|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
11-1158 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 609.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 11 AALRSLPAARDALGAYPLSSEQKRLWLLAQLAGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPV 90
Cdd:COG1020 4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 91 RLLMPTGLVKLEYFDRPPSDADMAELIGAA---------FELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPS----- 156
Cdd:COG1020 84 QVIQPVVAAPLPVVVLLVDLEALAEAAAEAaaaaealapFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSdglll 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 157 --LQRIAQTLFQTEPDHQYPAVGAIAEVFQREQTLAQDAQITEQWQQWGIGLQ-APAATEIPTENPRPAIKGS------- 226
Cdd:COG1020 164 aeLLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAgLPPLLELPTDRPRPAVQSYrgarvsf 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 227 --DRQVHEALTAWgdqpvAEAE-------IVSSWLTVLMRWQGSQSAL--CAIKVRDKAHA-NLIGPLQTYLPVRVDMPD 294
Cdd:COG1020 244 rlPAELTAALRAL-----ARRHgvtlfmvLLAAFALLLARYSGQDDVVvgTPVAGRPRPELeGLVGFFVNTLPLRVDLSG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 295 GSTLAQL--RLQvEEQLNGNDHP--SFSTLLEVCPPKRDLSRTPYFQTGLQFIAHDVEQRDFHAGNLTRLPTKQPSSDLD 370
Cdd:COG1020 319 DPSFAELlaRVR-ETLLAAYAHQdlPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 371 LFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLS---APGEQPIATVALMGQQMQQTVLAQAHGPRT-TPPQLT 446
Cdd:COG1020 398 LTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEalaADPDQPLGDLPLLTAAERQQLLAEWNATAApYPADAT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 447 LTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPID 526
Cdd:COG1020 478 LHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITsDQQSVEGWP----QVARIRMEALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVV 602
Cdd:COG1020 558 PAYPAERLAYMLEDAGARLVLT-QSALAARLPelgvPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 603 VEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVP 682
Cdd:COG1020 637 VEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTP 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 683 SLLGTLIDHPFAnDCRAVKLVLSGGEVLNPELAHKIQKVW-QADVANLYGPTEATIDALYFSIDKN--AAGAIPIGYPID 759
Cdd:COG1020 717 SLLRALLDAAPE-ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPdaDGGSVPIGRPIA 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 760 NTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFG--NGRVYATGDLGRRWSSGAISYLGRRDQQ 837
Cdd:COG1020 796 NTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfpGARLYRTGDLARWLPDGNLEFLGRADDQ 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 838 VKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPR 917
Cdd:COG1020 876 VKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 918 TATGKVdmlKLDQLAAPQLNDAGGTECRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSILLTRLAGTLSAKYQV 997
Cdd:COG1020 956 PLTGNG---KLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 998 QIPLHEFFLTPTPAAVAQAIEIYRREGLTALLSRQHAQTLEQDIYLEEHIRPDGLPHANWYQPSVVFLTGATGYLGLYLI 1077
Cdd:COG1020 1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALL 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1078 EQLLKRTTSRVICLCRAKDAEHAKARILEGLktYRIDVGSEL*RVEYLTGDLALPHLGLSEHQWQTLAEEVDVIYHNGAL 1157
Cdd:COG1020 1113 LLLALLLALLAALRARRAVRQEGPRLRLLVA--LAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
|
.
gi 37542635 1158 V 1158
Cdd:COG1020 1191 L 1191
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
459-928 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 566.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITsdqqsvegwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRT 618
Cdd:cd05930 81 EDSGAKLVLT--------------------DPD------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 619 WPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCR 698
Cdd:cd05930 129 YPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 AVKLVLSGGEVLNPELAHKIQKV-WQADVANLYGPTEATIDALYFSIDKNAA--GAIPIGYPIDNTDAYIVDLNLNPVPP 775
Cdd:cd05930 209 SLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYRVPPDDEedGRVPIGRPIPNTRVYVLDENLRPVPP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 776 GVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPF-GNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLL 854
Cdd:cd05930 289 GVPGELYIGGAGLARGYLNRPELTAERFVPNPFgPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 855 CQALELKEAIVFAQHAGTEQARLVAAI--EQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05930 369 LAHPGVREAAVVAREDGDGEKRLVAYVvpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
448-924 |
5.88e-156 |
|
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: 480.62 E-value: 5.88e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 448 TEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDP 527
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 528 RLPTDRIQFLIENSGCELVITSDQQSVEG-----WPQVARIRMEALDPDIRWVAPTGlshSDAAYLIYTSGSTGVPKGVV 602
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLpaggdVALLGDEALAAPPATPPLVPPRP---DNLAYVIYTSGSTGRPKGVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 603 VEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVP 682
Cdd:cd17646 158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 683 SLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNA-AGAIPIGYPIDNT 761
Cdd:cd17646 238 SMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAeTPSVPIGRPVPNT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 762 DAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVKI 840
Cdd:cd17646 318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGsRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 841 RGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVA---AIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPR 917
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPL 477
|
....*..
gi 37542635 918 TATGKVD 924
Cdd:cd17646 478 TANGKLD 484
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
16-1037 |
6.51e-155 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 522.03 E-value: 6.51e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 16 LPAARDALGAYPLSSEQKRLWLLAQL---AGTATLPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRL 92
Cdd:PRK12467 40 IPQVRSAFERIPLSYAQERQWFLWQLdpdSAAYNIPTALR--LRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 93 LMPTGLVKLEYFDRPPSDADMAEL---------IGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQT 163
Cdd:PRK12467 118 IDASLSLTIPLDDLANEQGRARESqieayineeVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 164 LFQTEPDH------QYPAVG---AIAEVFQREQTLA-QDAQITEQWQQwGIGLQAPAaTEIPTENPRPAI---KGSDRQV 230
Cdd:PRK12467 198 LVQLYSAYsqgrepSLPALPiqyADYAIWQRSWLEAgERERQLAYWQE-QLGGEHTV-LELPTDRPRPAVpsyRGARLRV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 231 H-EALTAWGDQPVAEAE-------IVSSWLTVLMRWQGsQSALCA---IKVRDKAHAN-LIGPL--QTYLPVRVD--MPD 294
Cdd:PRK12467 276 DlPQALSAGLKALAQREgvtlfmvLLASFQTLLHRYSG-QSDIRIgvpNANRNRVETErLIGFFvnTQVLKAEVDpqASF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 295 GSTLAQLRLQVEEQLNGNDHPsFSTLLEVCPPKRDLSRTPYFQTGL--QFIAHDVEQR---DFHAGNLTRLPTKQPSSDL 369
Cdd:PRK12467 355 LELLQQVKRTALGAQAHQDLP-FEQLVEALQPERSLSHSPLFQVMFnhQNTATGGRDRegaQLPGLTVEELSWARHTAQF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 370 DLFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSAPGEQP---IATVALMGQQMQQTVLAQAHGPRTTPPQLT 446
Cdd:PRK12467 434 DLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPrrrLGELPLLDAEERARELVRWNAPATEYAPDC 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 447 LTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPID 526
Cdd:PRK12467 514 VHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITSDQQSVEgWPQVARIRMEALDPDIRWVA-------PTGLSHSDAAYLIYTSGSTGVPK 599
Cdd:PRK12467 594 PEYPQDRLAYMLDDSGVRLLLTQSHLLAQ-LPVPAGLRSLCLDEPADLLCgysghnpEVALDPDNLAYVIYTSGSTGQPK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 600 GVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLG 679
Cdd:PRK12467 673 GVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLK 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 680 GVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKI-QKVWQADVANLYGPTEATIDALYFSIDKNAA--GAIPIGY 756
Cdd:PRK12467 753 IVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVrALGPGARLINHYGPTETTVGVSTYELSDEERdfGNVPIGQ 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 757 PIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFG--NGRVYATGDLGRRWSSGAISYLGRR 834
Cdd:PRK12467 833 PLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGadGGRLYRTGDLARYRADGVIEYLGRM 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 835 DQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQhAGTEQARLVA-------AIEQQPGLHSEGIKQELLRHLPAYLIPS 907
Cdd:PRK12467 913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAylvpaavADGAEHQATRDELKAQLRQVLPDYMVPA 991
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 908 QLLLLDELPRTATGKVDMLKLDQLAAPQLNDAggteCRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSILLTRL 987
Cdd:PRK12467 992 HLLLLDSLPLTPNGKLDRKALPKPDASAVQAT----FVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQV 1067
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 988 AGTLSAKYQVQIPLHEFFLTPTPAAVAQAIEIYRREGLTALL--SRQHAQTL 1037
Cdd:PRK12467 1068 ISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPdvDRDQPLPL 1119
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
16-983 |
8.19e-152 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 512.78 E-value: 8.19e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 16 LPAARDAlgAYPLSSEQKRLWLLAQL-AGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLM 94
Cdd:PRK12467 1109 PDVDRDQ--PLPLSYAQERQWFLWQLePGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIH 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 95 PTGLVKLEYFDRPPSDADMAEL-------IGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTL--- 164
Cdd:PRK12467 1187 PVGSLTLEEPLLLAADKDEAQLkvyveaeARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELval 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 165 ---FQTEPDHQYPAVG---AIAEVFQREQTLA-QDAQITEQWQQwGIGLQAPAaTEIPTENPRPAIkGSDRQVHEALT-- 235
Cdd:PRK12467 1267 yaaYSQGQSLQLPALPiqyADYAVWQRQWMDAgERARQLAYWKA-QLGGEQPV-LELPTDRPRPAV-QSHRGARLAFElp 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 236 ---AWGDQPVAEAE-------IVSSWLTVLMRWQGSQSALCAIKVRDKAHAN---LIGPLQTYLPVRVDMPDGSTLAQLR 302
Cdd:PRK12467 1344 palAEGLRALARREgvtlfmlLLASFQTLLHRYSGQDDIRVGVPIANRNRAEtegLIGFFVNTQVLRAEVDGQASFQQLL 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 303 LQVEEQ-LNGNDHPS--FSTLLEVCPPKRDLSRTPYFQTGL--QFIAHDVeQRDFHAGNLTRLPTKQPSSDLDLFISCWV 377
Cdd:PRK12467 1424 QQVKQAaLEAQAHQDlpFEQLVEALQPERSLSHSPLFQVMFnhQRDDHQA-QAQLPGLSVESLSWESQTAQFDLTLDTYE 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 378 SDGTLGLTLDYDCAVLNSSQVEVLA---QALISVLSAPGEQPIATVALM-GQQMQQTVLAQAHGPRTTPPQLTLTEWVAA 453
Cdd:PRK12467 1503 SSEGLQASLTYATDLFEASTIERLAghwLNLLQGLVADPERRLGELDLLdEAERRQILEGWNATHTGYPLARLVHQLIED 1582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 454 STEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDR 533
Cdd:PRK12467 1583 QAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER 1662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 534 IQFLIENSGCELVITSdQQSVEGWPQVARIRMEALDPDIRWVAPTG-------LSHSDAAYLIYTSGSTGVPKGVVVEHR 606
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQ-SHLQARLPLPDGLRSLVLDQEDDWLEGYSdsnpavnLAPQNLAYVIYTSGSTGRPKGAGNRHG 1741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 607 QVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLG 686
Cdd:PRK12467 1742 ALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQ 1821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 687 TLIDHPFA-NDCRAVKLVLSGGEVLNPELAhkiQKVWQ----ADVANLYGPTEATIDALYFSI---DKNAAGAIPIGYPI 758
Cdd:PRK12467 1822 QLLQMDEQvEHPLSLRRVVCGGEALEVEAL---RPWLErlpdTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPI 1898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 759 DNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYATGDLGRRWSSGAISYLGRRDQ 836
Cdd:PRK12467 1899 ANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTvgSRLYRTGDLARYRADGVIEYLGRIDH 1978
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 837 QVKIRGHRIELNEV-AHLLCQAlELKEAIVFAQH-AGTEQ---------ARLVAAIEQQPGLHSEgIKQELLRHLPAYLI 905
Cdd:PRK12467 1979 QVKIRGFRIELGEIeARLREQG-GVREAVVIAQDgANGKQlvayvvptdPGLVDDDEAQVALRAI-LKNHLKASLPEYMV 2056
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 906 PSQLLLLDELPRTATGKVDMLKLDQLAAPQLNDAggteCRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSIL 983
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKALPAPDASELQQA----YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSII 2130
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-983 |
1.31e-149 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 506.42 E-value: 1.31e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 12 ALRSLPAARDALGAYPLSSEQKRLWLLAQL---AGTATLPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVE---- 84
Cdd:PRK12316 36 SLFPIPAGVSSAERDRLSYAQQRMWFLWQLepqSGAYNLPSAVR--LNGPLDRQALERAFASLVQRHETLRTVFPRgadd 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 85 -----VLERP--VRLLMPTGLVKLEYFDRPPSDADMAELIgaAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSL 157
Cdd:PRK12316 114 slaqvPLDRPleVEFEDCSGLPEAEQEARLRDEAQRESLQ--PFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 158 QRIAQTLFQ------TEPDHQYPAVG---AIAEVFQREQTLA--QDAQItEQWQQwGIGLQAPAaTEIPTENPRPAI--- 223
Cdd:PRK12316 192 NVLIEEFSRfysayaTGAEPGLPALPiqyADYALWQRSWLEAgeQERQL-EYWRA-QLGEEHPV-LELPTDHPRPAVpsy 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 224 KGS------DRQVHEAL--TAWGDQPVAEAEIVSSWLTVLMRWQGsQSAL---CAIKVRDKAHAN-LIGPLQTYLPVRVD 291
Cdd:PRK12316 269 RGSryefsiDPALAEALrgTARRQGLTLFMLLLGAFNVLLHRYSG-QTDIrvgVPIANRNRAEVEgLIGFFVNTQVLRSV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 292 MPDGSTLAQLRLQVEEQLNG----NDHPsFSTLLEVCPPKRDLSRTPYFQTGL--QFIAHDVEQRDFHAG-NLTRLPTKQ 364
Cdd:PRK12316 348 FDGRTRVATLLAGVKDTVLGaqahQDLP-FERLVEALKVERSLSHSPLFQVMYnhQPLVADIEALDTVAGlEFGQLEWKS 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 365 PSSDLDLFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSAPGEQPIATVA----LMGQQMQQTVLAQAHGPRT 440
Cdd:PRK12316 427 RTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDelpmLDAEERGQLVEGWNATAAE 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 441 TPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGH 520
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 521 AFLPIDPRLPTDRIQFLIENSGCELVItSDQQSVEGWPQVARIRMEALDPDIRWVAptglSHSDA-----------AYLI 589
Cdd:PRK12316 587 AYVPLDPEYPAERLAYMLEDSGVQLLL-SQSHLGRKLPLAAGVQVLDLDRPAAWLE----GYSEEnpgtelnpenlAYVI 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 590 YTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDL 669
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVEL 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 670 MIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKI-QKVWQADVANLYGPTEATIDALYFSIDKNA 748
Cdd:PRK12316 742 INREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEG 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 749 AGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGA 827
Cdd:PRK12316 822 GDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGeRMYRTGDLARYRADGV 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 828 ISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQhagtEQARLVAAI--EQQPGLHSEGIKQELLRHLPAYLI 905
Cdd:PRK12316 902 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVvlESEGGDWREALKAHLAASLPEYMV 977
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 906 PSQLLLLDELPRTATGKVDMlklDQLAAPQLNDAgGTECRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSIL 983
Cdd:PRK12316 978 PAQWLALERLPLTPNGKLDR---KALPAPEASVA-QQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIV 1051
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
19-1018 |
8.22e-145 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 476.07 E-value: 8.22e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 19 ARDALGAYPLSSEQKRLWLLAQLAGTATLPVTVRY-AFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPT- 96
Cdd:PRK10252 1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYvELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 97 GLVKLEYFDRP----PSDADMAeLIGA----AFELDKG-PLLRAFITRTAAQQHELHLVGHPIVVDEPSL----QRIA-- 161
Cdd:PRK10252 81 TFPLPEIIDLRtqpdPHAAAQA-LMQAdlqqDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFpaitRRIAai 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 162 ---QTLFQTEPDHQYPAVGAIAEVFQREQTLAQDAQITEQWQQWGIGLQAPA---ATEIPTENP-----RPAIKGSDRQV 230
Cdd:PRK10252 160 ycaWLRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPAslsPAPLPGRSAsadilRLKLEFTDGAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 231 HEALTAWGDQPVAE--AEIVSSWLT------------VLMRWQGSqSALCAIkvrdkahanliGPLQTYLPVRVDMPDGS 296
Cdd:PRK10252 240 RQLAAQASGVQRPDlaLALVALWLGrlcgrmdyaagfIFMRRLGS-AALTAT-----------GPVLNVLPLRVHIAAQE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 297 TLAQLRLQVEEQLN-GNDHPSFSTLLEVcppkRDLSR----TPYFQTGLQFIAHDvEQRDFHA--GNLTRLPTKqPSSDL 369
Cdd:PRK10252 308 TLPELATRLAAQLKkMRRHQRYDAEQIV----RDSGRaagdEPLFGPVLNIKVFD-YQLDFPGvqAQTHTLATG-PVNDL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 370 DLFIScwvSDGTLGLTLDYDC--AVLNSSQVEVLAQALISVLSAPGEQPIATVA----LMGQQMQQtvLAQAHGPRTTPP 443
Cdd:PRK10252 382 ELALF---PDEHGGLSIEILAnpQRYDEATLIAHAERLKALIAQFAADPALLCGdvdiLLPGEYAQ--LAQVNATAVEIP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 444 QLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFL 523
Cdd:PRK10252 457 ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 524 PIDPRLPTDRIQFLIENSGCELVITSDQQS--VEGWPQVARIRMEALDPDIRwVAPTGLSH-SDAAYLIYTSGSTGVPKG 600
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADQLprFADVPDLTSLCYNAPLAPQG-AAPLQLSQpHHTAYIIFTSGSTGRPKG 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 601 VVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGG 680
Cdd:PRK10252 616 VMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHF 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 681 VPSLLGTLIDHP----FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYF-----SIDKNAAGA 751
Cdd:PRK10252 696 VPSMLAAFVASLtpegARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYpafgeELAAVRGSS 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 752 IPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISY 830
Cdd:PRK10252 776 VPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGeRMYRTGDVARWLDDGAVEY 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 831 LGRRDQQVKIRGHRIELNEVAHLLcQALELKE-----AIVFAQHA--GTEQARLVAAIEQQPGLH--SEGIKQELLRHLP 901
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEIDRAM-QALPDVEqavthACVINQAAatGGDARQLVGYLVSQSGLPldTSALQAQLRERLP 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 902 AYLIPSQLLLLDELPRTATGkvdmlKLDQLAAPQLNDAGGTECRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNS 981
Cdd:PRK10252 935 PHMVPVVLLQLDQLPLSANG-----KLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHS 1009
|
1050 1060 1070
....*....|....*....|....*....|....*..
