGEIVFSGRCLARGYVNDPIRTALAFT 553
Cdd:PLN02574 353 GMTEsTAVGTrgfNTEKLSKySSVGLLAPNMQAKV---VDWSTGCLLP-P-GNCGELWIQGPGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 554 ASPLFpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACY--- 630
Cdd:PLN02574 428 KDGWL------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFvvr 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502993051 631 SAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARI 680
Cdd:PLN02574 502 RQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
208-637 |
6.95e-15 |
|
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: 78.25 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSacgraltDE 287
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS-------EA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 VGAAVTDRlgglvpglrargvDEilrgghpsevpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVR 367
Cdd:cd05914 81 KAIFVSDE-------------DD-------------------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 AGTVV------AQTAPQCFDislwqLLAPLITGGTVVIVSQ--QALLDVEQFAaeldrsRVEVAQLVPsyveVLLGHLER 439
Cdd:cd05914 129 KGDKIlsilplHHIYPLTFT-----LLLPLLNGAHVVFLDKipSAKIIALAFA------QVTPTLGVP----VPLVIEKI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 440 RPRALPALRCVSATGEALKAALVRRWF------------------------AVLPEVL---------LVNAYGLTETC-- 484
Cdd:cd05914 194 FKMDIIPKLTLKKFKFKLAKKINNRKIrklafkkvheafggnikefviggaKINPDVEeflrtigfpYTIGYGMTETApi 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 485 ---DDTNHEVLDRAqdgsrvplGRAIAGVGVHVVDgnlmPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgq 561
Cdd:cd05914 274 isySPPNRIRLGSA--------GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWF--- 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 562 rlyRSGDFGRWTPDGRLEFSGR-RDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLA 637
Cdd:cd05914 339 ---HTGDLGKIDAEGYLYIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKA 412
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
209-616 |
9.38e-15 |
|
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: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSA-----CGRA 283
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKptivfCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 284 LTDEVgAAVTDRLGgLVPGLRARGVDEILRG-------------GHPSEVPGTPVVAG---QLAYIYFTSGSTGEPKGVM 347
Cdd:cd17642 126 GLQKV-LNVQKKLK-IIKTIIILDSKEDYKGyqclytfitqnlpPGFNEYDFKPPSFDrdeQVALIMNSSGSTGLPKGVQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 348 CEHEGMLNHMLAKIDDL---GVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQ 424
Cdd:cd17642 204 LTHKNIVARFSHARDPIfgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYK---FEEELFLRSLQDYKVQSAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LVPSYVEVLLGHLERRPRALPALRCVSATGEALKAAL---VRRWFAvLPEVLlvNAYGLTETcddTNHEVLDRAQDGSRV 501
Cdd:cd17642 281 LVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVgeaVAKRFK-LPGIR--QGYGLTET---TSAILITPEGDDKPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 502 PLGRAIAGVGVHVVD---GNLmpvpLGA--TGEIVFSGRCLARGYVNDPIRTalaftaSPLFPGQRLYRSGDFGRWTPDG 576
Cdd:cd17642 355 AVGKVVPFFYAKVVDldtGKT----LGPneRGELCVKGPMIMKGYVNNPEAT------KALIDKDGWLHSGDIAYYDEDG 424
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502993051 577 RLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI 616
Cdd:cd17642 425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA 464
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
186-616 |
1.43e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 77.93 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 186 QLIADTAAARPDDVAVVAgLDQ---LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPV 262
Cdd:PRK08315 20 QLLDRTAARYPDREALVY-RDQglrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 263 EPHFPLERIAAMVTRSACgRAL-----------------------TDEVGAAVTDRLgglvPGLR---------ARG--- 307
Cdd:PRK08315 99 NPAYRLSELEYALNQSGC-KALiaadgfkdsdyvamlyelapelaTCEPGQLQSARL----PELRrviflgdekHPGmln 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 308 VDEILRGGHPSEVPGTPVVAGQLAY-----IYFTSGSTGEPKGVMCEHEGMLNHmlakiddlgvraGTVVAQT---APQ- 378
Cdd:PRK08315 174 FDELLALGRAVDDAELAARQATLDPddpinIQYTSGTTGFPKGATLTHRNILNN------------GYFIGEAmklTEEd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 379 ----------CFDISLwQLLAPLITGGTVVIVSQ-----QALLDVEQ------------FAAELDrsrvevaqlvpsyve 431
Cdd:PRK08315 242 rlcipvplyhCFGMVL-GNLACVTHGATMVYPGEgfdplATLAAVEEerctalygvptmFIAELD--------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 432 vllgHLERRPRALPALRcvsaTG---------EALKAAlVRRWFavLPEVLLvnAYGLTETC--------DDTnhevLDR 494
Cdd:PRK08315 306 ----HPDFARFDLSSLR----TGimagspcpiEVMKRV-IDKMH--MSEVTI--AYGMTETSpvstqtrtDDP----LEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 495 aqdgsRV-PLGRAIAGVGVHVVD---GNlmPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpgQRLYRSGDFG 570
Cdd:PRK08315 369 -----RVtTVGRALPHLEVKIVDpetGE--TVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA------DGWMHTGDLA 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502993051 571 RWTPDGRLEFSGRrdtqVK---IRGfrveiG------EIEDRLLRLPGVREATVI 616
Cdd:PRK08315 436 VMDEEGYVNIVGR----IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVV 481
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
208-589 |
1.54e-14 |
|
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: 77.64 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGgcyLPVephfpleriaamVTrsacgraltde 287
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPI------------VT----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 288 vgaaVTDRLG--GLVPGLRARGVDEILRGGHPSEvpgtpvvagqLAYIYFTSGSTGEPKGVMCEHEGM---LNHMLAKID 362
Cdd:cd17639 60 ----VYATLGedALIHSLNETECSAIFTDGKPDD----------LACIMYTSGSTGNPKGVMLTHGNLvagIAGLGDRVP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 363 DLGVRAGTVVAQTaPQ------CFDISLwqllapLITGGTVVIVSQQALL---------DVEQF--------AAELDRSR 419
Cdd:cd17639 126 ELLGPDDRYLAYL-PLahifelAAENVC------LYRGGTIGYGSPRTLTdkskrgckgDLTEFkptlmvgvPAIWDTIR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 420 VEVAQLVP--SYVE--VLLGHLERRPRALPALRCV------------SATGEALKAALV---------RRWFAVL--Pev 472
Cdd:cd17639 199 KGVLAKLNpmGGLKrtLFWTAYQSKLKALKEGPGTplldelvfkkvrAALGGRLRYMLSggaplsadtQEFLNIVlcP-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 473 lLVNAYGLTETCddTNHEVLD-RAQDGSRVplGRAIAGVGVHVVD------GNLMPVPlgaTGEIVFSGRCLARGYVNDP 545
Cdd:cd17639 277 -VIQGYGLTETC--AGGTVQDpGDLETGRV--GPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNP 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 502993051 546 IRTALAFTasplfpGQRLYRSGDFGRWTPDGRLEFSGRRDTQVK 589
Cdd:cd17639 349 EKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVK 386
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
209-677 |
4.71e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 76.28 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDEV 288
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 289 GAAVTDRLGGLVPGLR------------ARGVD----EILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEG 352
Cdd:PRK07008 121 FLPLVDALAPQCPNVKgwvamtdaahlpAGSTPllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 353 MLNHMLAKI--DDLGVRAGTVVAQTAPQcFDISLWQL--LAPLiTGGTVVIVSQQalLD----VEQFAAEldrsRVEVAQ 424
Cdd:PRK07008 201 TVLHAYGAAlpDAMGLSARDAVLPVVPM-FHVNAWGLpySAPL-TGAKLVLPGPD--LDgkslYELIEAE----RVTFSA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 425 LVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTE-----TCDDTNHEVLDRAQDGS 499
Cdd:PRK07008 273 GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEmsplgTLCKLKWKHSQLPLDEQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 500 RVPL---GRAIAGVGVHVVDGNLMPVPLG--ATGEIVFSGRCLARGYVNDpirtalafTASPLFPGqrLYRSGDFGRWTP 574
Cdd:PRK07008 352 RKLLekqGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWVIDRYFRG--------DASPLVDG--WFPTGDVATIDA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 575 DGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGAA-----ESARLVACYSAAPSLAPGPLVEALARVL 649
Cdd:PRK07008 422 DGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACI--ACAhpkwdERPLLVVVKRPGAEVTREELLAFYEGKV 499
|
490 500
....*....|....*....|....*...