gi 37542635 982 ILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIE 1018
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1024 |
1.86e-140 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 478.89 E-value: 1.86e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 3 SPTIDTFEAALRSL------------PAARDalGAYPLSSEQKRLWLLAQL---AGTATLPVTVRyaFTGTVDLAVVQQN 67
Cdd:PRK05691 643 APTLAAFSAAVARQlagggaaqaaiaRLPRG--QALPQSLAQNRLWLLWQLdpqSAAYNIPGGLH--LRGELDEAALRAS 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 68 LSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEYFDRppSDADMAELIGAA-----------FELDKGPLLRAFITRT 136
Cdd:PRK05691 719 FQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDL--SDLPEAEREARAaqireeearqpFDLEKGPLLRVTLVRL 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 137 AAQQHELHLVGHPIVVDEPSLQRI-------------AQTLFQTEPDHQYPAVGAiaevFQREQTLAQDAQitEQWQQWG 203
Cdd:PRK05691 797 DDEEHQLLVTLHHIVADGWSLNILldefsrlyaaacqGQTAELAPLPLGYADYGA----WQRQWLAQGEAA--RQLAYWK 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 204 IGLQAPAAT-EIPTENPRPAIKGS-----DRQVHEAL------TAWGDQPVAEAEIVSSWLTVLMRWQGSQSALCAIKVR 271
Cdd:PRK05691 871 AQLGDEQPVlELATDHPRSARQAHsaarySLRVDASLsealrgLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNA 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 272 DKAH---ANLIGPLQTYLPVRVD----MPDGSTLAQLRLQVEEQLNGNDHPsFSTLLEVCPPKRdlsrtpyfQTGLQFIA 344
Cdd:PRK05691 951 NRPRletQGLVGFFINTQVLRAQldgrLPFTALLAQVRQATLGAQAHQDLP-FEQLVEALPQAR--------EQGLFQVM 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 345 HDVEQRDFHAgnLTRLP----------TKQPSSDLDLFiSCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSAPGE 414
Cdd:PRK05691 1022 FNHQQRDLSA--LRRLPgllaeelpwhSREAKFDLQLH-SEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCE 1098
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 415 QP---IATVALMGQQMQQTVLAQAHGPrTTPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHV 491
Cdd:PRK05691 1099 DPqraLGDVQLLDAAERAQLAQWGQAP-CAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKG 1177
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 492 AKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSdQQSVEGWPQ---VARIRMEAL 568
Cdd:PRK05691 1178 VGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQ-SHLLERLPQaegVSAIALDSL 1256
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 569 DPDIRWVAPTGLS-HSD-AAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPL 646
Cdd:PRK05691 1257 HLDSWPSQAPGLHlHGDnLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPL 1336
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 647 LTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKI-QKVWQAD 725
Cdd:PRK05691 1337 ITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVlQRLPQVQ 1416
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 726 VANLYGPTEATIDALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLP 805
Cdd:PRK05691 1417 LHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP 1496
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 806 NPFGNG--RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEV-AHLLCQAlELKEAIVFAqHAGTEQARLVA--A 880
Cdd:PRK05691 1497 DPLGEDgaRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIqARLLAQP-GVAQAAVLV-REGAAGAQLVGyyT 1574
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 881 IEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMlklDQLAAPQLNDaggTECRAPRTDLEQSVMTDFA 960
Cdd:PRK05691 1575 GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR---RALPEPVWQQ---REHVEPRTELQQQIAAIWR 1648
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 961 QVLGLTAVTPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIEIYRREG 1024
Cdd:PRK05691 1649 EVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAG 1712
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
472-865 |
2.20e-137 |
|
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: 427.84 E-value: 2.20e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 472 SYAELWARAALVAAN-ISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD 550
Cdd:TIGR01733 1 TYRELDERANRLARHlRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QQSvegwPQVARIRMEALDPDIRWVAPTG-----------LSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTW 619
Cdd:TIGR01733 81 ALA----SRLAGLVLPVILLDPLELAALDdapappppdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 620 PLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRH-DVSVLGGVPSLLGTLIDHPFAnDCR 698
Cdd:TIGR01733 157 GLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEhPVTVLNLTPSLLALLAAALPP-ALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 AVKLVLSGGEVLNPELAHKIQ-KVWQADVANLYGPTEATIDALYFSIDKNAAG---AIPIGYPIDNTDAYIVDLNLNPVP 774
Cdd:TIGR01733 236 SLRLVILGGEALTPALVDRWRaRGPGARLINLYGPTETTVWSTATLVDPDDAPresPVPIGRPLANTRLYVLDDDLRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 775 PGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFG---NGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVA 851
Cdd:TIGR01733 316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
410
....*....|....
gi 37542635 852 HLLCQALELKEAIV 865
Cdd:TIGR01733 396 AALLRHPGVREAVV 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-1046 |
5.13e-136 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 465.59 E-value: 5.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 4 PTIDTFEAALRSLPAAR-------DALGAYPLSSEQKRLWLLAQL-AGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHS 75
Cdd:PRK12316 2574 PTLAAFAASLESGQTSRapvlqkvTRVQPLPLSHAQQRQWFLWQLePESAAYHLPSALHLRGVLDQAALEQAFDALVLRH 2653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 76 ESLRSLFVEVLERPVRLLMPTGLVKLEYFDRPPSDAD-----MAELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPI 150
Cdd:PRK12316 2654 ETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAairqrVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHI 2733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 151 VVDEPS-------LQRIAQTLFQTEPDHQYPAVGAIAEVFQREQTLAQDAQITEQWQQWGIGLQAPAAT-EIPTENPRPA 222
Cdd:PRK12316 2734 VSDGWSmqvmvdeLVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVlELPLDRPRPA 2813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 223 IkgsdrQVHEALTAWGDQPVAEAE----------------IVSSWLTVLMRWQGSQSALCAIKVRDKAHAN---LIGPLQ 283
Cdd:PRK12316 2814 L-----QSHRGARLDVALDVALSRellalarregvtlfmlLLASFQVLLHRYSGQSDIRVGVPIANRNRAEterLIGFFV 2888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 284 TYLPVRVDMPDGSTLAQLRLQVEEQ---LNGNDHPSFSTLLEVCPPKRDLSRTPYFQTGLQFIAHDVEQRDFHAGNLTRL 360
Cdd:PRK12316 2889 NTQVLRAQVDAQLAFRDLLGQVKEQalgAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESF 2968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 361 PTKQPSSDLDLFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSAPGEQPIATVA----LMGQQMQQTVLAQAH 436
Cdd:PRK12316 2969 AWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDelamLDAEERGQLLEAWNA 3048
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 437 GPRTTPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVV 516
Cdd:PRK12316 3049 TAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAIL 3128
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 517 RAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQSVEGWPQVARIRMEALDPDIRWVAPTGLSHSD-AAYLIYTSGST 595
Cdd:PRK12316 3129 KAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPEnLAYVIYTSGST 3208
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 596 GVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDV 675
Cdd:PRK12316 3209 GKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGV 3288
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 676 SVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIqkVWQADVANLYGPTEATIDALYFSIDKNAAGAIPIG 755
Cdd:PRK12316 3289 DVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIG 3366
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 756 YPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRR 834
Cdd:PRK12316 3367 RPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGeRLYRTGDLARYRADGVIEYIGRV 3446
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 835 DQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAaiEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDE 914
Cdd:PRK12316 3447 DHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVP--EDEAGDLREALKAHLKASLPEYMVPAHLLFLER 3524
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 915 LPRTATGKVDMLKLDQLAAPQLNdaggTECRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSILLTRL------A 988
Cdd:PRK12316 3525 MPLTPNGKLDRKALPRPDAALLQ----QDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVvsrarqA 3600
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 989 GT-LSAKYQVQIPLHEFFLTPTPAAVAQAIEIYRREGLTALLSRQHaQTLEQDIYLEEH 1046
Cdd:PRK12316 3601 GIrFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQ-QFFEEPVPERHH 3658
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-1021 |
1.73e-135 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 464.05 E-value: 1.73e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 4 PTIDTFEAALRSLP-AARDALGAYPLSSEQKRLW---LLAQLAGTATLPVTVryaftgTVDLAVVQQNLSAWIAHSES-- 77
Cdd:PRK12316 4080 PLAGLDQARLDALPlPLGEIEDIYPLSPMQQGMLfhsLYEQEAGDYINQMRV------DVQGLDVERFRAAWQAALDRhd 4153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 78 -LRSLFVEV--LERP---VRLLMPTGLVKLEYFDRPPSDADMAELIGA----AFELDKGPLLRAFITRTAAQQHELHLVG 147
Cdd:PRK12316 4154 vLRSGFVWQgeLGRPlqvVHKQVSLPFAELDWRGRADLQAALDALAAAererGFDLQRAPLLRLVLVRTAEGRHHLIYTN 4233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 148 HPIVVDEPSlqriaQTLFQTEPDHQYPAVGAIAEVFQREQTLA----QDAQITEQ-WQQWGIGLQAPA--ATEIPTENPR 220
Cdd:PRK12316 4234 HHILMDGWS-----NSQLLGEVLERYSGRPPAQPGGRYRDYIAwlqrQDAAASEAfWREQLAALDEPTrlAQAIARADLR 4308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 221 PAIKGSD--RQVHEALTAWGDQPVAEAEIV------SSWLTVLMRWQGSQSALCAIKVRDKAH-----ANLIGPLQTYLP 287
Cdd:PRK12316 4309 SANGYGEhvRELDATATARLREFARTQRVTlntlvqAAWLLLLQRYTGQDTVAFGATVAGRPAelpgiEGQIGLFINTLP 4388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 288 VRVDMPDGSTLAQLRLQVEEQ---LNGNDHpsfsTLLEVCPPKRDLSRTPYFQTGLQFIAHDVE---QRDFHAGNLTRLP 361
Cdd:PRK12316 4389 VIATPRAQQSVVEWLQQVQRQnlaLREHEH----TPLYEIQRWAGQGGEALFDSLLVFENYPVSealQQGAPGGLRFGEV 4464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 362 TKQPSSDLDLFISCWVSDgTLGLTLDYDCAVLNSSQVEVLA---QALISVLSAPGEQPIATVALMGQQMQQTVLAQahGP 438
Cdd:PRK12316 4465 TNHEQTNYPLTLAVGLGE-TLSLQFSYDRGHFDAATIERLArhlTNLLEAMAEDPQRRLGELQLLEKAEQQRIVAL--WN 4541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 439 RTT---PPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGV 515
Cdd:PRK12316 4542 RTDagyPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAV 4621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 516 VRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQSvEGWPQVARIRMEALDPDIRWV-----APTGLSHSD-AAYLI 589
Cdd:PRK12316 4622 LKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLL-QRLPIPDGLASLALDRDEDWEgfpahDPAVRLHPDnLAYVI 4700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 590 YTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVrTMEDSTALLDL 669
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDD-SLWDPERLYAE 4779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 670 MIRHDVSVLGGVPSLLGTLIDH-PFANDCRAVKLVLSGGEVLNPELAhkiQKVWQA----DVANLYGPTEATIDALYFSI 744
Cdd:PRK12316 4780 IHEHRVTVLVFPPVYLQQLAEHaERDGEPPSLRVYCFGGEAVAQASY---DLAWRAlkpvYLFNGYGPTETTVTVLLWKA 4856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 745 ---DKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFG--NGRVYATGDL 819
Cdd:PRK12316 4857 rdgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGapGGRLYRTGDL 4936
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 820 GRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQ----------ARLVAAIEQQPGLHS 889
Cdd:PRK12316 4937 ARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKqlvgyvvpqdPALADADEAQAELRD 5016
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 890 EgIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQLNDAggteCRAPRTDLEQSVMTDFAQVLGLTAVT 969
Cdd:PRK12316 5017 E-LKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQA----YVAPRSELEQQVAAIWAEVLQLERVG 5091
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 970 PDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIEIYR 1021
Cdd:PRK12316 5092 LDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAG 5143
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
449-924 |
1.63e-132 |
|
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: 417.76 E-value: 1.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 449 EWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPR 528
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 529 LPTDRIQFLIENSGCELVITsdQQSVEGW---PQVARIRMEALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEH 605
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLT--DRSLAGRaggLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 606 RQVVNniLWRQRTW-PLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSL 684
Cdd:cd12117 159 RGVVR--LVKNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 685 LGTLIDHpfANDCRA-VKLVLSGGEVLNPELAHKIQKVWQAD-VANLYGPTEATIDALYFSIDK--NAAGAIPIGYPIDN 760