gi 502993051 650 PDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK07008 500 AKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
192-677 |
5.09e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.04 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERaIPWLV-AVLGVLKAGGCYLPVEPHFPLER 270
Cdd:PLN02479 30 AVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPN-IPAMYeAHFGVPMAGAVVNCVNIRLNAPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 271 IAAMVTRSACGRALTDE---------------------------VGAAVTDRLGGLVPGLRaRGV---DEILRGGHPSEV 320
Cdd:PLN02479 109 IAFLLEHSKSEVVMVDQefftlaeealkilaekkkssfkpplliVIGDPTCDPKSLQYALG-KGAieyEKFLETGDPEFA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 321 PGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQ------CFDislWQLLAPLITG 394
Cdd:PLN02479 188 WKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMfhcngwCFT---WTLAALCGTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 395 GTVVIVSQQALLD------VEQFAAeldrSRVEVAQLVPSYVEVLLGHLerrPRALPALRCVSATGEALKAALVRRWFAV 468
Cdd:PLN02479 265 ICLRQVTAKAIYSaianygVTHFCA----APVVLNTIVNAPKSETILPL---PRVVHVMTAGAAPPPSVLFAMSEKGFRV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 469 lpevllVNAYGLTETCDDT----------NHEVLDRAQDGSRVPLgRAIAGVGVHVVDGNLM-PVPL-GAT-GEIVFSGR 535
Cdd:PLN02479 338 ------THTYGLSETYGPStvcawkpewdSLPPEEQARLNARQGV-RYIGLEGLDVVDTKTMkPVPAdGKTmGEIVMRGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 536 CLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATV 615
Cdd:PLN02479 411 MVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993051 616 iVAGAAES-----ARLVACYSAAPSLAPGPLVEALARV----LPDYMVPRDWYWlDVLPLTGNGKVDRKEL 677
Cdd:PLN02479 484 -VARPDERwgespCAFVTLKPGVDKSDEAALAEDIMKFcrerLPAYWVPKSVVF-GPLPKTATGKIQKHVL 552
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
175-344 |
6.56e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 75.68 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 175 APRELPDRrvhqlIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLK 254
Cdd:PRK08279 35 SKRSLGDV-----FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 255 AGGcylpvephfplerIAAMVTRSACGRALT--------------DEVGAAVTDRLGGLVPGLRA-----------RGVD 309
Cdd:PRK08279 110 LGA-------------VVALLNTQQRGAVLAhslnlvdakhlivgEELVEAFEEARADLARPPRLwvaggdtlddpEGYE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 502993051 310 EILR--GGHPSEVPGT--PVVAGQLAYIYFTSGSTGEPK 344
Cdd:PRK08279 177 DLAAaaAGAPTTNPASrsGVTAKDTAFYIYTSGTTGLPK 215
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
168-678 |
8.59e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.43 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 168 QLTAFSGAPRELPDRRVHQliadtAAARPDDVAV--VAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPW 245
Cdd:PRK05857 5 KFQAMPQLPSTVLDRVFEQ-----ARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 246 LVAVLGVLKAGGCYLPVEPHFP---LERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLRargVDEILRGGHPSEVPG 322
Cdd:PRK05857 80 YLSVLACAKLGAIAVMADGNLPiaaIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIA---VDIAAVTRESEHSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 323 TPVVAGQLAY-------IYFTSGSTGEPKGVMcehegMLNHMLAKIDDL----GVR-----AGTVVAQTAPQCFDISLWQ 386
Cdd:PRK05857 157 AASLAGNADQgsedplaMIFTSGTTGEPKAVL-----LANRTFFAVPDIlqkeGLNwvtwvVGETTYSPLPATHIGGLWW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 387 LLAPLITGGTVVIVSQQALLDVEQfaaeLDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRrwF 466
Cdd:PRK05857 232 ILTCLMHGGLCVTGGENTTSLLEI----LTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR--F 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 467 AVLPEVLLVNAYGLTET-----CDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLAR-- 539
Cdd:PRK05857 306 IEATGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGA---VGRPYPGVDVYLAATDGIGPTAPGAGPSASFGTLWIKsp 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 540 ----GYVNDPIRtalafTASPLFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATV 615
Cdd:PRK05857 383 anmlGYWNNPER-----TAEVLIDG--WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAAC 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993051 616 IVAGAAESARLVACYSAAPSLAPGPLVEALARVL-------PDYMV-PRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:PRK05857 456 YEIPDEEFGALVGLAVVASAELDESAARALKHTIaarfrreSEPMArPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
560-677 |
9.64e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 74.30 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 560 GQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGaaesARLVACYSAAP 634
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdpVAG----ERVKAKVISHE 364
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 502993051 635 SLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK08308 365 EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
203-679 |
1.44e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 74.82 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 203 AGLDQLTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACG 281
Cdd:PRK05620 34 AEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 282 RALTDEVGAavtDRLGGL---VPGLRArgvdEILRGGHPSEVPGTPVVAGQLAYIY------------------------ 334
Cdd:PRK05620 114 VIVADPRLA---EQLGEIlkeCPCVRA----VVFIGPSDADSAAAHMPEGIKVYSYealldgrstvydwpeldettaaai 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 335 -FTSGSTGEPKGVMCEHEGMLNH--MLAKIDDLGVRAGTVVAQTAP------QCFDISLWQLLAPLITGGtvvivsqqAL 405
Cdd:PRK05620 187 cYSTGTTGAPKGVVYSHRSLYLQslSLRTTDSLAVTHGESFLCCVPiyhvlsWGVPLAAFMSGTPLVFPG--------PD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 406 LDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLpEVLLVNAYGLTET-- 483
Cdd:PRK05620 259 LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETsp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 484 CDDTNHE---VLDRAQDGSRVPLGRAIAGVGVHVV-DGNLMPVPLGATGEIVFSGRCLARGYVNDPIRT----ALAFT-- 553
Cdd:PRK05620 338 VGTVARPpsgVSGEARWAYRVSQGRFPASLEYRIVnDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaASTFRge 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 554 ----ASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVA 628
Cdd:PRK05620 418 dvedANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIgYPDDKWGERPLA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 629 CYSAAPSLAPGP-----LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:PRK05620 498 VTVLAPGIEPTRetaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
209-677 |
1.50e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 74.40 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 209 TYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTDEV 288
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 289 GAAVTDRLGGLVPGLR------------------ARGVDEILRGGHPSEVPGTpVVAGQLAYIYFTSGSTGEPKGVMCEH 350
Cdd:PRK06018 121 FVPILEKIADKLPSVEryvvltdaahmpqttlknAVAYEEWIAEADGDFAWKT-FDENTAAGMCYTSGTTGDPKGVLYSH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 351 EGMLNH--MLAKIDDLGVRAGTVVAQTAPQcFDISLWQLLAPLITGGTvVIVSQQALLDVEQFAAELDRSRVEVAQLVPS 428
Cdd:PRK06018 200 RSNVLHalMANNGDALGTSAADTMLPVVPL-FHANSWGIAFSAPSMGT-KLVMPGAKLDGASVYELLDTEKVTFTAGVPT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 429 YVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVllVNAYGLTETCDDTNHEVL--------DRAQDGSR 500
Cdd:PRK06018 278 VWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEV--RHAWGMTEMSPLGTLAALkppfsklpGDARLDVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 501 VPLGRAIAGVGVHVVD--GNLMPVPLGATGEIVFSGRCLARGY--VNDPIRTALAFtasplfpgqrlYRSGDFGRWTPDG 576
Cdd:PRK06018 356 QKQGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYyrVDGEILDDDGF-----------FDTGDVATIDAYG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 577 RLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIvaGA-----AESARLVACYSAAPSLAPGPLVEALARVLPD 651
Cdd:PRK06018 425 YMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI--GVyhpkwDERPLLIVQLKPGETATREEILKYMDGKIAK 502
|
490 500
....*....|....*....|....*.
gi 502993051 652 YMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK06018 503 WWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
323-673 |
2.81e-13 |
|
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: 72.33 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 323 TPVVAgqlayIYfTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPqCFDI-SLWQLLAPLITGGTVVIVS 401
Cdd:cd17636 1 DPVLA-----IY-TAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGP-LFHIgTLMFTLATFHAGGTNVFVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 402 QqalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGE--ALKAALVRRWFAVLPevllvnAYG 479
Cdd:cd17636 74 R---VDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG------GYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 480 LTETCDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfp 559
Cdd:cd17636 145 QTEVMGLATFAALGGGAIGG---AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 560 gqRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGA--AESARLVACYSAAPSL 636
Cdd:cd17636 217 --GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIgVPDPrwAQSVKAIVVLKPGASV 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 502993051 637 APGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVD 673
Cdd:cd17636 295 TEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
173-583 |
5.75e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.77 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 173 SGAPRELPDRRVHQLIADTAAARPDDVAVV------AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWL 246
Cdd:PRK12582 40 SRHPLGPYPRSIPHLLAKWAAEAPDRPWLAqrepghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 247 VAVLGVLKAGGCYLPVEP--------HFPLERIAAMVT----------RSACGRALTDEVGAAVTdRLGGLVPGLRARGV 308
Cdd:PRK12582 120 LMTLAAMQAGVPAAPVSPayslmshdHAKLKHLFDLVKprvvfaqsgaPFARALAALDLLDVTVV-HVTGPGEGIASIAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 309 DEILrgghpsevpGTPVVAG-----------QLAYIYFTSGSTGEPKGVMCEHeGMLNHMLAKIDDLGVRAGTvvaQTAP 377
Cdd:PRK12582 199 ADLA---------ATPPTAAvaaaiaaitpdTVAKYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPD---PPPP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 378 QCFDISLWQ--------LLAPLITGGTVVIVSQQALldVEQFAAELDRSRvEVAQL----VPSYVEVLLGHLERRPrALP 445
Cdd:PRK12582 266 VSLDWMPWNhtmggnanFNGLLWGGGTLYIDDGKPL--PGMFEETIRNLR-EISPTvygnVPAGYAMLAEAMEKDD-ALR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 446 A-----LRCVSATGEALKAALVRRWFAVL-----PEVLLVNAYGLTETCDDTnhevLDRAQDGSRVPL-GRAIAGVGVHV 514
Cdd:PRK12582 342 RsffknLRLMAYGGATLSDDLYERMQALAvrttgHRIPFYTGYGATETAPTT----TGTHWDTERVGLiGLPLPGVELKL 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502993051 515 vdgnlmpVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplfpgQRLYRSGDFGRWTPDGRLE----FSGR 583
Cdd:PRK12582 418 -------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDE------EGFYRLGDAARFVDPDDPEkgliFDGR 477
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
319-700 |
7.05e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 72.37 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 319 EVPGTPvvAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDL--GVRAGTVVAQTAP--QCFDISLWQLLApLITG 394
Cdd:PRK06710 199 EVPCDP--ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLynCKEGEEVVLGVLPffHVYGMTAVMNLS-IMQG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 395 GTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALR-CVSatGEALKAALVRRWFAVLPEVL 473
Cdd:PRK06710 276 YKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRaCIS--GSAPLPVEVQEKFETVTGGK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 474 LVNAYGLTETCDDTNHEVLDRaqdgSRVPlgraiAGVGVHVVDGNLMPVPL--------GATGEIVFSGRCLARGYVNDP 545
Cdd:PRK06710 351 LVEGYGLTESSPVTHSNFLWE----KRVP-----GSIGVPWPDTEAMIMSLetgealppGEIGEIVVKGPQIMKGYWNKP 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 546 IRTALAFTASPLfpgqrlyRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAG---AAE 622
Cdd:PRK06710 422 EETAAVLQDGWL-------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPdpyRGE 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993051 623 SARLVACYSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVdrkelaritggLHRAMTEDERPRPGAER 700
Cdd:PRK06710 495 TVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKI-----------LRRVLIEEEKRKNEDEQ 561
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
184-675 |
7.34e-13 |
|