Cdd:cd12117 237 FNQLADE--DPECFAgLRELLTGGEVVSPPHVRRVLAACPGLrLVNGYGPTENTTFTTSHVVTEldEVAGSIPIGRPIAN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVK 839
Cdd:cd12117 315 TRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGeRLYRTGDLARWLPDGRLEFLGRIDDQVK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 840 IRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTA 919
Cdd:cd12117 395 IRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTA 474
|
....*
gi 37542635 920 TGKVD 924
Cdd:cd12117 475 NGKVD 479
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
456-928 |
1.09e-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: 415.96 E-value: 1.09e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:cd17655 8 EKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVIT-SDQQSVEGWPQVArIRMEalDPDIRWVAPTGLSH----SDAAYLIYTSGSTGVPKGVVVEHRQVVN 610
Cdd:cd17655 88 YILEDSGADILLTqSHLQPPIAFIGLI-DLLD--EDTIYHEESENLEPvsksDDLAYVIYTSGSTGKPKGVMIEHRGVVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 611 NILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLgTLID 690
Cdd:cd17655 165 LVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL-KLLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 691 HpfANDCRAVKL--VLSGGEVLNPELAHKIQKVWQADVA--NLYGPTEATIDALYFSIDKNAA--GAIPIGYPIDNTDAY 764
Cdd:cd17655 244 A--ADDSEGLSLkhLIVGGEALSTELAKKIIELFGTNPTitNAYGPTETTVDASIYQYEPETDqqVSVPIGKPLGNTRIY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 765 IVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFG-NGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGH 843
Cdd:cd17655 322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 844 RIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
....*
gi 37542635 924 DMLKL 928
Cdd:cd17655 482 DRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-1034 |
3.40e-125 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 432.66 E-value: 3.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 4 PTIDTFEAALRSLP-AARDALGAYPLSSEQKRLWLLAQLAGTATLPVT-VRYAFTGtVDLAVVQQNLSAWIAHSESLRSL 81
Cdd:PRK12467 2624 PLAGLSQEQLDRLPvAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINqMRVDVEG-LDVERFRTAWQAVIDRHEILRSG 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 82 FVEV--LERPVRLL-----MPtgLVKLEYFDRPPSDADMAELIGAA----FELDKGPLLRAFITRTAAQQHELHLVGHPI 150
Cdd:PRK12467 2703 FLWDgeLEEPLQVVykqarLP--FSRLDWRDRADLEQALDALAAADrqqgFDLLSAPLLRLTLVRTGEDRHHLIYTNHHI 2780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 151 VVDEPSLQRIAQTLFQTEPDHQYPA-VGAIAEVFQREQtlAQDAQITEQ-WQQWGIGLQAPA--ATEIPTENPRPAIKGS 226
Cdd:PRK12467 2781 LMDGWSGSQLLGEVLQRYFGQPPPArEGRYRDYIAWLQ--AQDAEASEAfWKEQLAALEEPTrlARALYPAPAEAVAGHG 2858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 227 DRQVH------EALTAWG-DQPVAEAEIV-SSWLTVLMRWQGSQSALCAIKVRDKAhANL------IGPLQTYLPVrVDM 292
Cdd:PRK12467 2859 AHYLHldatqtRQLIEFArRHRVTLNTLVqGAWLLLLQRFTGQDTVCFGATVAGRP-AQLrgaeqqLGLFINTLPV-IAS 2936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 293 PDGS-TLAQLRLQVEEQ---LNGNDHPS---------------FSTLL--EVCPPKRDLSRTPyfQTGLQFIAhdVEQRD 351
Cdd:PRK12467 2937 PRAEqTVSDWLQQVQAQnlaLREFEHTPladiqrwagqggealFDSILvfENYPISEALKQGA--PSGLRFGA--VSSRE 3012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 352 fhagnltrlptkQPSSDLDLFISCwvsDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSAPGEQP---IATVALMGQQMQ 428
Cdd:PRK12467 3013 ------------QTNYPLTLAVGL---GDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPaarLGELPTLAAHER 3077
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 429 QTVLAQAHGPRTTPP-QLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAE 507
Cdd:PRK12467 3078 RQVLHAWNATAAAYPsERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVE 3157
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 508 FIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITsdQQSV-EGWPQVARIRMEALDPDIRWVAP-----TGLS 581
Cdd:PRK12467 3158 MIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT--QAHLlEQLPAPAGDTALTLDRLDLNGYSennpsTRVM 3235
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 582 HSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRtME 661
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND-LW 3314
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 662 DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNP-ELAHKIQKVWQADVANLYGPTEATIDAL 740
Cdd:PRK12467 3315 DPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPaAFEQVKRKLKPRGLTNGYGPTEAVVTVT 3394
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 741 YFSIDKNA---AGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYA 815
Cdd:PRK12467 3395 LWKCGGDAvceAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGsgGRLYR 3474
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 816 TGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQ-HAGTEQ--ARLVAAIEQQpglhseGI 892
Cdd:PRK12467 3475 TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARdGAGGKQlvAYVVPADPQG------DW 3548
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 893 KQELLRH----LPAYLIPSQLLLLDELPRTATGKVdmlklDQLAAPQLNDAGGTECRAPRTDLEQSVMTDFAQVLGLTAV 968
Cdd:PRK12467 3549 RETLRDHlaasLPDYMVPAQLLVLAAMPLGPNGKV-----DRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQV 3623
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 969 TPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPA-----------AVAQAIEIYRREGLTALLSRQHA 1034
Cdd:PRK12467 3624 GVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAelagysplgdvPVNLLLDLNRLETGFPALFCRHE 3700
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
447-928 |
1.40e-123 |
|
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: 392.45 E-value: 1.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 447 LTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPID 526
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITsdqqsvegwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHR 606
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT--------------------DPD------------DLAYVIYTSGSTGRPKGVAIEHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 607 QVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADvrtmeDSTALLDLMIRHDVSVLGGVPSLLG 686
Cdd:cd12115 129 NAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAAA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 687 TLIDH-PFANDCRAVKLvlsGGEVLNPELAHKIQKVWQAD-VANLYGPTEATIDALYFSIDKNAAGAIPIGYPIDNTDAY 764
Cdd:cd12115 204 ELLRHdALPASVRVVNL---AGEPLPRDLVQRLYARLQVErVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 765 IVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVKIRGH 843
Cdd:cd12115 281 VLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGaRLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 844 RIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHS--EGIKQELLRHLPAYLIPSQLLLLDELPRTATG 921
Cdd:cd12115 361 RIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGlvEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNG 440
|
....*..
gi 37542635 922 KVDMLKL 928
Cdd:cd12115 441 KIDRSAL 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
459-924 |
2.29e-122 |
|
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: 390.11 E-value: 2.29e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITsDQQSVEGWPQVARIRMEALDPDIRW--VAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQ 616
Cdd:cd12116 81 EDAEPALVLT-DDALPDRLPAGLPVLLLALAAAAAApaAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 617 RTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANd 696
Cdd:cd12116 160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 697 cRAVKLVLSGGEVLNPELAHKIQ-KVwqADVANLYGPTEATIDALYFSIDKnAAGAIPIGYPIDNTDAYIVDLNLNPVPP 775
Cdd:cd12116 239 -RAGLTALCGGEALPPDLAARLLsRV--GSLWNLYGPTETTIWSTAARVTA-AAGPIPIGRPLANTQVYVLDAALRPVPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 776 GVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHL 853
Cdd:cd12116 315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37542635 854 LCQALELKEAIVFAQHAGTEQaRLVAAIEQQ--PGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd12116 395 LAAHPGVAQAAVVVREDGGDR-RLVAYVVLKagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
451-924 |
1.43e-119 |
|
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: 383.23 E-value: 1.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 451 VAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLP 530
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 531 TDRIQFLIENSGCELVIT----SDQQSVEGWPQVARIRMEAL-DPDIRWVAPTGLSHsdAAYLIYTSGSTGVPKGVVVEH 605
Cdd:cd17651 81 AERLAFMLADAGPVLVLThpalAGELAVELVAVTLLDQPGAAaGADAEPDPALDADD--LAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 606 RQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLA--DVRTmeDSTALLDLMIRHDVSVLGGVPS 683
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPpeEVRT--DPPALAAWLDEQRISRVFLPTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 684 LLGTLIDHPFANDCR--AVKLVLSGGE--VLNPELAHKIQKVWQADVANLYGPTEATI-DALYFSIDKNAAGAIP-IGYP 757
Cdd:cd17651 237 ALRALAEHGRPLGVRlaALRYLLTGGEqlVLTEDLREFCAGLPGLRLHNHYGPTETHVvTALSLPGDPAAWPAPPpIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 758 IDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPF-GNGRVYATGDLGRRWSSGAISYLGRRDQ 836
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvPGARMYRTGDLARWLPDGELEFLGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 837 QVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDE 914
Cdd:cd17651 397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSAFVLLDA 476
|
490
....*....|
gi 37542635 915 LPRTATGKVD 924
Cdd:cd17651 477 LPLTPNGKLD 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-1068 |
2.64e-118 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 412.04 E-value: 2.64e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 10 EAALRSLPAARDALG-AYPLSSEQKRLW---LLAQLAG--TATLPVTVryaftGTVDLAVVQQNLSAWIAHSESLRSLFV 83
Cdd:PRK12316 1540 QAQLDALPLPAGEIAdIYPLSPMQQGMLfhsLYEQEAGdyINQLRVDV-----QGLDPDRFRAAWQATVDRHEILRSGFL 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 84 EV--LERPVRLL---MPTGLVKLEYFDRPPSDADMAELIGA----AFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDE 154
Cdd:PRK12316 1615 WQdgLEQPLQVIhkqVELPFAELDWRGREDLGQALDALAQAerqkGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDG 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 155 PSLQRIAQTLFQTEPDHQYPAVGA-----IAEVfQReqtlaQDAQITEQ-WQQWGIGLQAP------AATEIPTENPRPA 222
Cdd:PRK12316 1695 WSNAQLLGEVLQRYAGQPVAAPGGryrdyIAWL-QR-----QDAAASEAfWKEQLAALEEPtrlaqaARTEDGQVGYGDH 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 223 IKGSDRQVHEALTAWGD-QPVAEAEIV-SSWLTVLMRWQGSQSALCAIKVRDKAhANL------IGPLQTYLPV----RV 290
Cdd:PRK12316 1769 QQLLDPAQTRALAEFARaQKVTLNTLVqAAWLLLLQRYTGQETVAFGATVAGRP-AELpgieqqIGLFINTLPViaapRP 1847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 291 DMPDGSTLAQLRLQveeQLNGNDHPSfstllevcPPKRDLSR------TPYFQTGLQF----IAHDVEQRDfHAGNLTRL 360
Cdd:PRK12316 1848 DQSVADWLQEVQAL---NLALREHEH--------TPLYDIQRwagqggEALFDSLLVFenypVAEALKQGA-PAGLVFGR 1915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 361 PTKQPSSDLDLFISCWVSDgTLGLTLDYDCAVLNSSQVEVLAQALISVL---SAPGEQPIATVALMGQQMQQTVLAQ-AH 436
Cdd:PRK12316 1916 VSNHEQTNYPLTLAVTLGE-TLSLQYSYDRGHFDAAAIERLDRHLLHLLeqmAEDAQAALGELALLDAGERQRILADwDR 1994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 437 GPRTTPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVV 516
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 517 RAGHAFLPIDPRLPTDRIQFLIENSGCELVITsDQQSVEGWPQVARIRMEALDPDIRWVA-PTG-----LSHSDAAYLIY 590
Cdd:PRK12316 2075 KAGGAYVPLDPNYPAERLAYMLEDSGAALLLT-QRHLLERLPLPAGVARLPLDRDAEWADyPDTapavqLAGENLAYVIY 2153
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 591 TSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADvRTMEDSTALLDLM 670
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRD-DELWDPEQLYDEM 2232
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 671 IRHDVSVLGGVPSLLGTLIDHPFANDCR-AVKLVLSGGEVLNPELAHKIQKVWQAD-VANLYGPTEATIDALYFS---ID 745
Cdd:PRK12316 2233 ERHGVTILDFPPVYLQQLAEHAERDGRPpAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKcrpQD 2312
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 746 KNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYATGDLGRRW 823
Cdd:PRK12316 2313 PCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgERLYRTGDLARYR 2392
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 824 SSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQhAGTEQARLVAAIEQQPG--LHSEGIKQELLRHLP 901
Cdd:PRK12316 2393 ADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAaeDLLAELRAWLAARLP 2471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 902 AYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQLNDAGgtecRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNS 981
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAY----VAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHS 2547
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 982 ILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIEIYRREGLTALLSRQHAQTL-----EQDIYLEEHIRPDGlphAN 1056
Cdd:PRK12316 2548 LLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLplshaQQRQWFLWQLEPES---AA 2624
|
1130
....*....|..
gi 37542635 1057 WYQPSVVFLTGA 1068
Cdd:PRK12316 2625 YHLPSALHLRGV 2636
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
459-924 |
7.31e-116 |
|
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: 371.64 E-value: 7.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITsdqqsvegwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNnILWRQRT 618
Cdd:cd17643 81 ADSGPSLLLT--------------------DPD------------DLAYVIYTSGSTGRPKGVVVSHANVLA-LFAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 619 W-PLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLI--DHPFAN 695
Cdd:cd17643 128 WfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVeaADRDGR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 DCRAVKLVLSGGEVLNPEL------AHKIQKvwqADVANLYGPTEATIDALYFSI---DKNAAGAIPIGYPIDNTDAYIV 766
Cdd:cd17643 208 DPLALRYVIFGGEALEAAMlrpwagRFGLDR---PQLVNMYGITETTVHVTFRPLdaaDLPAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 767 DLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG--RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHR 844
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPgsRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 845 IELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAI---EQQPGLHSEgIKQELLRHLPAYLIPSQLLLLDELPRTATG 921
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVvadDGAAADIAE-LRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
...
gi 37542635 922 KVD 924
Cdd:cd17643 444 KLD 446
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
1062-1346 |
1.46e-114 |
|
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187546 [Multi-domain] Cd Length: 290 Bit Score: 361.58 E-value: 1.46e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1062 VVFLTGATGYLGLYLIEQLLKRT-TSRVICLCRAKDAEHAKARILEGLKTYR--IDVGSEL*RVEYLTGDLALPHLGLSE 1138
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRKnVSKIYCLVRAKDEEAALERLIDNLKEYGlnLWDELELSRIKVVVGDLSKPNLGLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1139 HQWQTLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPRPFIE-DDAPLRS 1217
Cdd:cd05235 81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEeSDDMLES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1218 AVGVPVGYTGSKWVAEGVANLGLRRGIPVSIFRPGLILGHTETGASQSIDYLLVALRGFLPMGIVPDYPRIFDIVPVDYV 1297
Cdd:cd05235 161 QNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIYPISGAPLDLSPVDWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 37542635 1298 AAAIVHISMQPQGRDKFFHLFNPAPVTIRQFCDWIREFGYEFKLVDFEH 1346
Cdd:cd05235 241 ARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEE 289
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
1063-1426 |
1.55e-114 |
|
thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.
Pssm-ID: 273787 [Multi-domain] Cd Length: 367 Bit Score: 364.81 E-value: 1.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKR-TTSRVICLCRAKDAEHAKARILEGLKTYRIDVGSEL*-RVEYLTGDLALPHLGLSEHQ 1140
Cdd:TIGR01746 2 VLLTGATGFLGAYLLEELLRRsTRAKVICLVRADSEEHAMERLREALRSYRLWHENLAMeRIEVVAGDLSKPRLGLSDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1141 WQTLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPRPFIEDDAPLRSAVG 1220
Cdd:TIGR01746 82 WERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVTEDDATVTPYPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1221 VPVGYTGSKWVAEGVANLGLRRGIPVSIFRPGLILGHTETGASQSIDYLLVALRGFLPMGIVPDYPRI-FDIVPVDYVAA 1299
Cdd:TIGR01746 162 LAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQSPELtEDLTPVDFVAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1300 AIVHISMQPQGRD--KFFHLFNPAPVTIRQFCDWIREFGYEFKLVDFEHGRQQALSVP---PGHLLYPLVPLIRDADPLP 1374
Cdd:TIGR01746 242 AIVALSSRPAASAggIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLEDSDtakRDSRRYPLLPLLHFTGDAF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 1375 hRALDPDyihevNPALECKQTLELLASSDITLSKTTKAYAHTILRYLIDTGF 1426
Cdd:TIGR01746 322 -ESDETD-----TRNLDSRSTAEALEGDGIREPSITAPLLHLYLQYLKEIGF 367
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
459-924 |
1.56e-114 |
|
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: 368.91 E-value: 1.56e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITsDQQSVEGWPQVARIRMEALDPDIRW--VAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQ 616
Cdd:cd12114 81 ADAGARLVLT-DGPDAQLDVAVFDVLILDLDALAAPapPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 617 RTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN- 695
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAq 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 -DCRAVKLVLSGGEVLNPELAHKIQKVW-QADVANLYGPTEATIDALYFSIDKNAA--GAIPIGYPIDNTDAYIVDLNLN 771
Cdd:cd12114 240 aLLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSIYHPIDEVPPdwRSIPYGRPLANQRYRVLDPRGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 772 PVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGnGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVA 851
Cdd:cd12114 320 DCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDG-ERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 852 HLLCQALELKEAIVfAQHAGTEQARLVAAIEQQPG---LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd12114 399 AALQAHPGVARAVV-VVLGDPGGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
459-928 |
3.25e-114 |
|
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: 366.58 E-value: 3.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITSdqqsvegwpqvarirmealdPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRT 618
Cdd:cd17652 81 ADARPALLLTT--------------------PD------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 619 WPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIdhpfANDCR 698
Cdd:cd17652 129 FDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALP----PDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 AVKLVLSGGEVLNPELAHKiqkvWQAD--VANLYGPTEATIDALYFSIDKnAAGAIPIGYPIDNTDAYIVDLNLNPVPPG 776
Cdd:cd17652 205 DLRTLVVAGEACPAELVDR----WAPGrrMINAYGPTETTVCATMAGPLP-GGGVPPIGRPVPGTRVYVLDARLRPVPPG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 777 VPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLL 854
Cdd:cd17652 280 VPGELYIAGAGLARGYLNRPGLTAERFVADPFGApgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAAL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 855 CQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd17652 360 TEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
201-1430 |
5.38e-111 |
|
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: 383.26 E-value: 5.38e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 201 QWGIGLQAPAATEIPTENPRPAIKGS-----DRQVHEALTAWGDQPVAEAEIVSSWLTVLMRWQGSQSAlcAIKVRDKAH 275
Cdd:TIGR03443 1 RWSERLDNPTLSVLPHDYLRPANNRLveatySLQLPSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDI--VLGTSSNKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 276 ANLigplqtyLPVRVDMPDGSTLAQLRLQV---EEQLNGNDHPSFSTLLEVCPPKRDLSRTP-YFQTGLQFiAHDVEQRD 351
Cdd:TIGR03443 79 GRP-------FVLRLNITPELSFLQLYAKVseeEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQD-APDNQQTT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 352 FHAGNLTrlptkqpssDLDLFIScwVSDGTLGLTLDYDCAVLNSSQVEVLAQAL---ISVLSAPGEQPIATVALMGQQmQ 428
Cdd:TIGR03443 151 YSTGSTT---------DLTVFLT--PSSPELELSIYYNSLLFSSDRITIVADQLaqlLSAASSNPDEPIGKVSLITPS-Q 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 429 QTVLaqahgPRTTPpQLTLTEWV-------AASTEKSPLAVAVI---------DHGQQLSYAELWARAALVAANISQHVA 492
Cdd:TIGR03443 219 KSLL-----PDPTK-DLDWSGFRgaihdifADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 493 KPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDR-IQFL----------IENSGC-----------ELVITS- 549
Cdd:TIGR03443 293 KRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLsvakpralivIEKAGTldqlvrdyidkELELRTe 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 550 -------DQQSVEGwpqvARIRMEALDPDIRWVA----PTG--LSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQ 616
Cdd:TIGR03443 373 ipalalqDDGSLVG----GSLEGGETDVLAPYQAlkdtPTGvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 617 RTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVladVRTMED---STALLDLMIRHDVSVLGGVPS---LLGTLID 690
Cdd:TIGR03443 449 KRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL---VPTADDigtPGRLAEWMAKYGATVTHLTPAmgqLLSAQAT 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 691 HPFAndcrAVKLVLSGGEVLNPELAHKIQKVWQ-ADVANLYGPTEATIDALYFSID---------KNAAGAIPIGYPIDN 760
Cdd:TIGR03443 526 TPIP----SLHHAFFVGDILTKRDCLRLQTLAEnVCIVNMYGTTETQRAVSYFEIPsrssdstflKNLKDVMPAGKGMKN 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVDLNLNPVPPGVP--GEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN-----------------------GRVYA 815
Cdd:TIGR03443 602 VQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDpshwidldkennkperefwlgprDRLYR 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 816 TGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQP---------- 885
Cdd:TIGR03443 682 TGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDksdeleefks 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 886 -------------GLHS-----EGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL-----DQLAAPQLNDAGGT 942
Cdd:TIGR03443 762 evddeessdpvvkGLIKyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALpfpdtAQLAAVAKNRSASA 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 943 EcRAPRTDLEQSVMTDFAQVL--GLTAVTPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIEIY 1020
Cdd:TIGR03443 842 A-DEEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRL 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1021 RREGLTALL----SRQHAQTLEQDIYLEEHIRPDGLP-------HANWYQPSVVFLTGATGYLGLYLIEQLLKRTTSR-- 1087
Cdd:TIGR03443 921 KKGEELADEgdseIEEEETVLELDYAKDAKTLVDSLPksypsrkELDASTPITVFLTGATGFLGSFILRDLLTRRSNSnf 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1088 -VICLCRAKDAEHAKARILEGLKTYRIDVGSEL*RVEYLTGDLALPHLGLSEHQWQTLAEEVDVIYHNGALVNFVYPYSA 1166
Cdd:TIGR03443 1001 kVFAHVRAKSEEAGLERLRKTGTTYGIWDEEWASRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSK 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1167 LKATNVGGTQAILELACTARLKSVQYVSTVDTLLATH---------------VPrpfiEDDAPLRSAVGVPVGYTGSKWV 1231
Cdd:TIGR03443 1081 LRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYyvnlsdelvqaggagIP----ESDDLMGSSKGLGTGYGQSKWV 1156
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1232 AEGVANLGLRRGIPVSIFRPGLILGHTETGASQSIDYLLVALRGFLPMGIVPDYPRIFDIVPVDYVAAAIVHISMQPQGR 1311
Cdd:TIGR03443 1157 AEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNTDDFLLRMLKGCIQLGLIPNINNTVNMVPVDHVARVVVAAALNPPKE 1236
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1312 DKF--FHLFNPAPVTIRQFCDWIREFGYEFKLVDFEHGR----QQALSVPPGHLLYPLVPLIRDADPLPHRAldpdyihe 1385
Cdd:TIGR03443 1237 SELavAHVTGHPRIRFNDFLGTLKTYGYDVEIVDYVHWRksleRFVIERSEDNALFPLLHFVLDDLPQSTKA-------- 1308
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 1386 vnPALECKQTLELL----ASSDITLSKTTKAYAHTI---LRYLIDTGFMAKP 1430
Cdd:TIGR03443 1309 --PELDDTNAATSLkadaAWTGVDVSSGAGVTEEQIgiyIAYLVKVGFLPAP 1358
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
459-924 |
4.24e-110 |
|
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: 355.91 E-value: 4.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITSDQQSvegwpqvarirmealdpdirwvaptglshsdAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRT 618
Cdd:cd17649 81 EDSGAGLLLTHHPRQ-------------------------------LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 619 WPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTL---IDHPFAN 695
Cdd:cd17649 130 YGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLaeeADRTGDG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 DCRAVKLVLSGGEVLNPELAHKIQKvwqADVA--NLYGPTEATIDALYFSI---DKNAAGAIPIGYPIDNTDAYIVDLNL 770
Cdd:cd17649 210 RPPSLRLYIFGGEALSPELLRRWLK---APVRlfNAYGPTEATVTPLVWKCeagAARAGASMPIGRPLGGRSAYILDADL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 771 NPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELN 848
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApgSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 849 EVAHLLCQALELKEAIVFAQHAGTEQ---ARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDGAGGKqlvAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
447-933 |
4.81e-107 |
|
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: 348.38 E-value: 4.81e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 447 LTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPID 526
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITSDqqsvegwpqvarirmealdpdirwvaptglsHSDAAYLIYTSGSTGVPKGVVVEHR 606
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTSS-------------------------------PSDAAYVIFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 607 QVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTI-VLADVRTMEDstaLLDLMIRHDVSVLGGVPSLL 685
Cdd:cd05918 130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcIPSEEDRLND---LAGFINRLRVTWAFLTPSVA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 686 GTLidHPfaNDCRAVKLVLSGGEVLNPELAHKiqkvWQADVA--NLYGPTEATIDALYFSIDKNAAGAIpIGYPIDNTdA 763
Cdd:cd05918 207 RLL--DP--EDVPSLRTLVLGGEALTQSDVDT----WADRVRliNAYGPAECTIAATVSPVVPSTDPRN-IGRPLGAT-C 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 764 YIVDLNLN--PVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPF--------GNGRVYATGDLGRRWSSGAISYLGR 833
Cdd:cd05918 277 WVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 834 RDQQVKIRGHRIELNEV-AHLLCQALELKEAIVFA-QHA-GTEQARLVAAIEQQPGLHSEG------------------- 891
Cdd:cd05918 357 KDTQVKIRGQRVELGEIeHHLRQSLPGAKEVVVEVvKPKdGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefralvae 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 37542635 892 IKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAA 933
Cdd:cd05918 437 LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
453-930 |
1.90e-105 |
|
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: 342.37 E-value: 1.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 453 ASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTD 532
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 533 RIQFLIENSGCELVITSDqqsvegwpqvarirmealdpdirwvaptglSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI 612
Cdd:cd17653 85 RIQAILRTSGATLLLTTD------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 613 LWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADvrTMEDSTALLDlmirhDVSVLGGVPSLLGTLIDHP 692
Cdd:cd17653 135 SQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD--PSDPFAHVAR-----TVDALMSTPSILSTLSPQD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 693 FANdcraVKLVLSGGEVLNPELAHKiqkvWQADVA--NLYGPTEATIDALYFSIDknAAGAIPIGYPIDNTDAYIVDLNL 770
Cdd:cd17653 208 FPN----LKTIFLGGEAVPPSLLDR----WSPGRRlyNAYGPTECTISSTMTELL--PGQPVTIGKPIPNSTCYILDADL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 771 NPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNE 849
Cdd:cd17653 278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGsRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 850 VahllcqalelkEAIVFAQHAGTEQA-------RLVAAIEQQpGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGK 922
Cdd:cd17653 358 I-----------EEVVLQSQPEVTQAaaivvngRLVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425
|
....*...