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: 72.52 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 VHQLIADTAAARPDDVAVV-----AGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGC 258
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRwegedGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 259 YLPVEPHFPLEriAAMVTRSACG-RALTDEVGAAVTDRLGGLVPGLR-----ARGVDEIL---RGG------------HP 317
Cdd:cd05968 143 VVPIFSGFGKE--AAATRLQDAEaKALITADGFTRRGREVNLKEEADkacaqCPTVEKVVvvrHLGndftpakgrdlsYD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 318 SEVPGTPVVAGQLA-----YIYFTSGSTGEPKGVMCEHEGMlnhMLAKIDDLG----VRAGTVVAQTAPQCFDISLWQLL 388
Cdd:cd05968 221 EEKETAGDGAERTEsedplMIIYTSGTTGKPKGTVHVHAGF---PLKAAQDMYfqfdLKPGDLLTWFTDLGWMMGPWLIF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 389 APLITGGTVVIVS-QQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRA--LPALRCVSATGEALKAALVRRW 465
Cdd:cd05968 298 GGLILGATMVLYDgAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAhdLSSLRVLGSTGEPWNPEPWNWL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 466 FAVL--PEVLLVNAYGLTETCDDTNHEVLDRAQDGSrvPLGRAIAGVGVHVVDGNLMPVPlGATGEIVFSGRC--LARGY 541
Cdd:cd05968 378 FETVgkGRNPIINYSGGTEISGGILGNVLIKPIKPS--SFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPWpgMTRGF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 542 VNDPIRTALAFTASplFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVRE-ATVIVAGA 620
Cdd:cd05968 455 WRDEDRYLETYWSR--FDN--VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsAAIGVPHP 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 621 AESARLVACYSAAPSLAPGP-----LVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRK 675
Cdd:cd05968 531 VKGEAIVCFVVLKPGVTPTEalaeeLMERVADELGKPLSPERILFVKDLPKTRNAKVMRR 590
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
328-679 |
1.23e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 70.59 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 328 GQLAYIYFTSGSTGEPKGVMCEHEGMLNH--MLAKIDDLGVRAGTVVAQTAPQCFDiSLWQLLAPLITGGTVVIVSQQAL 405
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNawMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 406 LD---VEQFAAELDRSRVEVAQLVPSYVEVLLghleRRP--RALPALRCVSATGEALKAALVRRwFAVLPEVLLVNAYGL 480
Cdd:cd05944 81 RNpglFDNFWKLVERYRITSLSTVPTVYAALL----QVPvnADISSLRFAMSGAAPLPVELRAR-FEDATGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 481 TETCDDTNHEVLDRAQDGSRVPLGRAIAGVGVHVVDGN---LMPVPLGATGEIVFSGRCLARGYVNDPirtalafTASPL 557
Cdd:cd05944 156 TEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTE-------GNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 558 FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSaapSLA 637
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV---QLK 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502993051 638 PGPLVE-------ALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:cd05944 306 PGAVVEeeellawARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
192-678 |
4.37e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 69.52 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 192 AAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERI 271
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 272 AAMVTRSACGRALTDEVGAAvtdrlgglVPGLRARgvdeilrggHPSEVPGTPVVA---GQLAYIYFTSGSTGEPKGV-- 346
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENT--------FSALTSL---------HLQLVEGAHAVAwqpQRLATMTLTSGSTGLPKAAvh 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 347 -----MCEHEGMLNHMlakiddlgvragtvvaQTAPQC--------FDIS----LWQLLApliTGGTVVIVSQQALLDve 409
Cdd:PRK09029 156 taqahLASAEGVLSLM----------------PFTAQDswllslplFHVSgqgiVWRWLY---AGATLVVRDKQPLEQ-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 410 qfaaelDRSRVEVAQLVPSYVEVLLGHLERRpralpalrcvsatgEALKAALVRRwfAVLPEVLLVNA----------YG 479
Cdd:PRK09029 215 ------ALAGCTHASLVPTQLWRLLDNRSEP--------------LSLKAVLLGG--AAIPVELTEQAeqqgircwcgYG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 480 LTETcddtnhevldraqdGSRVPLGRA--IAGVG-------VHVVDgnlmpvplgatGEIVFSGRCLARGYVNDPIRTal 550
Cdd:PRK09029 273 LTEM--------------ASTVCAKRAdgLAGVGsplpgreVKLVD-----------GEIWLRGASLALGYWRQGQLV-- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 551 aftasPLFPGQRLYRSGDFGRWTpDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-VAGAAESARLVAC 629
Cdd:PRK09029 326 -----PLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVpVADAEFGQRPVAV 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502993051 630 YSAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELA 678
Cdd:PRK09029 400 VESDSEAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALK 448
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
178-740 |
1.95e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 68.66 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 178 ELPDRRVHQLiADTAAARPDDVAVVAGLDQ------LTYRQLDERANQVAHALLADglaaedvvAVVSERAI-------P 244
Cdd:PRK05691 6 ELPLTLVQAL-QRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQAR--------ASFGDRAVllfpsgpD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 245 WLVAVLGVLKAGGCYLPVEP-----HFPLERIAAMVTRSACGRALTDevgAAVTDRLGGLvPGLRARGVDEIL-----RG 314
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTV---ADLRDSLLQM-EELAAANAPELLcvdtlDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 315 GHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGT--VVAQTAPQCFDISL-WQLLAPL 391
Cdd:PRK05691 153 ALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddVIVSWLPLYHDMGLiGGLLQPI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 392 ITGGTVVIVSQQALLDVEQ------------------FAAELDRSRVEvaqlvpsyvEVLLGHLErrpraLPALRCVSAT 453
Cdd:PRK05691 233 FSGVPCVLMSPAYFLERPLrwleaiseyggtisggpdFAYRLCSERVS---------ESALERLD-----LSRWRVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 454 GEALKAALVRRW---FAVL---PEVLLVnAYGLTE--------------TCDDTNHEVL--DRAQDGSRVPL---GRAIA 508
Cdd:PRK05691 299 SEPIRQDSLERFaekFAACgfdPDSFFA-SYGLAEatlfvsggrrgqgiPALELDAEALarNRAEPGTGSVLmscGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 509 GVGVHVVDGN-LMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTAsplFPGQRLYRSGDFGrWTPDGRLEFSGRRDTQ 587
Cdd:PRK05691 378 GHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 588 VKIRGFRVEIGEIEDRLLR-LPGVREATVIVAG-----------AAESARlvacySAAPSLAPGPLVEALARVLPD--YM 653
Cdd:PRK05691 454 LIVRGHNLYPQDIEKTVEReVEVVRKGRVAAFAvnhqgeegigiAAEISR-----SVQKILPPQALIKSIRQAVAEacQE 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 654 VPRDWYWLD--VLPLTGNGKVDRKE------------LARITGGLHRAMTEDERPRPGAERRLAAAWATVLGVApdRVGR 719
Cdd:PRK05691 529 APSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsYALFPALQAVEAAQTAASGDELQARIAAIWCEQLKVE--QVAA 606
|
650 660
....*....|....*....|.
gi 502993051 720 TDDFFASGGSSLSALQLVIEL 740
Cdd:PRK05691 607 DDHFFLLGGNSIAATQVVARL 627
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
324-677 |
3.57e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 67.36 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 324 PVVAGQLAYIYFTSGSTGEPKGVMCEHEgmlnHMLAKIDDLGVRAGTVVAQTAPQC---------FDISLWqllAPLITG 394
Cdd:PRK06060 141 PMGGDALAYATYTSGTTGPPKAAIHRHA----DPLTFVDAMCRKALRLTPEDTGLCsarmyfaygLGNSVW---FPLATG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 395 GTVVIVSqqalLDVEQFAAELDRSRVEVAQL--VPSYVEVLLGHLErrPRALPALRCVSATGEALKAALVRRWFAVLPEV 472
Cdd:PRK06060 214 GSAVINS----APVTPEAAAILSARFGPSVLygVPNFFARVIDSCS--PDSFRSLRCVVSAGEALELGLAERLMEFFGGI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 473 LLVNAYGLTETCDDTNHEVLDRAQDGSrvpLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPirtalaf 552
Cdd:PRK06060 288 PILDGIGSTEVGQTFVSNRVDEWRLGT---LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP------- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 553 taSPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYsA 632
Cdd:PRK06060 358 --DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAF-L 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502993051 633 APSLAPGpLVEALAR--------VLPDYMVPRDWYWLDVLPLTGNGKVDRKEL 677
Cdd:PRK06060 435 VATSGAT-IDGSVMRdlhrgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
207-679 |
5.00e-11 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 66.29 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALTD 286
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 287 EVGAAVTDRlgglvpglrargvdeilrgghPSEVPGTPVVA--GQLAYIYfTSGSTGEPKGVMCEHEGMLNHMLAKIDDL 364
Cdd:cd05939 83 LLDPLLTQS---------------------STEPPSQDDVNfrDKLFYIY-TSGTTGLPKAAVIVHSRYYRIAAGAYYAF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 365 GVRAGTVVAQTAP------------QCfdislwqllapLITGGTVVIVSQqalLDVEQFAAELDRSRVEVAQLVPSYVEV 432
Cdd:cd05939 141 GMRPEDVVYDCLPlyhsaggimgvgQA-----------LLHGSTVVIRKK---FSASNFWDDCVKYNCTIVQYIGEICRY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 433 LLGhleRRPRALPALRCVS-ATGEALKAAL----VRRwFAVlPEVllVNAYGLTE-TCDDTNHevldraqDG-------- 498
Cdd:cd05939 207 LLA---QPPSEEEQKHNVRlAVGNGLRPQIweqfVRR-FGI-PQI--GEFYGATEgNSSLVNI-------DNhvgacgfn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 499 SRVPL--------------GRAIAGvgvhvVDGNLMPVPLGATGEIVfsGRCLAR-------GYVNDPiRTALAFTASPL 557
Cdd:cd05939 273 SRILPsvypirlikvdedtGELIRD-----SDGLCIPCQPGEPGLLV--GKIIQNdplrrfdGYVNEG-ATNKKIARDVF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 558 FPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI---VAGAAESARLVACYSAAP 634
Cdd:cd05939 345 KKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYgveVPGVEGRAGMAAIVDPER 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502993051 635 SLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELAR 679
Cdd:cd05939 425 KVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
331-629 |
7.11e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 65.99 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAP--QCFDISLWQLLaPLITGGTVVIVSQQalLDV 408
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPpfHAYGFNSCTLF-PLLSGVPVVFAYNP--LYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 409 EQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTN 488
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVIT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 489 HEVLDRAQDGSRVplGRAIAGVGVHVV-DGNLMPVPLGATGEIVFSGRCLARGYV-NDPIRTALAFTasplfpGQRLYRS 566
Cdd:PRK06334 343 INTVNSPKHESCV--GMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELG------GETWYVT 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502993051 567 GDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATvivagaaESARLVAC 629
Cdd:PRK06334 415 GDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAD-------HAGPLVVC 470
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
384-680 |
7.61e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.40 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 384 LWQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSrveVAQLVPSYVEVLLghlERRPRALPALRCV----SATGEAL-- 457
Cdd:PRK07445 175 LMQFMRSFLTGGKLVILPYKRLKSGQELPPNPSDF---FLSLVPTQLQRLL---QLRPQWLAQFRTIllggAPAWPSLle 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 458 KAAlvrrwFAVLPevlLVNAYGLTET----CddtnheVLDRAQ--DGSRvPLGRAIAGVGVHVVDGnlmpvplgATGEIV 531
Cdd:PRK07445 249 QAR-----QLQLR---LAPTYGMTETasqiA------TLKPDDflAGNN-SSGQVLPHAQITIPAN--------QTGNIT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 532 FSGRCLARGYVndPirtalaftasPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVR 611
Cdd:PRK07445 306 IQAQSLALGYY--P----------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQ 373
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502993051 612 EATVIvaGAAES---ARLVACYS-AAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARI 680
Cdd:PRK07445 374 DVCVL--GLPDPhwgEVVTAIYVpKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
512-766 |
1.09e-10 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 64.00 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 512 VHVVDGNLMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFP---GQRLYRSGDFGRWTPDGRLEFSGRRDTQV 588
Cdd:COG3433 24 IVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPvpyPAQPGRQADDLRLLLRRGLGPGGGLERLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 589 KIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESARLVACYSAAPSLAPGPLVEALAR----VLPDYMVPRDWYWLDVL 664
Cdd:COG3433 104 QQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALaaldKVPPDVVAASAVVALDA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 665 PLTGNGKVDRK---ELARITGGLHRAMTEDERPRPGAERRLAAAWATVLGVAPDRVGRTDDFFASGGSSLSALQLVIELD 741
Cdd:COG3433 184 LLLLALKVVARaapALAAAEALLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWR 263
|
250 260
....*....|....*....|....*...