gi 37542635 923 VDMLKLDQ 930
Cdd:cd17653 426 VDRKALRE 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-983 |
3.23e-105 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 371.81 E-value: 3.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQLAgtatlPVTVRY------AFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVK 100
Cdd:PRK05691 1730 PLSYSQQRMWFLWQME-----PDSPAYnvggmaRLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLR 1804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 101 LEY--FDRPPSDADMAELIGAA-------FELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLfqtepdh 171
Cdd:PRK05691 1805 MDWqdFSALPADARQQRLQQLAdseahqpFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFAREL------- 1877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 172 qypavGAIAEVF--QREQTLAQ-DAQITE--QWQ-QW---------------GIGLQAPAaTEIPTENPRPAIkgsdrQV 230
Cdd:PRK05691 1878 -----GALYEAFldDRESPLEPlPVQYLDysVWQrQWlesgerqrqldywkaQLGNEHPL-LELPADRPRPPV-----QS 1946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 231 HEALTAWGDQPVAEAEIVSSW-----LTVLM-----------RWQGSQS----ALCAIKVRDKAHAnLIGP-LQT-YLPV 288
Cdd:PRK05691 1947 HRGELYRFDLSPELAARVRAFnaqrgLTLFMtmtatlaallyRYSGQRDlrigAPVANRIRPESEG-LIGAfLNTqVLRC 2025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 289 RVD--MPDGSTLAQLRLQVEEQLNGNDHPsFSTLLEVCPPKRDLSRTPYFQTGLQFIAHDVEQRDFHAG-NLTRLPTKQP 365
Cdd:PRK05691 2026 QLDgqMSVSELLEQVRQTVIEGQSHQDLP-FDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRQLAGmTVEYLVNDAR 2104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 366 SSDLDLFISCWVSDGTLGLTLDYDCAVLNSSQVEVLA---QALISVLSAPGEQPIATVALMGQQMQQTVLAQAHG-PRTT 441
Cdd:PRK05691 2105 ATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAehwQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGeAGEA 2184
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 442 PPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHA 521
Cdd:PRK05691 2185 RLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 522 FLPIDPRLPTDRIQFLIENSGCELVItSDQQSVEGWPQ----VARIRME----ALD--PDIRWVAPTGLSHSdaAYLIYT 591
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLL-SDRALFEALGElpagVARWCLEddaaALAaySDAPLPFLSLPQHQ--AYLIYT 2341
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 592 SGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLAdVRTMEDSTALLDLMI 671
Cdd:PRK05691 2342 SGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLR-AQGQWGAEEICQLIR 2420
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 672 RHDVSVLGGVPSLLGTLIDHPFANDCR-AVKLVLSGGEVLNPELAHKIQKVWQADVA-NLYGPTEATI---DALYFSIDK 746
Cdd:PRK05691 2421 EQQVSILGFTPSYGSQLAQWLAGQGEQlPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETVVmplACLAPEQLE 2500
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 747 NAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGN--GRVYATGDLGRRWS 824
Cdd:PRK05691 2501 EGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdgGRLYRTGDLVRLRA 2580
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 825 SGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA-------QHAGTEQARLVAAIEQQPGLHSEGIKQELL 897
Cdd:PRK05691 2581 DGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAldtpsgkQLAGYLVSAVAGQDDEAQAALREALKAHLK 2660
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 898 RHLPAYLIPSQLLLLDELPRTATGkvdmlKLDQLAAPQLNDAGGTEC-RAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFE 976
Cdd:PRK05691 2661 QQLPDYMVPAHLILLDSLPLTANG-----KLDRRALPAPDPELNRQAyQAPRSELEQQLAQIWREVLNVERVGLGDNFFE 2735
|
....*..
gi 37542635 977 QGGNSIL 983
Cdd:PRK05691 2736 LGGDSIL 2742
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
456-924 |
7.62e-104 |
|
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: 339.03 E-value: 7.62e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:cd17644 11 ERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITSdqqsvegwpqvarirmealdpdirwvaPTGLshsdaAYLIYTSGSTGVPKGVVVEHRQVVNNILWR 615
Cdd:cd17644 91 YILEDAQISVLLTQ---------------------------PENL-----AYVIYTSGSTGKPKGVMIEHQSLVNLSHGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 616 QRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN 695
Cdd:cd17644 139 IKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 DC---RAVKLVLSGGEVLNPELAHKIQKVWQADVA--NLYGPTEATIDALYFSIDKNAAGAI---PIGYPIDNTDAYIVD 767
Cdd:cd17644 219 TIdlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPTEATIAATVCRLTQLTERNItsvPIGRPIANTQVYILD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 768 LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG---RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHR 844
Cdd:cd17644 299 ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSeseRLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 845 IELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAI--EQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGK 922
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIvpHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGK 458
|
..
gi 37542635 923 VD 924
Cdd:cd17644 459 ID 460
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
459-924 |
9.69e-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: 338.29 E-value: 9.69e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITsdqqsvegwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNIL-WRQR 617
Cdd:cd17650 81 EDSGAKLLLT--------------------QPE------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHaWRRE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 618 TWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN-- 695
Cdd:cd17650 129 YELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNgl 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 DCRAVKLVLSGGEVLNPElahkiQKVWQAD-------VANLYGPTEATIDALYFSIDKNA---AGAIPIGYPIDNTDAYI 765
Cdd:cd17650 209 DLSAMRLLIVGSDGCKAQ-----DFKTLAArfgqgmrIINSYGVTEATIDSTYYEEGRDPlgdSANVPIGRPLPNTAMYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 766 VDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHR 844
Cdd:cd17650 284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGeRMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 845 IELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
447-939 |
1.89e-102 |
|
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: 334.86 E-value: 1.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 447 LTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPID 526
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITsdqqsvegwpqvarirmealdpdirwvaptglshsdaAYLIYTSGSTGVPKGVVVEHR 606
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT-------------------------------------ALILYTSGTTGRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 607 QVVNNILWRQRTWPLTAQDNVLH----NHSFSFdpsVWALFWPLLTGGTIVLADVRTMEdstALLDLMIRHDVSVLGGVP 682
Cdd:COG0318 124 NLLANAAAIAAALGLTPGDVVLValplFHVFGL---TVGLLAPLLAGATLVLLPRFDPE---RVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 683 SLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAIPIGYPIDN 760
Cdd:COG0318 198 TMLARLLRHPEFAryDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKI 840
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 841 RGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRT 918
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGaeLDAEELRAFLRERLARYKVPRRVEFVDELPRT 431
|
490 500
....*....|....*....|.
gi 37542635 919 ATGKVDMLKLDQLAAPQLNDA 939
Cdd:COG0318 432 ASGKIDRRALRERYAAGALEA 452
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
1062-1326 |
4.17e-102 |
|
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 442549 [Multi-domain] Cd Length: 265 Bit Score: 326.39 E-value: 4.17e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1062 VVFLTGATGYLGLYLIEQLLKRTTSRVICLCRAKDAEHAKARILEGLKTYRIDVGSEL*RVEYLTGDLALPHLGLSEHQW 1141
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERYGLWLELDASRVVVVAGDLTQPRLGLSEAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1142 QTLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVDTllATHVPRPFIEDDAPLRSAVGV 1221
Cdd:COG3320 82 QELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAV--AGPADRSGVFEEDDLDEGQGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1222 PVGYTGSKWVAEGVANLGLRRGIPVSIFRPGLILGHTETGASQSIDYLLVALRGFLPMGIVPDYPRI-FDIVPVDYVAAA 1300
Cdd:COG3320 160 ANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPGLGDArLNLVPVDYVARA 239
|
250 260
....*....|....*....|....*.
gi 37542635 1301 IVHISMQPQGRDKFFHLFNPAPVTIR 1326
Cdd:COG3320 240 IVHLSRQPEAAGRTFHLTNPQPLSLG 265
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
456-928 |
2.79e-100 |
|
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: 328.44 E-value: 2.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITsdqqsvegwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWR 615
Cdd:cd05945 82 EILDAAKPALLIA--------------------DGD------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 616 QRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPfaN 695
Cdd:cd05945 130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSP--T 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 DCRA----VKLVLSGGEVLNPELAHKIQKVW-QADVANLYGPTEATIDALYFSIDK---NAAGAIPIGYPIDNTDAYIVD 767
Cdd:cd05945 208 FTPEslpsLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTPevlDGYDRLPIGYAKPGAKLVILD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 768 LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIEL 847
Cdd:cd05945 288 EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE--GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIEL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 848 NEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEG---IKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd05945 366 EEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLtkaIKAELAERLPPYMIPRRFVYLDELPLNANGKID 445
|
....
gi 37542635 925 MLKL 928
Cdd:cd05945 446 RKAL 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
456-924 |
4.28e-96 |
|
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: 316.80 E-value: 4.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:cd17645 9 ERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITsdqqsvegwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWR 615
Cdd:cd17645 89 YMLADSSAKILLT--------------------NPD------------DLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 616 QRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVlggvpSLLGTLIDHPF-A 694
Cdd:cd17645 137 RPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI-----SFLPTGAAEQFmQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 695 NDCRAVKLVLSGGEVLNpelaHKIQKVWQadVANLYGPTEATIDALYFSIDKnAAGAIPIGYPIDNTDAYIVDLNLNPVP 774
Cdd:cd17645 212 LDNQSLRVLLTGGDKLK----KIERKGYK--LVNNYGPTENTVVATSFEIDK-PYANIPIGKPIDNTRVYILDEALQLQP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 775 PGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHL 853
Cdd:cd17645 285 IGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGeRMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPF 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37542635 854 LCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17645 365 LMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
456-841 |
1.07e-95 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 314.64 E-value: 1.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAV-IDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRI 534
Cdd:pfam00501 6 ARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 535 QFLIENSGCELVITSDQQSVE---------------------GWPQVARIRMEALDPDIRWVAPTGLSHSDAAYLIYTSG 593
Cdd:pfam00501 86 AYILEDSGAKVLITDDALKLEellealgklevvklvlvldrdPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 594 STGVPKGVVVEHRQVVNNILW----RQRTWPLTAQDNVLHNHSFSFDPSV-WALFWPLLTGGTIVLADVRTMEDSTALLD 668
Cdd:pfam00501 166 TTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDPAALLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 669 LMIRHDVSVLGGVPSLLGTLIDHPFANDCR--AVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDK 746
Cdd:pfam00501 246 LIERYKVTVLYGVPTLLNMLLEAGAPKRALlsSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 747 NAAGAIP-IGYPIDNTDAYIVD-LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPnpfgnGRVYATGDLGRRWS 824
Cdd:pfam00501 326 EDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-----DGWYRTGDLGRRDE 400
|
410
....*....|....*..
gi 37542635 825 SGAISYLGRRDQQVKIR 841
Cdd:pfam00501 401 DGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
458-928 |
1.67e-93 |
|
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: 310.95 E-value: 1.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 458 SPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFL 537
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 538 IENSGCELVITsdQQSVEGWPQVARIRMEALDPDIRWVAPTGLSHS----DAAYLIYTSGSTGVPKGVVVEHRQVVNNIL 613
Cdd:cd17656 81 MLDSGVRVVLT--QRHLKSKLSFNKSTILLEDPSISQEDTSNIDYInnsdDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 614 WRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGgVPSLLGTLI--DH 691
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF-LPVAFLKFIfsER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 692 PFAND-CRAVKLVLSGGE--VLNPELAHKIQKvWQADVANLYGPTEATIDALY-FSIDKNAAGAIPIGYPIDNTDAYIVD 767
Cdd:cd17656 238 EFINRfPTCVKHIITAGEqlVITNEFKEMLHE-HNVHLHNHYGPSETHVVTTYtINPEAEIPELPPIGKPISNTWIYILD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 768 LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPF-GNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIE 846
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 847 LNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDML 926
Cdd:cd17656 397 LGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
..
gi 37542635 927 KL 928
Cdd:cd17656 477 AL 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
459-928 |
1.09e-92 |
|
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: 307.40 E-value: 1.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARA-ALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFL 537
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERAnRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 538 IENSGCELVITSDqqsvegwpqvarirmealdpdirwvaptglshSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQR 617
Cdd:cd17648 81 LEDTGARVVITNS--------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 618 TWPLTAQDN--VLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLgTLIDhpFAN 695
Cdd:cd17648 129 RYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL-QQYD--LAR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 dCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPP 775
Cdd:cd17648 206 -LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 776 GVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFG---------NGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIE 846
Cdd:cd17648 285 GAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 847 LNEVAHLLCQALELKEAIVFA-----QHAGTEQARLVAAIEQQPGLHSEG-IKQELLRHLPAYLIPSQLLLLDELPRTAT 920
Cdd:cd17648 365 PGEVEAALASYPGVRECAVVAkedasQAQSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPVTIN 444
|
....*...
gi 37542635 921 GKVDMLKL 928
Cdd:cd17648 445 GKLDVRAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-1018 |
8.02e-89 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 320.96 E-value: 8.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 10 EAALRSLP-AARDALGAYPLSSEQKRLWLLAQL-AGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFV-EVL 86
Cdd:PRK05691 3241 QAQLDALPvPAAEIEDVYPLTPMQEGLLLHTLLePGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSwNAG 3320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 87 ERPVRLLMPTGLVKLEYFD-RPPSDADMAELIGA--------AFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSL 157
Cdd:PRK05691 3321 ETMLQVIHKPGRTPIDYLDwRGLPEDGQEQRLQAlhkqereaGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCR 3400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 158 QRIAQTLFQTepdhqYPAVGAiaevfQREQTLA--------------QDAQITEQWqqWGIGLQA-PAATEIPTENP--- 219
Cdd:PRK05691 3401 SLLMNDFFEI-----YTALGE-----GREAQLPvppryrdyigwlqrQDLAQARQW--WQDNLRGfERPTPIPSDRPflr 3468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 220 RPAIKGSDRQVHEALT-------------AWGDQPVAEAEIVSSWLTVLMRWQGSQSALCAIKVRDK-----AHANLIGP 281
Cdd:PRK05691 3469 EHAGDSGGMVVGDCYTrldaadgarlrelAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvsmpQMQRTVGL 3548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 282 LQTYLPVRVDMPDGSTLAQLR------LQVEEQLNGNDHPSFSTLLEVCP-PKRDlsrtPYFQTGLQFIAHDVEqrdfhA 354
Cdd:PRK05691 3549 FINSIALRVQLPAAGQRCSVRqwlqglLDSNMELREYEYLPLVAIQECSElPKGQ----PLFDSLFVFENAPVE-----V 3619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 355 GNLTRLPTKQPSSD-------LDLFISCWVSDgTLGLTLDYDCAVLNSSQVEVLA---QALISVLSAPGEQPIATVALMG 424
Cdd:PRK05691 3620 SVLDRAQSLNASSDsgrthtnFPLTAVCYPGD-DLGLHLSYDQRYFDAPTVERLLgefKRLLLALVQGFHGDLSELPLLG 3698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 425 QQMQQTVLAQA-HGPRTTPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARA-----ALVAANISqhVAKPRSII 498
Cdd:PRK05691 3699 EQERDFLLDGCnRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAAnrlghALRAAGVG--VDQPVALL 3776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 499 AvalPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQSVEG-----------------WPQVA 561
Cdd:PRK05691 3777 A---ERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQAralldelgcanrprllvWEEVQ 3853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 562 RIRMEALDPDIrWVAPTGLshsdaAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWA 641
Cdd:PRK05691 3854 AGEVASHNPGI-YSGPDNL-----AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQ 3927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 642 LFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLL-GTLIDHPFANDcrAVKLVLSGGEVLNPELAHK-IQ 719
Cdd:PRK05691 3928 FLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIqGMLAEDRQALD--GLRWMLPTGEAMPPELARQwLQ 4005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 720 KVWQADVANLYGPTEATIDALYFSIDKNA-AGA-IPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPA 797
Cdd:PRK05691 4006 RYPQIGLVNAYGPAECSDDVAFFRVDLAStRGSyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPL 4085
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 798 QTAQRFLPNPFG--NGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEV-AHLLCQAlELKEAIVFAQhAGTEQ 874
Cdd:PRK05691 4086 RTALAFVPHPFGapGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIeARLHEQA-EVREAAVAVQ-EGVNG 4163
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 875 ARLVAAI-----EQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMlklDQLAAPQLNDAGGTECRAPRT 949
Cdd:PRK05691 4164 KHLVGYLvphqtVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR---KALPALDIGQLQSQAYLAPRN 4240
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 950 DLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIE 1018
Cdd:PRK05691 4241 ELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
456-930 |
2.01e-76 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 263.16 E-value: 2.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:TIGR01734 11 ETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITSDQQSVEgWPQVARIRMEALDPDIRWVAPTGLSH----SDAAYLIYTSGSTGVPKGVVVEHRQVVNN 611
Cdd:TIGR01734 91 MIIEAAGPELVIHTAELSID-AVGTQIITLSALEQAETSGGPVSFDHavkgDDNYYIIYTSGSTGNPKGVQISHDNLVSF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 612 ILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADvRTMEDSTALLDLMI-RHDVSVLGGVPSLLG-TLI 689
Cdd:TIGR01734 170 TNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLD-KDITNNFKLLFEELpKTGLNVWVSTPSFVDmCLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 690 DHPFANDC--RAVKLVLSgGEVLNPELAHK-IQKVWQADVANLYGPTEATIDALYFSIDK---NAAGAIPIGYPIDNTDA 763
Cdd:TIGR01734 249 DPNFNQENypHLTHFLFC-GEELPVKTAKAlLERFPKATIYNTYGPTEATVAVTSVKITQeilDQYPRLPIGFAKPDMNL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 764 YIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpNPFGNGRVYATGDLGrRWSSGAISYLGRRDQQVKIRGH 843
Cdd:TIGR01734 328 FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF--FSHEGQPAYRTGDAG-TITDGQLFYQGRLDFQIKLHGY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 844 RIELNEVAHLLCQALELKEAIVFAQHAGTEQ-ARLVAAIEQQPG------LHSEGIKQELLRHLPAYLIPSQLLLLDELP 916
Cdd:TIGR01734 405 RIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEdfekefQLTKAIKKELKKSLPAYMIPRKFIYRDQLP 484
|
490
....*....|....
gi 37542635 917 RTATGKVDMLKLDQ 930
Cdd:TIGR01734 485 LTANGKIDRKALAE 498
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
1065-1301 |
2.16e-73 |
|
Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.
Pssm-ID: 462334 [Multi-domain] Cd Length: 257 Bit Score: 245.21 E-value: 2.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1065 LTGATGYLGLYLIEQLLKRTT--SRVICLCRAKDAEHAKARILEGLKTYRI---DVGSEL*RVEYLTGDLALPHLGLSEH 1139
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRSTPdvKKIYLLVRAKDGESALERLRQELEKYPLfdaLLKEALERIVPVAGDLSEPNLGLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1140 QWQTLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTAR-LKSVQYVST--VDTLLATHVPRPF-------- 1208
Cdd:pfam07993 81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKqLKPFHHVSTayVNGERGGLVEEKPypegeddm 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1209 IEDDAPLRSAVGVPVGYTGSKWVAEGVANLGLRRGIPVSIFRPGLILGHTETGASQSIDYLLVALRGFLPMGIVPDYP-- 1286
Cdd:pfam07993 161 LLDEDEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSILgd 240
|
250
....*....|....*..
gi 37542635 1287 --RIFDIVPVDYVAAAI 1301
Cdd:pfam07993 241 pdAVLDLVPVDYVANAI 257
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
456-924 |
9.59e-71 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 246.73 E-value: 9.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:PRK04813 13 QTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITSDQQSVEGwPQVARIRMEALDPDIRWVAPTGLSHS----DAAYLIYTSGSTGVPKGVVVEHrqvvNN 611
Cdd:PRK04813 93 MIIEVAKPSLIIATEELPLEI-LGIPVITLDELKDIFATGNPYDFDHAvkgdDNYYIIFTSGTTGKPKGVQISH----DN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 612 IL----WRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADvRTMEDSTALLDLMIRH-DVSVLGGVPSllg 686
Cdd:PRK04813 168 LVsftnWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALP-KDMTANFKQLFETLPQlPINVWVSTPS--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 687 tlidhpFANDCravkLVLSG-GEVLNP----------ELAHK-----IQKVWQADVANLYGPTEATIDALYFSIDK---N 747
Cdd:PRK04813 244 ------FADMC----LLDPSfNEEHLPnlthflfcgeELPHKtakklLERFPSATIYNTYGPTEATVAVTSIEITDemlD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 748 AAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpNPFGNGRVYATGDLGrRWSSGA 827
Cdd:PRK04813 314 QYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF--FTFDGQPAYHTGDAG-YLEDGL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 828 ISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSE------GIKQELLRHLP 901
Cdd:PRK04813 391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFERefeltkAIKKELKERLM 470
|
490 500
....*....|....*....|...
gi 37542635 902 AYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK04813 471 EYMIPRKFIYRDSLPLTPNGKID 493
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
584-924 |
2.51e-66 |
|
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: 227.94 E-value: 2.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADvrtMEDS 663
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 664 TALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALY 741
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAgyDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 742 FSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQrflpnPFGNGRvYATGDLGR 821
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-----VDEDGW-YRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 822 RWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRH 899
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGadLDAEELRAHVRER 311
|
330 340
....*....|....*....|....*
gi 37542635 900 LPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
452-928 |
5.61e-60 |
|
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: 213.96 E-value: 5.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 452 AASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPT 531
Cdd:cd05936 6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 532 DRIQFLIENSGCELVITsdqqsVEGWPQVarirMEALDPDIRWVAPTGlshSDAAYLIYTSGSTGVPKGVVVEHRQVVNN 611
Cdd:cd05936 86 RELEHILNDSGAKALIV-----AVSFTDL----LAAGAPLGERVALTP---EDVAVLQYTSGTTGVPKGAMLTHRNLVAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 612 IL--WRQRTWPLTAQDNVLHN----HSFSFdpSVwALFWPLLTGGTIVLadVRTMEDSTaLLDLMIRHDVSVLGGVPSLL 685
Cdd:cd05936 154 ALqiKAWLEDLLEGDDVVLAAlplfHVFGL--TV-ALLLPLALGATIVL--IPRFRPIG-VLKEIRKHRVTIFPGVPTMY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 686 GTLIDHP--FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT-IDALYFSIDKNAAGAIpiGYPIDNTD 762
Cdd:cd05936 228 IALLNAPefKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSI--GIPLPGTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 763 AYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpnpfgNGRVYaTGDLGRRWSSGAISYLGRRDQQVKIRG 842
Cdd:cd05936 306 VKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-----DGWLR-TGDIGYMDEDGYFFIVDRKKDMIIVGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 843 HRIELNEVAHLLCQALELKEAIV---FAQHAGTEqarLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPR 917
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVvgvPDPYSGEA---VKAFVVLKEGasLTEEEIIAFCREQLAGYKVPRQVEFRDELPK 456
|
490
....*....|.
gi 37542635 918 TATGKVDMLKL 928
Cdd:cd05936 457 SAVGKILRREL 467
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
446-924 |
3.23e-56 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 204.63 E-value: 3.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 446 TLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPI 525
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 526 DPRLPTDRIQFLIENSGCELVITSDQ-------------------------QSVEGWPQVARIRMEALDPDIRWVAPTGL 580
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSErldllhpalpgchdlrtliivgdpaHASEGHPGEEPASWPKLLALGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 581 SHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTM 660
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 661 EDstaLLDLMIRHDVSVLGGVPSLLGTL--IDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAtID 738
Cdd:TIGR03098 241 RD---VLKALEKHGITGLAAVPPLWAQLaqLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEA-FR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 ALYfsIDKNAAGAIP--IGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNGR---- 812
Cdd:TIGR03098 317 STY--LPPEEVDRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGElhlp 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 813 ---VYaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--L 887
Cdd:TIGR03098 395 elaVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGeeL 473
|
490 500 510
....*....|....*....|....*....|....*..
gi 37542635 888 HSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:TIGR03098 474 DRAALLAECRARLPNYMVPALIHVRQALPRNANGKID 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
461-928 |
3.29e-51 |
|
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: 189.06 E-value: 3.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIEN 540
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 541 SGCELVITSDQQSVE---------------GWPQVARIR------MEALDPDIRWVAPTGLSH-SDAAYLIYTSGSTGVP 598
Cdd:cd05926 85 LGSKLVLTPKGELGPasraasklglailelALDVGVLIRapsaesLSNLLADKKNAKSEGVPLpDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 599 KGVVVEHRQVVNNILWRQRTWPLTAQDNVL------HNHSFsfdpsVWALFWPLLTGGTIVLADvrtMEDSTALLDLMIR 672
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfHVHGL-----VASLLSTLAAGGSVVLPP---RFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 673 HDVSVLGGVPSLLGTLIDHPFANDCRA---VKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT--IDALYFSIDKN 747
Cdd:cd05926 237 YNATWYTAVPTIHQILLNRPEPNPESPppkLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 748 AAGAIPIGypiDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGA 827
Cdd:cd05926 317 KPGSVGKP---VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-----FRTGDLGYLDADGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 828 ISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTEqarLVAAIEQQPGLH--SEGIKQELLRHLPA 902
Cdd:cd05926 389 LFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGvpdEKYGEE---VAAAVVLREGASvtEEELRAFCRKHLAA 465
|
490 500
....*....|....*....|....*.
gi 37542635 903 YLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05926 466 FKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
441-923 |
2.63e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 183.95 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 441 TPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGH 520
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 521 AFLPIDPRLPTDRIQFLIENSGCELVIT------SDQQSVEGWPQVARI---RMEALDPDI-------RWVAPT------ 578
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVlglflgVDYSATTRLPALEHVvicETEEDDPHTekmktftDFLAAGdpaera 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 579 -GLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNIlwrqRTWP----LTAQDNVL----HNHSFSFDPSVWAlfwPLLTG 649
Cdd:PRK07656 161 pEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNA----ADWAeylgLTEGDRYLaanpFFHVFGYKAGVNA---PLMRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 650 GTIVLADVRtmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQAD-V 726
Cdd:PRK07656 234 ATILPLPVF---DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSaeDLSSLRLAVTGAASMPVALLERFESELGVDiV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 727 ANLYGPTEATIDALYFSID---KNAAGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRF 803
Cdd:PRK07656 311 LTGYGLSEASGVTTFNRLDddrKTVAGT--IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 804 LPnpfgNGRVYaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQARL----VA 879
Cdd:PRK07656 389 DA----DGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI----GVPDERLgevgKA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 37542635 880 AIEQQPGlhSEGIKQELL----RHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK07656 460 YVVLKPG--AELTEEELIaycrEHLAKYKVPRSIEFLDELPKNATGKV 505
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
463-928 |
2.00e-48 |
|
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: 179.58 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 463 AVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSG 542
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 543 CELVITSDQqsvegwpqvarirmealdpdirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRqvvnNILWRQRTWP-- 620
Cdd:cd05919 83 ARLVVTSAD--------------------------------DIAYLLYSSGTTGPPKGVMHAHR----DPLLFADAMAre 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 621 ---LTAQDNVLHNHSFSFDPSVW-ALFWPLLTGGTIVLADVRTmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPF--A 694
Cdd:cd05919 127 algLTPGDRVFSSAKMFFGYGLGnSLWFPLAVGASAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYANLLDSCAgsP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 695 NDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEatidaLYFSIDKNAAGAIPI---GYPIDNTDAYIVDLNLN 771
Cdd:cd05919 205 DALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATE-----VGHIFLSNRPGAWRLgstGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 772 PVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVA 851
Cdd:cd05919 280 TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 852 HLLCQALELKEAIVFA---QHAGTE-QARLVAAIEQQP-GLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDML 926
Cdd:cd05919 354 SLIIQHPAVAEAAVVAvpeSTGLSRlTAFVVLKSPAAPqESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRF 433
|
..