gi 502993051 742 RA---VSLGDVTAHPVLADLAGVLGTGA 766
Cdd:COG3433 264 KAgldVSFADLAEHPTLAAWWALLAAAQ 291
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
204-611 |
4.02e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.48 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 204 GLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVepHFPLERIAAMVTRSACGRA 283
Cdd:PRK07768 26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML--HQPTPRTDLAVWAEDTLRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 284 LtDEVGAA---VTDRLGGLVPGLRARGVDEILRGGHPSEVPGTPVVAGQ--LAYIYFTSGSTGEPKGVMCEHEGMLNHML 358
Cdd:PRK07768 104 I-GMIGAKavvVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDPVETGEddLALMQLTSGSTGSPKAVQITHGNLYANAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 359 AKIDDLGVRAGT-VVAQTAPQCFDISLWQLLA-PLITGGTVVIVSQQALL-DVEQFAAELDRSRVEVAqLVPSYVEVLLG 435
Cdd:PRK07768 183 AMFVAAEFDVETdVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPMDFLrDPLLWAELISKYRGTMT-AAPNFAYALLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLERRPRA-----LPALRCVSATGEALKAALVRRWFAV-----LPEVLLVNAYGLTET--------CD-----DTNH--- 489
Cdd:PRK07768 262 RRLRRQAKpgafdLSSLRFALNGAEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEAtlavsfspCGaglvvDEVDadl 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 490 -EVLDRAQDG------SRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYVndpirTALAFTasPLFPGQR 562
Cdd:PRK07768 342 lAALRRAVPAtkgntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFI--PAQDADG 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502993051 563 LYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVR 611
Cdd:PRK07768 415 WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVR 463
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
176-683 |
5.19e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 63.08 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 176 PRELPdrrVHQLIADTAAARPDDVAVVAGL--DQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVL 253
Cdd:PLN02246 20 PNHLP---LHDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGAS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 254 KAGGCYLPVEPHFPLERIAAMVTRSACGRALTDevgAAVTDRLGGLVPGlraRGVDEILRGGHP--------------SE 319
Cdd:PLN02246 97 RRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ---SCYVDKLKGLAED---DGVTVVTIDDPPegclhfseltqadeNE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 320 VPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKID----DLGVRAGTVVAQTAPQcFDI-SLWQ-LLAPLIT 393
Cdd:PLN02246 171 LPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPM-FHIySLNSvLLCGLRV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 394 GGTVVIVSQ---QALLDVEQfaaeldRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALVRRWFAVLP 470
Cdd:PLN02246 250 GAAILIMPKfeiGALLELIQ------RHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 471 EVLLVNAYGLTET------CDDTNHEVLDrAQDGSrvpLGRAIAGVGVHVVDGNL-MPVPLGATGEIVFSGRCLARGYVN 543
Cdd:PLN02246 324 NAVLGQGYGMTEAgpvlamCLAFAKEPFP-VKSGS---CGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 544 DPIRTALAFTAsplfpgQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VA 618
Cdd:PLN02246 400 DPEATANTIDK------DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVpmkdeVA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 619 GAAESARLVAcySAAPSLAPGPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL-ARITGG 683
Cdd:PLN02246 474 GEVPVAFVVR--SNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLrAKLAAG 537
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
327-679 |
5.94e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 62.89 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 327 AGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQL-LAPLITGgtvvivSQQAL 405
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAG------MNQYL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 406 LDVEQF-------------------------------------AAELDRSRVEV-----AQLVPSYVEVLLGHLE----R 439
Cdd:cd05908 179 MPTRLFirrpilwlkkasehkativsspnfgykyflktlkpekANDWDLSSIRMilngaEPIDYELCHEFLDHMSkyglK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 440 RPRALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNHEVLdraqdgSRVPLGRAIAGVGVHVVDGNL 519
Cdd:cd05908 259 RNAILPVYGLAEASVGASLPKAQSPFKTITLGRRHVTHGEPEPEVDKKDSECL------TFVEVGKPIDETDIRICDEDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 520 MPVPLGATGEIVFSGRCLARGYVNDPIRTALAFTASPLFpgqrlyRSGDFGrWTPDGRLEFSGRRDTQVKIRGFRVEIGE 599
Cdd:cd05908 333 KILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHD 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 600 IEDRLLRLPGVREATVIVAGAAES---ARLVACY----SAAPSLApgPLVEALARVLPDYmvpRDWYWLDVLPL-----T 667
Cdd:cd05908 406 IERIAEELEGVELGRVVACGVNNSntrNEEIFCFiehrKSEDDFY--PLGKKIKKHLNKR---GGWQINEVLPIrripkT 480
|
410
....*....|..
gi 502993051 668 GNGKVDRKELAR 679
Cdd:cd05908 481 TSGKVKRYELAQ 492
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
188-616 |
1.53e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 61.89 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFP 267
Cdd:PRK08162 24 LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 268 LERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLRARGVD------------------EILRGGHPS---EVPGTPVV 326
Cdd:PRK08162 104 AASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDvddpeypggrfigaldyeAFLASGDPDfawTLPADEWD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 327 AGQLAYiyfTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQ------CFDislWQLLApliTGGTVVI- 399
Cdd:PRK08162 184 AIALNY---TSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMfhcngwCFP---WTVAA---RAGTNVCl 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 400 --VSQQALLD------VEQFAAeldrsrvevAQLVPSyvevLLGHLERRPRALPALRCVSATGEALKAAlvrrwfAVLPE 471
Cdd:PRK08162 255 rkVDPKLIFDlirehgVTHYCG---------APIVLS----ALINAPAEWRAGIDHPVHAMVAGAAPPA------AVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 472 VL-----LVNAYGLTET------C------DDTNHEvlDRAQ----DGSRVPLGRAIAgvgvhVVDGNLM-PVPL-GAT- 527
Cdd:PRK08162 316 MEeigfdLTHVYGLTETygpatvCawqpewDALPLD--ERAQlkarQGVRYPLQEGVT-----VLDPDTMqPVPAdGETi 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 528 GEIVFSGRCLARGYVNDPIRTALAFTASplfpgqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRL 607
Cdd:PRK08162 389 GEIMFRGNIVMKGYLKNPKATEEAFAGG-------WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRH 461
|
....*....
gi 502993051 608 PGVREATVI 616
Cdd:PRK08162 462 PAVLVAAVV 470
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
269-615 |
3.48e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 60.46 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 269 ERIAAMVTRSACGRALTDEVGAAVTDrlgGLVPGLRARGVD-----EILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEP 343
Cdd:PRK07867 91 AALARDIAHADCQLVLTESAHAELLD---GLDPGVRVINVDspawaDELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 344 KGVMCEHEGML--NHMLAkiDDLGVRAGTVVAQTAPQCFDISLWQLLAP-LITGGTVVIvsqQALLDVEQFAAELDRSRV 420
Cdd:PRK07867 168 KAVRCTHRKVAsaGVMLA--QRFGLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIAL---RRKFSASGFLPDVRRYGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 421 EVAQLVPSYVEVLLGHLERRPRALPALRCVSATgEALKAALVRrwFAVLPEVLLVNAYGLTET------CDDTNHEVLDR 494
Cdd:PRK07867 243 TYANYVGKPLSYVLATPERPDDADNPLRIVYGN-EGAPGDIAR--FARRFGCVVVDGFGSTEGgvaitrTPDTPPGALGP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 495 AQDGSRV--PLGRAIAGVGVHVVDGNLMPVPlgATGEIV-FSGRCLARGYVNDPIRTAlaftasplfpgQRL----YRSG 567
Cdd:PRK07867 320 LPPGVAIvdPDTGTECPPAEDADGRLLNADE--AIGELVnTAGPGGFEGYYNDPEADA-----------ERMrggvYWSG 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502993051 568 DFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATV 615
Cdd:PRK07867 387 DLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAV 434
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
269-699 |
3.83e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 60.43 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 269 ERIAAMVTRSACGRALTDEVGAAVTDRLGglVPGLRARGVDEI----LRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPK 344
Cdd:PRK13388 89 AALAADIRRADCQLLVTDAEHRPLLDGLD--LPGVRVLDVDTPayaeLVAAAGALTPHREVDAMDPFMLIFTSGTTGAPK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 345 GVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAP-LITGGTVVIVSQQA----LLDVEQFAAELdrsr 419
Cdd:PRK13388 167 AVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPAKFSasgfLDDVRRYGATY---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 420 vevaqlvPSYVEVLLGHL----ERRPRALPALRCVSAT--GEALKAALVRRwFAVLpevlLVNAYGLTETC------DDT 487
Cdd:PRK13388 243 -------FNYVGKPLAYIlatpERPDDADNPLRVAFGNeaSPRDIAEFSRR-FGCQ----VEDGYGSSEGAvivvrePGT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 488 NHEVLDRAQDGSRV--PLGRAIAGVGVHVVDGNLMPvPLGATGEIV-FSGRCLARGYVNDPIRTAlaftasplfpgQRL- 563
Cdd:PRK13388 311 PPGSIGRGAPGVAIynPETLTECAVARFDAHGALLN-ADEAIGELVnTAGAGFFEGYYNNPEATA-----------ERMr 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 564 ---YRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVI-----VAGAAESARLVAcySAAPS 635
Cdd:PRK13388 379 hgmYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYavpdeRVGDQVMAALVL--RDGAT 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 636 LAPGPLVEALA--RVLPDYMVPRDWYWLDVLPLTGNGKVDRKEL--------------ARITGGLHRAMTEDERPRPGAE 699
Cdd:PRK13388 457 FDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELiaqgwatgdpvtlwVRRGGPAYRLMSEPAKAALAAE 536
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
187-351 |
4.32e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 60.34 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 187 LIADTAAARPDDVAVV--------AGL-DQLTYRQLDERANQVAHALLADGlAAEDVVAVVSERAIPWLVAVLGVLKAGG 257
Cdd:PRK05850 6 LLRERASLQPDDAAFTfidyeqdpAGVaETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 258 CYLPV-EPHFPL--ERIAAMVTRSACGRALT-----DEVGAAVTDRLGGLVPGLRArgVDeILRGGHPSEVPGTPVVAGQ 329
Cdd:PRK05850 85 IAVPLsVPQGGAhdERVSAVLRDTSPSVVLTtsavvDDVTEYVAPQPGQSAPPVIE--VD-LLDLDSPRGSDARPRDLPS 161
|
170 180
....*....|....*....|..
gi 502993051 330 LAYIYFTSGSTGEPKGVMCEHE 351
Cdd:PRK05850 162 TAYLQYTSGSTRTPAGVMVSHR 183
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
142-354 |
4.84e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 60.28 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 142 ALRLAAADPDAEHAGQcllGAAELRhQLTAFSGAPRELPDRRVHQliadtAAARPDDVAVV-----AGLDQLTYRQLDER 216
Cdd:PRK08180 8 PVAFAPPAVEVERRAD---GTIYLR-SAEPLGDYPRRLTDRLVHW-----AQEAPDRVFLAergadGGWRRLTYAEALER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 217 ANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPL-----ERIAAMVTR-----------SAC 280
Cdd:PRK08180 79 VRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLELltpglvfaddgAAF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 281 GRALTDEVGAAVTD-RLGGLVPGLRARGVDEILRGGHPSEVPGT--PVVAGQLAYIYFTSGSTGEPKGVMCEHeGML 354
Cdd:PRK08180 159 ARALAAVVPADVEVvAVRGAVPGRAATPFAALLATPPTAAVDAAhaAVGPDTIAKFLFTSGSTGLPKAVINTH-RML 234
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
196-616 |
6.04e-09 |
|
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: 59.98 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 196 PDDVAVVAG----LDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGG----C--------- 258
Cdd:cd05943 83 DDPAAIYAAedgeRTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwssCspdfgvpgv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 259 ---YLPVEP---------------HFPLERIAAMVtRSACGRALTDEVGAAVTDRLGGLVPGLRARGVDEILRGGHPSEV 320
Cdd:cd05943 163 ldrFGQIEPkvlfavdaytyngkrHDVREKVAELV-KGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 321 PGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGML-NHMLAKIDDLGVRAGtvvaqtapqcfDISLWQ----------LLA 389
Cdd:cd05943 242 EFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLlQHLKEHILHCDLRPG-----------DRLFYYttcgwmmwnwLVS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 390 PLITGGTVVIV-------SQQALLDVeqfaaeLDRSRVEVAQLVPSYVEVLL--GHLERRPRALPALRCVSATGEALKA- 459
Cdd:cd05943 311 GLAVGATIVLYdgspfypDTNALWDL------ADEEGITVFGTSAKYLDALEkaGLKPAETHDLSSLRTILSTGSPLKPe 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 460 --ALVRRwfAVLPEVLLVNAYGLTETCDDTnhevldrAQDGSRVPLGR-----AIAGVGVHVVDGNLMPVPlGATGEIV- 531
Cdd:cd05943 385 sfDYVYD--HIKPDVLLASISGGTDIISCF-------VGGNPLLPVYRgeiqcRGLGMAVEAFDEEGKPVW-GEKGELVc 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 532 ---FSGRCLarGYVNDPIRTAL--AFTASplFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLR 606
Cdd:cd05943 455 tkpFPSMPV--GFWNDPDGSRYraAYFAK--YPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEK 528
|
490
....*....|
gi 502993051 607 LPGVREATVI 616
Cdd:cd05943 529 IPEVEDSLVV 538
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
328-649 |
8.34e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 59.01 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 328 GQLAYIYFTSGSTGEPKGVM-CEHE-GMLNHMLAKI-DDLGVRAGTVVaqtapQ-CFDISLWqllapliTGG-------- 395
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVVGyTRKDlDRWAELFARSlRAAGVRPGDRV-----QnAFGYGLF-------TGGlglhygae 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 396 ----TVVIVS-----QQAlldveQFAAELdRSRVEVAqlVPSYVEVLLGHLERR---PRALPaLRCVSATGEALKAALvR 463
Cdd:COG1541 151 rlgaTVIPAGggnteRQL-----RLMQDF-GPTVLVG--TPSYLLYLAEVAEEEgidPRDLS-LKKGIFGGEPWSEEM-R 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 464 RWFAVLPEVLLVNAYGLTET-------CddtnhevldRAQDGSRVPLGRAIagvgVHVVD-GNLMPVPLGATGEIVFsgr 535
Cdd:COG1541 221 KEIEERWGIKAYDIYGLTEVgpgvayeC---------EAQDGLHIWEDHFL----VEIIDpETGEPVPEGEEGELVV--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 536 clargyvndpirTALAFTASPLFpgqRlYRSGDFGRWTPD----GR-----LEFSGRRDTQVKIRGFRVEIGEIEDRLLR 606
Cdd:COG1541 285 ------------TTLTKEAMPLI---R-YRTGDLTRLLPEpcpcGRthpriGRILGRADDMLIIRGVNVFPSQIEEVLLR 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 502993051 607 LPGVR-EATVIVAGAAESARLVACYSAAPSLAPGPLVEALARVL 649
Cdd:COG1541 349 IPEVGpEYQIVVDREGGLDELTVRVELAPGASLEALAEAIAAAL 392
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
309-616 |
1.18e-08 |
|
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: 58.87 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 309 DEILRGGHPseVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEG---MLNHMLAKIDDL--------GVRAGTVVAQTap 377
Cdd:cd05967 213 SELLAKAEP--VDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGhavALNWSMRNIYGIkpgdvwwaASDVGWVVGHS-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 378 qcfdislWQLLAPLITGGTVVIVSQQALL--DVEQFAAELDRSRVEVAQLVPSYVEVL----LGHLERRPRALPALRCVS 451
Cdd:cd05967 289 -------YIVYGPLLHGATTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 452 ATGEALKAALVRrWFAVLPEVLLVNAYGLTET--CDDTNHevldRAQDGSRVPLG---RAIAGVGVHVVDGNLMPVPLGA 526
Cdd:cd05967 362 LAGERLDPPTLE-WAENTLGVPVIDHWWQTETgwPITANP----VGLEPLPIKAGspgKPVPGYQVQVLDEDGEPVGPNE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 527 TGEIVFSG----RCLARGYVNDPIRTALAFTaspLFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIED 602
Cdd:cd05967 437 LGNIVIKLplppGCLLTLWKNDERFKKLYLS---KFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
330
....*....|....
gi 502993051 603 RLLRLPGVREATVI 616
Cdd:cd05967 512 SVLSHPAVAECAVV 525
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
700-757 |
2.47e-08 |
|
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: 51.41 E-value: 2.47e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993051 700 RRLAAAWATVLGVAPDRVGRTDDFFASGGSSLSALQLVIELDRA----VSLGDVTAHPVLAD 757
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfgveIPPSDLFEHPTLAE 62
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
216-679 |
4.67e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.70 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 216 RANQVAHALLADGLAAedVVAVVSERAIPWLVAVLGVLKAGGCY--LPVEPHFPLERIAAMVTRSACGRALTDEV--GAA 291
Cdd:PRK05851 40 RAENVAARLLDRDRPG--AVGLVGEPTVELVAAIQGAWLAGAAVsiLPGPVRGADDGRWADATLTRFAGIGVRTVlsHGS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 292 VTDRLGGLVPGLRARGVDEIlrGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTV 371
Cdd:PRK05851 118 HLERLRAVDSSVTVHDLATA--AHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 372 VAQT-APQCFDISLWQLLAPLITGGTVVIVSQQAlldveqFAAE-------LDRSRVEVAQlVPSYVEVLLGHLERRPRA 443
Cdd:PRK05851 196 VGCSwLPLYHDMGLAFLLTAALAGAPLWLAPTTA------FSASpfrwlswLSDSRATLTA-APNFAYNLIGKYARRVSD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 444 --LPALRCVSATGEALKAALVRRWFAVLPEV-----LLVNAYGLTE-TCDDTN---------HEVLDRAQDGSR--VPLG 504
Cdd:PRK05851 269 vdLGALRVALNGGEPVDCDGFERFATAMAPFgfdagAAAPSYGLAEsTCAVTVpvpgiglrvDEVTTDDGSGARrhAVLG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 505 RAIAGVGVHVVDGNlMPVPLGA--TGEIVFSGRCLARGYVNDPirtalaftasPLFPGQrLYRSGDFGRWTpDGRLEFSG 582
Cdd:PRK05851 349 NPIPGMEVRISPGD-GAAGVAGreIGEIEIRGASMMSGYLGQA----------PIDPDD-WFPTGDLGYLV-DGGLVVCG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 583 RRDTQVKIRGFRVEIGEIEDRLLRLPGVREATVIVAGAAESA---RLVACYSAAPSLAPGPLVEALARVLPDY-MVPRDW 658
Cdd:PRK05851 416 RAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSarpGLVIAAEFRGPDEAGARSEVVQRVASECgVVPSDV 495
|
490 500
....*....|....*....|...