gi 37542635 927 KL 928
Cdd:cd05919 434 KL 435
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
462-923 |
7.87e-48 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 181.08 E-value: 7.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 462 VAVIDHG-----QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQF 536
Cdd:COG0365 26 VALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 537 LIENSGCELVITSDQQ-----SVEGWPQVARIRMEA-----------------LDPDIRW----------VAPTGLSHSD 584
Cdd:COG0365 106 RIEDAEAKVLITADGGlrggkVIDLKEKVDEALEELpslehvivvgrtgadvpMEGDLDWdellaaasaeFEPEPTDADD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 585 AAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTW-PLTAQDnVLHNHSfsfDPSvWA------LFWPLLTGGTIVLAD- 656
Cdd:COG0365 186 PLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGD-VFWCTA---DIG-WAtghsyiVYGPLLNGATVVLYEg 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 657 VRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLI---DHPFAN-DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGP 732
Cdd:COG0365 261 RPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMkagDEPLKKyDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 733 TEAT--------IDALYfsidknaAGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQN--LARGYLGKPAQTAQR 802
Cdd:COG0365 341 TETGgifisnlpGLPVK-------PGS--MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRET 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 803 FLPNPFGngrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRI----------ELNEVAhllcqalelkEAIVFAQ-HAG 871
Cdd:COG0365 412 YFGRFPG---WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIgtaeiesalvSHPAVA----------EAAVVGVpDEI 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 872 TEQaRLVAAIEQQPGLH-SEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKV 923
Cdd:COG0365 479 RGQ-VVKAFVVLKPGVEpSDELAKELQAHvreeLGPYAYPREIEFVDELPKTRSGKI 534
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
471-928 |
3.21e-47 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 176.12 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD 550
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QQSVEgwpqvARIRM-EALDPDIRwvAPTGLshsdaAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLH 629
Cdd:cd17654 97 ELDNA-----PLSFTpEHRHFNIR--TDECL-----AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 630 NHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLD-LMIRHDVSVLGGVPSLL----GTLIDHPFANDCRAVKLVL 704
Cdd:cd17654 165 TSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFrrfgSQSIKSTVLSATSSLRVLA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 705 SGGE-----VLNPELAHKIQKVwqaDVANLYGPTEATIDALYFSIDKNAAGaIPIGYPIDNTDAYIVDLNLNPvppgVPG 779
Cdd:cd17654 245 LGGEpfpslVILSSWRGKGNRT---RIFNIYGITEVSCWALAYKVPEEDSP-VQLGSPLLGTVIEVRDQNGSE----GTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 780 EIMLAGQNlaRGYlgkpaqtaqrFLPNPFG--NGRVYATGDLGRRwSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQA 857
Cdd:cd17654 317 QVFLGGLN--RVC----------ILDDEVTvpKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 858 LELkEAIVFAQHagtEQARLVAAIEQQPglHSEGIKQELLRH-LPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd17654 384 LGV-ESCAVTLS---DQQRLIAFIVGES--SSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
1063-1363 |
4.97e-46 |
|
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187573 [Multi-domain] Cd Length: 293 Bit Score: 167.93 E-value: 4.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRTtSRVICLCRAKDAEHAKARILEGlktyridvGSEL*RVEYLTGDLALPHLGLSEHQWQ 1142
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLENG-FKVLVLVRSESLGEAHERIEEA--------GLEADRVRVLEGDLTQPNLGLSAAASR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 TLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVdtllATHVPRPFIEDDAPLRSAVGVP 1222
Cdd:cd05263 72 ELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTA----YVAGNREGNIRETELNPGQNFK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1223 VGYTGSKWVAEGVanlgLRR---GIPVSIFRPGLILGHTETGASQSIDYLLVALRGFLPMGIVPDYPRI----FDIVPVD 1295
Cdd:cd05263 148 NPYEQSKAEAEQL----VRAaatQIPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRWLPMPGNkgarLNLVPVD 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 1296 YVAAAIVHISMQPQGRDKFFHLFNPAPVTIRQFCDWI-REFGYEFKLVDFEHgrQQALSVPPGHLLYPL 1363
Cdd:cd05263 224 YVADAIVYLSKKPEANGQIFHLTDPTPQTLREIADLFkSAFLSPGLLVLLMN--EPNASLPNALRRSLL 290
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
457-924 |
1.23e-44 |
|
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: 168.17 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 457 KSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQF 536
Cdd:cd17631 7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 537 LIENSGCELVItsdqqsvegwpqvarirmealdpdirwvaptglshSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQ 616
Cdd:cd17631 87 ILADSGAKVLF-----------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 617 RTWPLTAQDNVLHN----HSFSFDpsVWALFWpLLTGGTIVLadvrtME--DSTALLDLMIRHDVSVLGGVPSLLGTLID 690
Cdd:cd17631 132 AALDLGPDDVLLVVaplfHIGGLG--VFTLPT-LLRGGTVVI-----LRkfDPETVLDLIERHRVTSFFLVPTMIQALLQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 691 HPFAN--DCRAVKLVLSGGEVLNPELAHKIQkVWQADVANLYGPTEATIDALYFSIDKNAAGAIPIGYPIDNTDAYIVDL 768
Cdd:cd17631 204 HPRFAttDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 769 NLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQrflpnPFGNGRVYaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELN 848
Cdd:cd17631 283 DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-----AFRDGWFH-TGDLGRLDEDGYLYIVDRKKDMIISGGENVYPA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 849 EVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGlhSEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17631 357 EVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG--AELDEDELIAHcrerLARYKIPKSVEFVDALPRNATGKIL 434
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
444-924 |
8.88e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 168.06 E-value: 8.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 444 QLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFL 523
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 524 PIDPRLPTDRIQFLIENSGCELVITSDqqsvEGWPQVARIR--MEAL-------DPDIRWVAPTGLSHS----------- 583
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDS----EFVPLLAAILpqLPTVrtvivegDGPAAPLAPEVGEYEellaaasdtfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 -------DAAYLIYTSGSTGVPKGVVVEHRQVVNNIL----WRQrtwpLTAQDNVL----HNHSFsfdpsvwALFWP--- 645
Cdd:PRK06187 161 fpdidenDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLavcaWLK----LSRDDVYLvivpMFHVH-------AWGLPyla 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 646 LLTGGTIVLADvRTmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQ 723
Cdd:PRK06187 230 LMAGAKQVIPR-RF--DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfvDFSSLRLVIYGGAALPPALLREFKEKFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 724 ADVANLYGPTEA--TIDALYFSIDKNAAGAIPI--GYPIDNTDAYIVDLNLNPVPP--GVPGEIMLAGQNLARGYLGKPA 797
Cdd:PRK06187 307 IDLVQGYGMTETspVVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 798 QTAQRFLpnpfgNGRvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARL 877
Cdd:PRK06187 387 ATAETID-----GGW-LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERP 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 37542635 878 VAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK06187 461 VAVVVLKPGatLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKIL 509
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
498-928 |
1.13e-43 |
|
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: 166.08 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAGHA----FLPIDPRLPTDRIQFLIENSGCELVI--------TSDQQSVEGWPQVArIRM 565
Cdd:cd05922 21 VVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLadagaadrLRDALPASPDPGTV-LDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 566 EALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWP 645
Cdd:cd05922 100 DGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 646 LLTGGTIVLADVRTMEDstALLDLMIRHDVSVLGGVPSLLGTL--IDHPFANDCRAVKLVLSGG---EVLNPELAHKIQK 720
Cdd:cd05922 180 LLRGATLVLTNDGVLDD--AFWEDLREHGATGLAGVPSTYAMLtrLGFDPAKLPSLRYLTQAGGrlpQETIARLRELLPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 721 vwqADVANLYGPTEATIDALYFSID--KNAAGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAq 798
Cdd:cd05922 258 ---AQVYVMYGQTEATRRMTYLPPEriLEKPGS--IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPP- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 799 taqrFLPNPFGNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQhAGTEQARLV 878
Cdd:cd05922 332 ----YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL-PDPLGEKLA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 37542635 879 AAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05922 407 LFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
461-924 |
2.44e-43 |
|
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: 164.77 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAANISQHVAKPR-SIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIE 539
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 540 NSGCELVItsdqqsvegwpqvarirmealdpdirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTW 619
Cdd:cd05941 82 DSEPSLVL------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 620 PLTAQDNVL------HNHSFsfdpsVWALFWPLLTGGTIVLadvrtMEDSTALLDLMIRHD--VSVLGGVPSLLGTLIDH 691
Cdd:cd05941 126 RWTEDDVLLhvlplhHVHGL-----VNALLCPLFAGASVEF-----LPKFDPKEVAISRLMpsITVFMGVPTIYTRLLQY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 692 PFAND----------CRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIdALYFSID-KNAAGAipIGYPIDN 760
Cdd:cd05941 196 YEAHFtdpqfaraaaAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGM-ALSNPLDgERRPGT--VGMPLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVD-LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGR-RDQQV 838
Cdd:cd05941 273 VQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-----FKTGDLGVVDEDGYYWILGRsSVDII 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 839 KIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHS---EGIKQELLRHLPAYLIPSQLLLLDEL 915
Cdd:cd05941 348 KSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAAlslEELKEWAKQRLAPYKRPRRLILVDEL 427
|
....*....
gi 37542635 916 PRTATGKVD 924
Cdd:cd05941 428 PRNAMGKVN 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
463-928 |
7.01e-42 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 162.15 E-value: 7.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 463 AVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSG 542
Cdd:cd05959 22 AFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 543 CELVITSDqqsvEGWPQVArIRMEALDPDIRWV-------------------------APTGLSHSDA-AYLIYTSGSTG 596
Cdd:cd05959 102 ARVVVVSG----ELAPVLA-AALTKSEHTLVVLivsggagpeagalllaelvaaeaeqLKPAATHADDpAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 597 VPKGVVveHRQvvNNILWRQRTWpltAQdNVLHNHS----FSFDPSVWA------LFWPLLTGGTIVLADVRTMEDstAL 666
Cdd:cd05959 177 RPKGVV--HLH--ADIYWTAELY---AR-NVLGIREddvcFSAAKLFFAyglgnsLTFPLSVGATTVLMPERPTPA--AV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 667 LDLMIRHDVSVLGGVPSLLGTLIDHPFA--NDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATidALYFSi 744
Cdd:cd05959 247 FKRIRRYRPTVFFGVPTLYAAMLAAPNLpsRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEML--HIFLS- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 745 dkNAAGAI---PIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpnpfgnGRVYATGDLGR 821
Cdd:cd05959 324 --NRPGRVrygTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GEWTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 822 RWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRH-- 899
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEfv 475
|
490 500 510
....*....|....*....|....*....|..
gi 37542635 900 ---LPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05959 476 kdrLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
468-923 |
9.35e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 156.68 E-value: 9.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVI 547
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 548 TsdqqsvegwpqvarirmealdpdirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNV 627
Cdd:cd05934 81 V-----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 628 LHNHS-FSFDPSVWALFWPLLTGGTIVLADVRTmedSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSG 706
Cdd:cd05934 126 LTVLPlFHINAQAVSVLAALSVGATLVLLPRFS---ASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 707 GEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGaiPIGYPIDNTDAYIVDLNLNPVPPGVPGEIML--- 783
Cdd:cd05934 203 GAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPG--SIGRPAPGYEVRIVDDDGQELPAGEPGELVIrgl 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 784 AGQNLARGYLGKPAQTAQRflpnpFGNGrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEA 863
Cdd:cd05934 281 RGWGFFKGYYNMPEATAEA-----MRNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREA 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 864 IVFAQHA--GTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05934 355 AVVAVPDevGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
471-928 |
6.30e-40 |
|
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: 154.42 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD 550
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QqsvegwpqvarirmealdpdirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWrQRTWPLTAQDNVLHN 630
Cdd:cd05972 81 E--------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPT-AAYWLGLRPDDIHWN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 631 HSfsfDPSvWA------LFWPLLTGGTIVLADVRTMeDSTALLDLMIRHDVSVLGGVPSLLGTLIDH-PFANDCRAVKLV 703
Cdd:cd05972 128 IA---DPG-WAkgawssFFGPWLLGATVFVYEGPRF-DAERILELLERYGVTSFCGPPTAYRMLIKQdLSSYKFSHLRLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 704 LSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAIpiGYPIDNTDAYIVDLNLNPVPPGVPGEIM- 782
Cdd:cd05972 203 VSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSM--GRPTPGYDVAIIDDDGRELPPGEEGDIAi 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 783 -LAGQNLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELK 861
Cdd:cd05972 281 kLPPPGLFLGYVGDPEKTEASI------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37542635 862 EAIVFAqHAGTEQARLVAA--IEQQPGLHSEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05972 355 EAAVVG-SPDPVRGEVVKAfvVLTSGYEPSEELAEELQGHvkkvLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
446-924 |
2.04e-39 |
|
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: 154.02 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 446 TLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGhaFLPI 525
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 526 DPrLPTDR---IQFLIENSGCELVITSDQQSVEGWPQVARIRMEaldpdirwvaptglSHSDAAYLIYTSGSTGVPKGVV 602
Cdd:cd05920 94 LA-LPSHRrseLSAFCAHAEAVAYIVPDRHAGFDHRALARELAE--------------SIPEVALFLLSGGTTGTPKLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 603 VEHRQVVNNILWRQRTWPLTAQDNVL------HNHSFSfDPSVwalFWPLLTGGTIVLADvrtMEDSTALLDLMIRHDVS 676
Cdd:cd05920 159 RTHNDYAYNVRASAEVCGLDQDTVYLavlpaaHNFPLA-CPGV---LGTLLAGGRVVLAP---DPSPDAAFPLIEREGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 677 VLGGVPSLLGTLIDH--PFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDalYFSIDKNAAGAIPI 754
Cdd:cd05920 232 VTALVPALVSLWLDAaaSRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLN--YTRLDDPDEVIIHT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 755 -GYPIDNTD-AYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLG 832
Cdd:cd05920 310 qGRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-----YRTGDLVRRTPDGYLVVEG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 833 RRDQQVKIRGHRIELNEVAHLLcqalelkeaivfAQHAGTEQARLVA-------------AIEQQPGLHSEGIKQELL-R 898
Cdd:cd05920 385 RIKDQINRGGEKIAAEEVENLL------------LRHPAVHDAAVVAmpdellgerscafVVLRDPPPSAAQLRRFLReR 452
|
490 500
....*....|....*....|....*.
gi 37542635 899 HLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd05920 453 GLAAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
472-923 |
4.36e-39 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 152.20 E-value: 4.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 472 SYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSdq 551
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 552 qsvegwpqvarirmEALDPdirwvaptglshsdaAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHnh 631
Cdd:cd05971 86 --------------GSDDP---------------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLY-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 632 sfsFDPSVWA-------LFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKL-- 702
Cdd:cd05971 135 ---WTPADWAwigglldVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLra 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 703 VLSGGEVLNPELAHKIQKVWQADVANLYGPTEATI----DALYFSIdKNAAgaipIGYPIDNTDAYIVDLNLNPVPPGVP 778
Cdd:cd05971 212 IATGGESLGEELLGWAREQFGVEVNEFYGQTECNLvignCSALFPI-KPGS----MGKPIPGHRVAIVDDNGTPLPPGEV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 779 GEIML--AGQNLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQ 856
Cdd:cd05971 287 GEIAVelPDPVAFLGYWNNPSATEKKM------AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLK 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 857 ALELKEAIVFAQHAGTEQARLVAAIEQQPG-LHSEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05971 361 HPAVLMAAVVGIPDPIRGEIVKAFVVLNPGeTPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKI 432
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
466-923 |
1.73e-38 |
|
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: 151.21 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 466 DHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCEL 545
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 546 VITSD------QQSVEGWPQVARI-----------------RMEALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVV 602
Cdd:cd05911 86 IFTDPdglekvKEAAKELGPKDKIivlddkpdgvlsiedllSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 603 VEHRQVVNNILWRQRTWPLT--AQDNVLH----NHSFSFdpsvWALFWPLLTGGTIVladvrTME--DSTALLDLMIRHD 674
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYGNdgSNDVILGflplYHIYGL----FTTLASLLNGATVI-----IMPkfDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 675 VSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQ-ADVANLYGPTEATIDALYFSIDKNAAGA 751
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLDkyDLSSLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 752 ipIGYPIDNTDAYIVDLNLNP-VPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISY 830
Cdd:cd05911 317 --VGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-----LHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 831 LGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA--QHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYlipSQ 908
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGipDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY---KQ 466
|
490
....*....|....*....