gi 502993051 659 YWLD--VLPLTGNGKVDRKELAR 679
Cdd:PRK05851 496 VFVApgSLPRTSSGKLRRLAVKR 518
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
188-649 |
6.04e-08 |
|
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: 56.67 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 188 IADTAAARPDDVAVVA-----GLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPV 262
Cdd:cd05921 1 LAHWARQAPDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 263 EPHFPLERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPGLRARGVDEILRGGHP--------SEVPGTPVVAG------ 328
Cdd:cd05921 81 SPAYSLMSQDLAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVagrgaisfAELAATPPTAAvdaafa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 329 -----QLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVvaqtaPQCFDISLWQ--------LLAPLITGG 395
Cdd:cd05921 161 avgpdTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNhtfggnhnFNLVLYNGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 396 TVVIVSQQALldVEQFAAELDRSRvEVAQL----VPSYVEVLLGHLER----RPRALPALRCVSATGEALKAALVRRWFA 467
Cdd:cd05921 236 TLYIDDGKPM--PGGFEETLRNLR-EISPTvyfnVPAGWEMLVAALEKdealRRRFFKRLKLMFYAGAGLSQDVWDRLQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 468 VLPE-----VLLVNAYGLTET---CDDTnHEVLDRAQDgsrvpLGRAIAGVGVHVVdgnlmpvPLGATGEIVFSGRCLAR 539
Cdd:cd05921 313 LAVAtvgerIPMMAGLGATETaptATFT-HWPTERSGL-----IGLPAPGTELKLV-------PSGGKYEVRVKGPNVTP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 540 GYVNDPIRTALAFTAsplfpgQRLYRSGDFGRWT----PDGRLEFSGRRDTQVKIR-GFRVEIGEIEDRLLRL--PGVRE 612
Cdd:cd05921 380 GYWRQPELTAQAFDE------EGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502993051 613 ATVIVAGAAESARLV-----AC--------YSAAPSLAPGPLVEALARVL 649
Cdd:cd05921 454 AVVAGEDRAEVGALVfpdllACrrlvglqeASDAEVLRHAKVRAAFRDRL 503
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
694-762 |
9.15e-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: 50.24 E-value: 9.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502993051 694 PRPGAERRLAAAWATVLGVAPDRVGRTDDFFAS-GGSSLSALQLVIELDRA----VSLGDVTAHPVLADLAGVL 762
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEDlGLDSLDAVELIAALEEEfgieLPDTELFEYPTVADLADYL 75
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
207-679 |
1.96e-07 |
|
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: 54.74 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAHALLADGLAAEDVVAVVSERaIPWLVAV-LGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRALT 285
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFN-HFRHLEAyFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 DEVGAAVTDRLGGLVPGL--------RARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGM-LNH 356
Cdd:cd05915 103 DPNLLPLVEAIRGELKTVqhfvvmdeKAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALvLHS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 357 M-LAKIDDLGVRAGTVVAQTAPQcFDISLWQLLAPLITGGTVVIVSQQALLDvEQFAAELDRSRVEVAQLVPSYVEVLLG 435
Cdd:cd05915 183 LaASLVDGTALSEKDVVLPVVPM-FHVNAWCLPYAATLVGAKQVLPGPRLDP-ASLVELFDGEGVTFTAGVPTVWLALAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 436 HLERRPRALPALRCVSATGEALKAALVRR----WFAVLPEVLLVNAYGLTETC-------DDTNHEVLD-RAQDGSRVpl 503
Cdd:cd05915 261 YLESTGHRLKTLRRLVVGGSAAPRSLIARfermGVEVRQGYGLTETSPVVVQNfvkshleSLSEEEKLTlKAKTGLPI-- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 504 graiAGVGVHVVDGNLMPVPL-GATGEIV-FSGRCLARGYVNDPIRT-ALAFTASplfpgqrLYRSGDFGRWTPDGRLEF 580
Cdd:cd05915 339 ----PLVRLRVADEEGRPVPKdGKALGEVqLKGPWITGGYYGNEEATrSALTPDG-------FFRTGDIAVWDEEGYVEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 581 SGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATViVAGAAESARLVACYSAAPSLAPG---PLVEALARVLPDY-MVPR 656
Cdd:cd05915 408 KDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAV-VAIPHPKWQERPLAVVVPRGEKPtpeELNEHLLKAGFAKwQLPD 486
|
490 500
....*....|....*....|...
gi 502993051 657 DWYWLDVLPLTGNGKVdRKELAR 679
Cdd:cd05915 487 AYVFAEEIPRTSAGKF-LKRALR 508
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
205-369 |
3.79e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.86 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 205 LDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGcyLPVEPHFP---------LERIAAMV 275
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL--VPVPLPLPmgfggresyIAQLRGML 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 276 TRSACGRALT-DEVGAAVTDRLGGLVPGLRARGVDEILRGGHPSEVPgtPVVAGQLAYIYFTSGSTGEPKGVMCEH-EGM 353
Cdd:PRK09192 125 ASAQPAAIITpDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALP--RPTPDDIAYLQYSSGSTRFPRGVIITHrALM 202
|
170
....*....|....*.
gi 502993051 354 LNHMLAKIDDLGVRAG 369
Cdd:PRK09192 203 ANLRAISHDGLKVRPG 218
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
206-657 |
4.04e-07 |
|
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: 54.00 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 206 DQLTYRQLDERANQVAHALLADG-LAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMV--TRSACGR 282
Cdd:cd17632 66 ETITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILaeTEPRLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 283 ALTDEVGAAVTDRLGGLVPGL------------------RARG--------------VDEILRGGHPSEVPGTPVVAGQL 330
Cdd:cd17632 146 VSAEHLDLAVEAVLEGGTPPRlvvfdhrpevdahraaleSARErlaavgipvttltlIAVRGRDLPPAPLFRPEPDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 331 AYIYFTSGSTGEPKGVMCEHEGM-------------------------LNHMLAKIDDLGVRAGTVVAQTAPQCFDISLW 385
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVatfwlkvssiqdirppasitlnfmpMSHIAGRISLYGTLARGGTAYFAAASDMSTLF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 386 QLLApLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVllgHLERRPRALPALRCVSATGEALKAALVRRW 465
Cdd:cd17632 306 DDLA-LVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERV---KAELRERVLGGRLLAAVCGSAPLSAEMKAF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 466 FAVLPEVLLVNAYGLTETCDDTNHEVLDRAQdgsrvplgraiagvgvhVVDGNLMPVP-LG--------ATGEIVFSGRC 536
Cdd:cd17632 382 MESLLDLDLHDGYGSTEAGAVILDGVIVRPP-----------------VLDYKLVDVPeLGyfrtdrphPRGELLVKTDT 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 537 LARGYVNDPIRTALAFTAsplfpgQRLYRSGD-FGRWTPDgRLEFSGRRDTQVKI-RGFRVEIGEIEDRLLRLPGVREat 614
Cdd:cd17632 445 LFPGYYKRPEVTAEVFDE------DGFYRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQ-- 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 615 VIVAGAAESARLVACYSAAP--------SLAPGPLVEALARV-----LPDYMVPRD 657
Cdd:cd17632 516 IFVYGNSERAYLLAVVVPTQdalagedtARLRAALAESLQRIareagLQSYEIPRD 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
208-592 |
4.26e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAhALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPV-EPHFP--LERIAAMVTRSACGRAL 284
Cdd:PRK07769 56 LTWSQFGARNRAVG-ARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAIL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 285 T-DEVGAAVTDRLGGLVPGLRAR--GVDEIlrgghPSEVPGT--PVVAGQ--LAYIYFTSGSTGEPKGVMCEHEGMLNHM 357
Cdd:PRK07769 135 TtTDSAEGVRKFFRARPAKERPRviAVDAV-----PDEVGATwvPPEANEdtIAYLQYTSGSTRIPAGVQITHLNLPTNV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 358 LAKIDDLGVRAGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLD-----VEQFAAELDrSRVEVAQLVPSYVev 432
Cdd:PRK07769 210 LQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRrpgrwIRELARKPG-GTGGTFSAAPNFA-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 433 lLGHLERR--PRA------LPALRCVSATGEALKAALVRRWFAV-----LPEVLLVNAYGLTE-------TCDDTNHEV- 491
Cdd:PRK07769 287 -FEHAAARglPKDgeppldLSNVKGLLNGSEPVSPASMRKFNEAfapygLPPTAIKPSYGMAEatlfvstTPMDEEPTVi 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 492 -LDRAQDGS----RVPLG--RAIAGVGVH---------VVDGN-LMPVPLGATGEIVFSGRCLARGYVNDPIRTALAFT- 553
Cdd:PRK07769 366 yVDRDELNAgrfvEVPADapNAVAQVSAGkvgvsewavIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQn 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502993051 554 --ASPLFP--------GQRLYRSGDFGRWTpDGRLEFSGRRDTQVKIRG 592
Cdd:PRK07769 446 ilKSRLSEshaegapdDALWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
774-1008 |
5.43e-07 |
|
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: 51.54 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 774 HRLTPPGRRTLVCFPYAGGNAVTYVPLAGELAaEGWAVYGVEPPGR---DGNEAPVSVPELAELVAGELAALDAGPLTLW 850
Cdd:COG0596 16 YREAGPDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHgrsDKPAGGYTLDDLADDLAALLDALGLERVVLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 851 GHSTGVAAALATARLLRSRghdVRRVLLGAQLpgdsgarRAQAAEVTALPDEAVvtalvesgrpelaevgDAHRRLLADA 930
Cdd:COG0596 95 GHSMGGMVALELAARHPER---VAGLVLVDEV-------LAALAEPLRRPGLAP----------------EALAALLRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993051 931 YRHDVAaacgylaealDAGDRLDVPVTVVLAADDvPDDLPGDPWDWSRLAGDVRVVELPDGGHYFAASRPASVARVIA 1008
Cdd:COG0596 149 ARTDLR----------ERLARITVPTLVIWGEKD-PIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALR 215
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
599-671 |
6.82e-07 |
|
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: 47.54 E-value: 6.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 599 EIEDRLLRLPGVREATVI-VAGAAESARLVACYSAAPSLAPGP--LVEALARVLPDYMVPRDWYWLDVLPLTGNGK 671
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVgVPDELKGEAPVAFVVLKPGVELLEeeLVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
208-377 |
9.43e-07 |
|
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: 52.68 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHfpLERIAAMVTRSACG-RALT 285
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTN--IRSKSLLHCFRCCGaKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 deVGAAVTDRLGGLVPGLRARGVdEILRGGHPSEVPGT-------------PVVAGQLA---------YIYfTSGSTGEP 343
Cdd:cd05938 84 --VAPELQEAVEEVLPALRADGV-SVWYLSHTSNTEGVislldkvdaasdePVPASLRAhvtikspalYIY-TSGTTGLP 159
|
170 180 190
....*....|....*....|....*....|....
gi 502993051 344 KGVMCEHEGMLnHMLAKIDDLGVRAGTVVAQTAP 377
Cdd:cd05938 160 KAARISHLRVL-QCSGFLSLCGVTADDVIYITLP 192
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
208-680 |
1.29e-06 |
|
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: 52.18 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGLAAEDVVAV----VSERAIPWLV-----AVLGVLKAGgcylpvephFPLERIAAMVTRS 278
Cdd:cd05966 85 ITYRELLREVCRFANVLKSLGVKKGDRVAIympmIPELVIAMLAcarigAVHSVVFAG---------FSAESLADRINDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 279 AC------------GR--ALTDEVGAA-----------VTDRLGGLVPGLRARGVD-EILRGGHPSEVPGTPVVAGQLAY 332
Cdd:cd05966 156 QCklvitadggyrgGKviPLKEIVDEAlekcpsvekvlVVKRTGGEVPMTEGRDLWwHDLMAKQSPECEPEWMDSEDPLF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 333 IYFTSGSTGEPKGVMCEHEGMLNHMLAKID---DLgvRAGTVVAQTApqcfDISlW------QLLAPLITGGTVVIV-SQ 402
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGYLLYAATTFKyvfDY--HPDDIYWCTA----DIG-WitghsyIVYGPLANGATTVMFeGT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 403 QALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRA--LPALRCVSATGEALKAAlVRRWFAvlpEVL------L 474
Cdd:cd05966 309 PTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKhdLSSLRVLGSVGEPINPE-AWMWYY---EVIgkercpI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 475 VNAYGLTETcddtnhevldraqdGSRV--PLGRAIA-----------GVGVHVVDGNLMPVPLGATGEIVFS----GrcL 537
Cdd:cd05966 385 VDTWWQTET--------------GGIMitPLPGATPlkpgsatrpffGIEPAILDEEGNEVEGEVEGYLVIKrpwpG--M 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 538 ARGYVNDPIRtalaF--TASPLFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVREATV 615
Cdd:cd05966 449 ARTIYGDHER----YedTYFSKFPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAV 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993051 616 I-----VAGAAESARLVACYSAAPSLAP-GPLVEALARVLPDYMVPRDWYWLDVLPLTGNGKVDRKELARI 680
Cdd:cd05966 523 VgrphdIKGEAIYAFVTLKDGEEPSDELrKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
522-678 |
1.63e-06 |
|
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: 51.66 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 522 VPLGATGEIVF----SGRCLARGYVNDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEI 597
Cdd:cd05937 294 APVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVST 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 598 GEIEDRLLRLPGVREATVI---VAGAAESARLVACYSAAPSLAPGP----LVEALARV-LPDYMVPRDWYWLDVLPLTGN 669
Cdd:cd05937 374 TEVADVLGAHPDIAEANVYgvkVPGHDGRAGCAAITLEESSAVPTEftksLLASLARKnLPSYAVPLFLRLTEEVATTDN 453
|
....*....
gi 502993051 670 GKVDRKELA 678
Cdd:cd05937 454 HKQQKGVLR 462
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
208-578 |
2.72e-06 |
|
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: 51.06 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERANQVAHALLADGL--AAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSacgralt 285
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 286 dEVGAAVTDrlgglvPGLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGM------------ 353
Cdd:cd05927 79 -EISIVFCD------AGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIvsnvagvfkile 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 354 ----------------LNHML------------AKI-----------DDLGVRAGTVVAqTAPQCFDISLWQLLAPLITG 394
Cdd:cd05927 152 ilnkinptdvyisylpLAHIFervvealflyhgAKIgfysgdirlllDDIKALKPTVFP-GVPRVLNRIYDKIFNKVQAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 395 GTVvivsQQALLDveqFAAELDRSRVEVAQLVPS-YVEVLLghLERRPRAL-PALRcVSATGEALKAALVRRWFAVLPEV 472
Cdd:cd05927 231 GPL----KRKLFN---FALNYKLAELRSGVVRASpFWDKLV--FNKIKQALgGNVR-LMLTGSAPLSPEVLEFLRVALGC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 473 LLVNAYGLTETCDDTnheVLDRAQDGSRVPLGRAIAGVGVHVVDgnlmpVP-LG-------ATGEIVFSGRCLARGYVND 544
Cdd:cd05927 301 PVLEGYGQTECTAGA---TLTLPGDTSVGHVGGPLPCAEVKLVD-----VPeMNydakdpnPRGEVCIRGPNVFSGYYKD 372
|
410 420 430
....*....|....*....|....*....|....
gi 502993051 545 PIRTALAFTASPLFpgqrlyRSGDFGRWTPDGRL 578
Cdd:cd05927 373 PEKTAEALDEDGWL------HTGDIGEWLPNGTL 400
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
783-995 |
6.08e-06 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 48.65 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 783 TLVCFPYAGGNAVTYVPLAGELAAEGWAVYGVEPPGRDGNEAP-----VSVPELAELVAGELAALDAGPLTLWGHSTGVA 857
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPkaqddYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 858 AALATARLLRSRghdVRR-VLLGA-------------QLPGDSGARRAQAAEVTALPDEAVVTALVESGRPELaEVGDAH 923
Cdd:pfam00561 82 IALAYAAKYPDR---VKAlVLLGAldppheldeadrfILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRL-RLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 924 RRLLADAYRHDVAAACGYLAEALDA------------GDRLDVPVTVVLAADDVPDDlPGDPWDWSRLAGDVRVVELPDG 991
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVTGALLFietwstelrakfLGRLDEPTLIIWGDQDPLVP-PQALEKLAQLFPNARLVVIPDA 236
|
....
gi 502993051 992 GHYF 995
Cdd:pfam00561 237 GHFA 240
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
205-357 |
1.16e-05 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 49.27 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 205 LDQLTYRQLDERANQVAHALLAD-GLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPVEPHFPLERIAAMVTRSACGRA 283
Cdd:cd05905 12 ATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 284 LTDEVGAAVTDRLGGLVP--GLRARG---------VDEILRGGHPSE--VPGTPVVAGQLAYIYFTSGSTGEPKGVMCEH 350
Cdd:cd05905 92 LTVEACLKGLPKKLLKSKtaAEIAKKkgwpkildfVKIPKSKRSKLKkwGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSH 171
|
....*..
gi 502993051 351 EGMLNHM 357
Cdd:cd05905 172 SSLLAHC 178
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
64-609 |
1.40e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.49 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 64 DGRPRVVDLGHRTW-RELIAHVAGAPAVAARCDTVVGEGELGGDAIVHIGLDGDALVVRCRREWVDDAYAARIADYHRTA 142
Cdd:COG3321 855 GRGRRRVPLPTYPFqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 143 LRLAAADPDAEHAGQCLLGAAELRHQLTAFSGAPRELPDRRVHQLIADTAAARPDDVAVVAGLDQLTYRQLDERANQVAH 222
Cdd:COG3321 935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAA 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 223 ALLADGLAAEDVVAVVSERAIPWLVAVLGVLkaggcylpVEPHFPLERIAAMVTRSACGRALTDEVGAAVTDRLGGLVPG 302
Cdd:COG3321 1015 AAAAAALLALAALLAAAAAALAAAAAAAAAA--------AALAALAAAAAAAAALALALAALLLLAALAELALAAAALAL 1086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 303 LRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLNHMLAKIDDLGVRAGTVVAQTAPQcfdi 382
Cdd:COG3321 1087 AAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAA---- 1162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 383 slwQLLAPLITGGTVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVEVLLGHLERRPRALPALRCVSATGEALKAALV 462
Cdd:COG3321 1163 ---LAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALA 1239
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 463 RRWFAVLPEVLLVNAYGLTETCDDTNHEVLDRAQDGSRVPLGRAIAGVGVHVVDGNLMPVPLGATGEIVFSGRCLARGYV 542
Cdd:COG3321 1240 AAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAA 1319
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993051 543 NDPIRTALAFTASPLFPGQRLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPG 609
Cdd:COG3321 1320 ALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
330-610 |
4.78e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.42 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 330 LAYIYFTSGSTGEPKGVMCEHegmlNHMLAKIDdlGVRagTVVAQTAPQcfDISLWQLlaPL-----ITGGTVVIVSQQA 404
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTH----GNIVATVA--GVM--TVVPKLGKN--DVYLAYL--PLahileLAAESVMAAVGAA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 405 L-----LDVEQFAAELDR-SRVEVAQLVPSYVEVLLGHLERRPRALpaLRCVSATGEALKA----ALVRR-------WF- 466
Cdd:PLN02387 320 IgygspLTLTDTSNKIKKgTKGDASALKPTLMTAVPAILDRVRDGV--RKKVDAKGGLAKKlfdiAYKRRlaaiegsWFg 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 467 AVLPEVLLVNA-------------------------------------------YGLTETC--------DDTNhevldra 495
Cdd:PLN02387 398 AWGLEKLLWDAlvfkkiravlggrirfmlsggaplsgdtqrfiniclgapigqgYGLTETCagatfsewDDTS------- 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 496 qdgsrvpLGRaiagVG-------VHVVD----GNLM---PVPlgaTGEIVFSGRCLARGYVNDPIRTALAFTASPlfPGQ 561
Cdd:PLN02387 471 -------VGR----VGpplpccyVKLVSweegGYLIsdkPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGM 534
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 502993051 562 RLYRSGDFGRWTPDGRLEFSGRRDTQVKIR-GFRVEIGEIEDRLLRLPGV 610
Cdd:PLN02387 535 RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV 584
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
118-350 |
6.76e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 46.89 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 118 LVVRCRREWVDDAYAARIADY-------------HRTALRLAAADPDAEHAgQCLLGAAELRHQLTAFSGAPRELPDRR- 183
Cdd:PTZ00216 9 MDKRNSRSEVPDPDIEEYRRYgpqnvpvpgteteNASAIYRIAGVTDEEHE-RLRNEWYYGPNFLQRLERICKERGDRRa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 184 ---------VHQLIAD-TAAARPDDVAVVAGLDQLTYRQLDERANQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGV- 252
Cdd:PTZ00216 88 layrpvervEKEVVKDaDGKERTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 253 ---------------------LKAGGCylpvephfpleriAAMVTRSACGRAL-----TDEVGAAVTDRLGGLVPGLRAR 306
Cdd:PTZ00216 168 sqsmvaatvyanlgedalayaLRETEC-------------KAIVCNGKNVPNLlrlmkSGGMPNTTIIYLDSLPASVDTE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 502993051 307 GVD-----EILRGGH--PSEVPGT-PVVAGQLAYIYFTSGSTGEPKGVMCEH 350
Cdd:PTZ00216 235 GCRlvawtDVVAKGHsaGSHHPLNiPENNDDLALIMYTSGTTGDPKGVMHTH 286
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
208-362 |
1.04e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 208 LTYRQLDERAnQVAHALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGgcylpvephfpleRIAAMVTRSACGRAL--- 284
Cdd:PRK06814 659 LTYRKLLTGA-FVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAG-------------RVPAMINFSAGIANIlsa 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 285 --TDEVGAAVTDR-------LGGLVPGLrARGVDEI--------------LRGGHPSEVPGTPVVAGQ---LAYIYFTSG 338
Cdd:PRK06814 725 ckAAQVKTVLTSRafiekarLGPLIEAL-EFGIRIIyledvraqigladkIKGLLAGRFPLVYFCNRDpddPAVILFTSG 803
|
170 180
....*....|....*....|....*..
gi 502993051 339 STGEPKGVMCEHEGML---NHMLAKID 362
Cdd:PRK06814 804 SEGTPKGVVLSHRNLLanrAQVAARID 830
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
207-675 |
2.12e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 45.12 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 207 QLTYRQLDERANQVAhALLADGLAAEDVVAVVSERAIPWLVAVLGVLKAGGCYLPV-EPHFP--LERIAAMVTRSACGRA 283
Cdd:PRK12476 68 ELTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 284 LTDEVGA-AVTDRLGGLVPGLRAR--GVDEILRGGHPSEVPgTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGM---LNHM 357
Cdd:PRK12476 147 LTTTAAAeAVEGFLRNLPRLRRPRviAIDAIPDSAGESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVgtnLVQM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 358 LAKIDDLGVraGTVVAQTAPQCFDISLWQLLAPLITGGTVVIVSQQALLD-----VEQFAAELDRSRVEVAqlVPSYVEV 432
Cdd:PRK12476 226 ILSIDLLDR--NTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRrpqrwIKALSEGSRTGRVVTA--APNFAYE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 433 LLGHlerrpRALPA------LRCVSAT--GEALKAALVRRWFAV-----LPEVLLVNAYGLTE-------TCDDTNHEV- 491
Cdd:PRK12476 302 WAAQ-----RGLPAegddidLSNVVLIigSEPVSIDAVTTFNKAfapygLPRTAFKPSYGIAEatlfvatIAPDAEPSVv 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 492 -LDRAQ--DGSRVPLGRAIAGVGVHVVDGNLMP--------------VPLGATGEIVFSGRCLARGYVNDPIRTALAFTA 554
Cdd:PRK12476 377 yLDREQlgAGRAVRVAADAPNAVAHVSCGQVARsqwavivdpdtgaeLPDGEVGEIWLHGDNIGRGYWGRPEETERTFGA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 555 ---SPLF---------PGQRLYRSGDFGRWTpDGRLEFSGRRDTQVKIRGFRVEIGEIEDRL-LRLPGVRE--ATVIVAG 619
Cdd:PRK12476 457 klqSRLAegshadgaaDDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVaEASPMVRRgyVTAFTVP 535
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502993051 620 AAESARLVACYSAAPSLA---PGPLVEAL-ARVLPDYMVP-RDWYWLD--VLPLTGNGKVDRK 675
Cdd:PRK12476 536 AEDNERLVIVAERAAGTSradPAPAIDAIrAAVSRRHGLAvADVRLVPagAIPRTTSGKLARR 598
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
764-993 |
3.51e-04 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 43.07 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 764 TGATGTRPVLHRLTPPG--RRTLVCFPYAGGNAVTYVPLAGELAAEGWAVYGVEPPGRDGNEAP-VSVPELAELVA---- 836
Cdd:COG2267 9 PTRDGLRLRGRRWRPAGspRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPrGHVDSFDDYVDdlra 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 837 --GELAALDAGPLTLWGHSTGvaaalatarllrsrGHDVRRVLlgaqlpgdsgARRAQAaevtalpdeavVTALV-ESGR 913
Cdd:COG2267 89 alDALRARPGLPVVLLGHSMG--------------GLIALLYA----------ARYPDR-----------VAGLVlLAPA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 914 PELAEVGDAHRRLLADAYRHDVAAacgylaealdagdRLDVPVTVVLAADDVpdDLPGDPWDW--SRLAGDVRVVELPDG 991
Cdd:COG2267 134 YRADPLLGPSARWLRALRLAEALA-------------RIDVPVLVLHGGADR--VVPPEAARRlaARLSPDVELVLLPGA 198
|
..
gi 502993051 992 GH 993
Cdd:COG2267 199 RH 200
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
302-602 |
7.00e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 43.47 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 302 GLRARGVDEILRGGHPSEVPGTPVVAGQLAYIYFTSGSTGEPKGVMCEHEGMLN------HMLAKIDD-LGVR------- 367
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTliagviRLLKSANAaLTVKdvylsyl 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 368 -AGTVVAQTAPQCF-----DISLWQllaplitGGTVVIVSQQALLDVEQFAAE---LDRSRVEVAQLVPS---------- 428
Cdd:PLN02614 277 pLAHIFDRVIEECFiqhgaAIGFWR-------GDVKLLIEDLGELKPTIFCAVprvLDRVYSGLQKKLSDggflkkfvfd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 429 --------YVEVLLGHLERRP-----------RALPALRCVSATGEALKAALVRRWFAVLPEVLLVNAYGLTETCDDTNH 489
Cdd:PLN02614 350 safsykfgNMKKGQSHVEASPlcdklvfnkvkQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFV 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 490 EVLDRaqdgsrvpLGR-AIAGVGVHVVDGNLMPVP------LGAT--GEIVFSGRCLARGYVNDPIRTALAFTASPLfpg 560
Cdd:PLN02614 430 SLPDE--------LDMlGTVGPPVPNVDIRLESVPemeydaLASTprGEICIRGKTLFSGYYKREDLTKEVLIDGWL--- 498
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502993051 561 qrlyRSGDFGRWTPDGRLEFSGRRDTQVKI-RGFRVEIGEIED 602
Cdd:PLN02614 499 ----HTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIEN 537
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
558-612 |
3.41e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.27 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 502993051 558 FPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVKIRGFRVEIGEIEDRLLRLPGVRE 612
Cdd:PTZ00237 490 FPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
792-1006 |
3.98e-03 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 39.76 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 792 GNAVTYVPLAgELAAEGWAVYGVEPPGR-DGNEAPVSVPELAELVAGELAALDAGPLTLWGHSTGvaaalATARLLRSRG 870
Cdd:pfam12697 6 GAGLSAAPLA-ALLAAGVAVLAPDLPGHgSSSPPPLDLADLADLAALLDELGAARPVVLVGHSLG-----GAVALAAAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 871 HDVRRVLLGAQLPGDSGARRAQAAEVTALPDEAVVTALVESGRPELAEVGDAHRRLLADAYRHDVAAACGYLAEALDAGD 950
Cdd:pfam12697 80 ALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLPLAAWR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993051 951 RLDVPVTVVLAADDVpddLPGDPWDWSRLAGDVRVVELPDGGHyFAASRPASVARV 1006
Cdd:pfam12697 160 DLPVPVLVLAEEDRL---VPELAQRLLAALAGARLVVLPGAGH-LPLDDPEEVAEA 211
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
333-628 |
6.39e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 40.60 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 333 IYFTSGSTGEPKGVMCEHEGMLNHMLAkIDDLGVRAGTVVAQT--------APQCFD-------------ISLW------ 385
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLS-TDHLLKVTDRVATEEdsyfsylpLAHVYDqvietyciskgasIGFWqgdiry 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 386 -----QLLAPLITGGtVVIVSQQALLDVEQFAAELDRSRVEVAQLVPSYVevlLGHLE---RRPRALPAL-RCV-SATGE 455
Cdd:PLN02861 304 lmedvQALKPTIFCG-VPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYK---LGNLRkglKQEEASPRLdRLVfDKIKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 456 AL----------KAAL---VRRWFAVLPEVLLVNAYGLTETCDdtnhevldraqdGSRVPLGRAIA-----GVGVHVVDG 517
Cdd:PLN02861 380 GLggrvrlllsgAAPLprhVEEFLRVTSCSVLSQGYGLTESCG------------GCFTSIANVFSmvgtvGVPMTTIEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993051 518 NLMPVP-LG-------ATGEIVFSGRCLARGYVNDPirtalAFTASPLFPGqrLYRSGDFGRWTPDGRLEFSGRRDTQVK 589
Cdd:PLN02861 448 RLESVPeMGydalsdvPRGEICLRGNTLFSGYHKRQ-----DLTEEVLIDG--WFHTGDIGEWQPNGAMKIIDRKKNIFK 520
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502993051 590 I-RGFRVEIGEIEDRLLRLPGVreATVIVAGAAESARLVA 628
Cdd:PLN02861 521 LsQGEYVAVENLENTYSRCPLI--ASIWVYGNSFESFLVA 558
|
|
| |