gi 37542635 909 L----LLLDELPRTATGKV 923
Cdd:cd05911 467 LrggvVFVDEIPKSASGKI 485
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
471-923 |
2.07e-38 |
|
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: 149.96 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSd 550
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 qqsvegwPQVARiRMEALDPdirwvaptglshsdaAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHn 630
Cdd:cd05969 80 -------EELYE-RTDPEDP---------------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWC- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 631 hsfSFDP-----SVWALFWPLLTGGTIVLADVRTmeDSTALLDLMIRHDVSVLGGVPSLLGTLI---DHPFAN-DCRAVK 701
Cdd:cd05969 136 ---TADPgwvtgTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMkegDELARKyDLSSLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 702 LVLSGGEVLNPELAHKIQKVWQADVANLYGPTE--ATIDALYFSIDKNAAGaipIGYPIDNTDAYIVDLNLNPVPPGVPG 779
Cdd:cd05969 211 FIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTEtgSIMIANYPCMPIKPGS---MGKPLPGVKAAVVDENGNELPPGTKG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 780 EIMLAGQ--NLARGYLGKPAQtaqrfLPNPFGNGrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQA 857
Cdd:cd05969 288 ILALKPGwpSMFRGIWNDEER-----YKNSFIDG-WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37542635 858 LELKEAIVFAQHAGTEQARLVAAIEQQPGLH-SEGIKQELL----RHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05969 362 PAVAEAGVIGKPDPLRGEIIKAFISLKEGFEpSDELKEEIInfvrQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
446-930 |
3.77e-38 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 151.44 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 446 TLTEWVAASTEKSPLAVAVID-HGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLP 524
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDnHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPRLPTDRIQFLIENSGC--------------ELVITSDQQSVEGWPQVARIRMEA-----------LDPDIRWVAPTG 579
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAkmffaptlfkqtrpVDLILPLQNQLPQLQQIVGVDKLApatsslslsqiIADYEPLTTAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 580 LSHSDAAYLIYTSGSTGVPKGVVVEHrqvvNNILWRQRTWP----LTAQDNVLH----NHSFSFDPSVWAlfwPLLTGGT 651
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTH----NNILASERAYCarlnLTWQDVFMMpaplGHATGFLHGVTA---PFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 652 IVLADVRTmedSTALLDLMIRHDVS-VLGGVP---SLLGTLIDHPFanDCRAVKLVLSGGEVLNPELahkIQKVWQADV- 726
Cdd:PRK06087 257 SVLLDIFT---PDACLALLEQQRCTcMLGATPfiyDLLNLLEKQPA--DLSALRFFLCGGTTIPKKV---ARECQQRGIk 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 727 -ANLYGPTEATIDAlYFSIDKNAA--GAIPiGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAqRF 803
Cdd:PRK06087 329 lLSVYGSTESSPHA-VVNLDDPLSrfMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 804 LPNpfgNGRVYaTGDLGRRWSSGAISYLGRRdQQVKIR-GHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIE 882
Cdd:PRK06087 406 LDE---EGWYY-SGDLCRMDEAGYIKITGRK-KDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 883 QQPGLHSEGIkQELLRHL-----PAYLIPSQLLLLDELPRTATGKVDMLKLDQ 930
Cdd:PRK06087 481 LKAPHHSLTL-EEVVAFFsrkrvAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
445-933 |
1.67e-37 |
|
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: 149.53 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 445 LTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGhaFLP 524
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPrLPTDR---IQFLIENSGCELVITSDQQS-----------VEGWPQV---------------ARIRMEALDPDIRWV 575
Cdd:COG1021 103 VFA-LPAHRraeISHFAEQSEAVAYIIPDRHRgfdyralarelQAEVPSLrhvlvvgdageftslDALLAAPADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 576 APtglshSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL----HNHSFSFdpSVWALFWPLLTGGT 651
Cdd:COG1021 182 DP-----DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLaalpAAHNFPL--SSPGVLGVLYAGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 652 IVLADVrtmEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP--FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANL 729
Cdd:COG1021 255 VVLAPD---PSPDTAFPLIERERVTVTALVPPLALLWLDAAerSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 730 YG-------------PTEATIDAlyfsidknaagaipIGYPIDNTDAY-IVDLNLNPVPPGVPGEIMLAGQNLARGYLGK 795
Cdd:COG1021 332 FGmaeglvnytrlddPEEVILTT--------------QGRPISPDDEVrIVDEDGNPVPPGEVGELLTRGPYTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 796 PAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVkIR-GHRIELNEVAHLLCqalelkeaivfaQHAGTEQ 874
Cdd:COG1021 398 PEHNARAFTPDGF-----YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLL------------AHPAVHD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 875 ARLVA---------------AIEQQPGLhsegikQELLRHL-----PAYLIPSQLLLLDELPRTATGKVDMLKLDQLAA 933
Cdd:COG1021 460 AAVVAmpdeylgerscafvvPRGEPLTL------AELRRFLrerglAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
470-923 |
4.24e-36 |
|
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: 143.00 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 470 QLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITS 549
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 550 DQQSvegwpqvarirmealdpdirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLH 629
Cdd:cd05935 81 SELD------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 630 N----HSFSFDPSVWAlfwPLLTGGTIVLAdvrTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP--FANDCRAVKLV 703
Cdd:cd05935 131 ClplfHVTGFVGSLNT---AVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPefKTRDLSSLKVL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 704 LSGGEVLNPELAHKIQKVWQADVANLYGPTEATIdalyfSIDKNAAGAIP---IGYPIDNTDAYIVDL-NLNPVPPGVPG 779
Cdd:cd05935 205 TGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMS-----QTHTNPPLRPKlqcLGIP*FGVDARVIDIeTGRELPPNEVG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 780 EIMLAGQNLARGYLGKPAQTAQRFLpnPFGNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALE 859
Cdd:cd05935 280 EIVVRGPQIFKGYWNRPEETEESFI--EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 860 LKEAIVFA---QHAGTE-QARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05935 358 I*EVCVISvpdERVGEEvKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
431-933 |
2.29e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 143.64 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 431 VLAQAHGPRTTP--PQ-----LTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALP 503
Cdd:PRK06178 12 ALQQAAWPAGIPrePEyphgeRPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 504 RSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQsvegWPQVARIRME----------------- 566
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL----APVVEQVRAEtslrhvivtsladvlpa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 567 ----ALDPDIR--WVAPTG----LSHSDA---------------AYLIYTSGSTGVPKGVVVEHRqvvnNILWRQRTWPL 621
Cdd:PRK06178 168 eptlPLPDSLRapRLAAAGaidlLPALRActapvplpppaldalAALNYTGGTTGMPKGCEHTQR----DMVYTAAAAYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 622 TAQDNVLHNHSFSFDPSVW------ALFWPLLTGGTIVLAdvrTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN 695
Cdd:PRK06178 244 VAVVGGEDSVFLSFLPEFWiagenfGLLFPLFSGATLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 696 D--------CRAVKLVLSggevLNPELAHKiqkvWQADVANL-----YGPTEA-TIDALY--FSIDKNAAGAIPI--GYP 757
Cdd:PRK06178 321 EydlsslrqVRVVSFVKK----LNPDYRQR----WRALTGSVlaeaaWGMTEThTCDTFTagFQDDDFDLLSQPVfvGLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 758 IDNTDAYIVDLNLN-PVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQ 836
Cdd:PRK06178 393 VPGTEFKICDFETGeLLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL------RDGWLHTGDIGKIDEQGFLHYLGRRKE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 837 QVKIRGHRIELNEVAHLLCQALE-LKEAIVFAQHAGTEQARlVAAIEQQPG--LHSEGIKQELLRHLPAYLIPsQLLLLD 913
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLGQHPAvLGSAVVGRPDPDKGQVP-VAFVQLKPGadLTAAALQAWCRENMAVYKVP-EIRIVD 544
|
570 580
....*....|....*....|
gi 37542635 914 ELPRTATGKVDMLKLDQLAA 933
Cdd:PRK06178 545 ALPMTATGKVRKQDLQALAE 564
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
1063-1302 |
1.90e-34 |
|
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187547 [Multi-domain] Cd Length: 320 Bit Score: 135.12 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKR--TTSRVICLCRAKDAEHAKARILEGLKTYRIDVGSEL*-----RVEYLTGDLALPHLG 1135
Cdd:cd05236 3 VLITGATGFLGKVLLEKLLRScpDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNplfesKIVPIEGDLSEPNLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1136 LSEHQWQTLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELA--CTaRLKSVQYVSTV----DTLLATHVPRP-- 1207
Cdd:cd05236 83 LSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAkrCK-KLKAFVHVSTAyvngDRQLIEEKVYPpp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1208 ---------------FIEDDAPLRSAVGVPVGYTGSKWVAEGVanLGLRRG-IPVSIFRPGLILGHTETGASQSIDYLLV 1271
Cdd:cd05236 162 adpeklidilelmddLELERATPKLLGGHPNTYTFTKALAERL--VLKERGnLPLVIVRPSIVGATLKEPFPGWIDNFNG 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 37542635 1272 ALRGFL--PMGIV------PDYprIFDIVPVDYVAAAIV 1302
Cdd:cd05236 240 PDGLFLayGKGILrtmnadPNA--VADIIPVDVVANALL 276
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
471-930 |
2.40e-34 |
|
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: 137.90 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITsd 550
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 qqsvegwPQVARIRMEALDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL-- 628
Cdd:cd05903 80 -------PERFRQFDPAAMPD------------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLva 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 629 ----HNHSFsfdpsVWALFWPLLTGGTIVLADVRtmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP--FANDCRAVKL 702
Cdd:cd05903 141 spmaHQTGF-----VYGFTLPLLLGAPVVLQDIW---DPDKALALMREHGVTFMMGATPFLTDLLNAVeeAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 703 VLSGGEVLNPELAHKIQKVWQADVANLYGPTEaTIDALYfSIDKNAAGAIPI--GYPIDNTDAYIVDLNLNPVPPGVPGE 780
Cdd:cd05903 213 FVCGGATVPRSLARRAAELLGAKVCSAYGSTE-CPGAVT-SITPAPEDRRLYtdGRPLPGVEIKVVDDTGATLAPGVEGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 781 IMLAGQNLARGYLGKPaQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRdQQVKIR-GHRIELNEVAHLLCQALE 859
Cdd:cd05903 291 LLSRGPSVFLGYLDRP-DLTADAAPEGW-----FRTGDLARLDEDGYLRITGRS-KDIIIRgGENIPVLEVEDLLLGHPG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 860 LKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRH-LPAYLIPSQLLLLDELPRTATGKVDMLKLDQ 930
Cdd:cd05903 364 VIEAAVVALPDERLGERACAVVVTKSGalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
442-820 |
3.05e-34 |
|
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: 138.91 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 442 PPQLTLTEWVAASTEKSPLAVAVID--HGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG 519
Cdd:cd05904 2 PTDLPLDSVSFLFASAHPSRPALIDaaTGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 HAFLPIDPRLPTDRIQFLIENSGCELVITS-----------------DQQSVEGWPQVARIRMEalDPDIRWVAPtgLSH 582
Cdd:cd05904 82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTaelaeklaslalpvvllDSAEFDSLSFSDLLFEA--DEAEPPVVV--IKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 583 SDAAYLIYTSGSTGVPKGVVVEHRQVVNNI-LWRQRTWPLTAQDNVL-----HNHSFSFdpsVWALFWPLLTGGTIVlad 656
Cdd:cd05904 158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVaQFVAGEGSNSDSEDVFlcvlpMFHIYGL---SSFALGLLRLGATVV--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 657 VRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDC--RAVKLVLSGGEVLNPELAHK-IQKVWQADVANLYGPT 733
Cdd:cd05904 232 VMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAfRAKFPNVDLGQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 734 EAT-IDALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLN-PVPPGVPGEIMLAGQNLARGYLGKPAQTA-----QRFLpn 806
Cdd:cd05904 312 ESTgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGeSLPPNQTGELWIRGPSIMKGYLNNPEATAatidkEGWL-- 389
|
410
....*....|....
gi 37542635 807 pfgngrvyATGDLG 820
Cdd:cd05904 390 --------HTGDLC 395
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
446-931 |
4.00e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 138.17 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 446 TLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPI 525
Cdd:PRK03640 3 TMPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 526 DPRLPTDRIQFLIENSGCELVITSD--QQSVEGwpqVARIRMEAL----DPDIRWVAPTGLShsDAAYLIYTSGSTGVPK 599
Cdd:PRK03640 83 NTRLSREELLWQLDDAEVKCLITDDdfEAKLIP---GISVKFAELmngpKEEAEIQEEFDLD--EVATIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 600 GVVvehrQVVNNILWRQRT----WPLTAQDNVL------HNHSFSfdpsvwALFWPLLTGGTIVLadvrtME--DSTALL 667
Cdd:PRK03640 158 GVI----QTYGNHWWSAVGsalnLGLTEDDCWLaavpifHISGLS------ILMRSVIYGMRVVL-----VEkfDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 668 DLMIRHDVSVLGGVPSLLGTLI----DHPFANDCRAVklVLSGGEVLNPELahKIQKVWQADVANLYGPTE-----ATID 738
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRLLerlgEGTYPSSFRCM--LLGGGPAPKPLL--EQCKEKGIPVYQSYGMTEtasqiVTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 ALYfSIDKNAAgaipIGYPIDNTDAYIVDlNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpnpfgNGRVYaTGD 818
Cdd:PRK03640 299 PED-ALTKLGS----AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-----DGWFK-TGD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 819 LGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLR 898
Cdd:PRK03640 367 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEE 446
|
490 500 510
....*....|....*....|....*....|...
gi 37542635 899 HLPAYLIPSQLLLLDELPRTATGKVDMLKLDQL 931
Cdd:PRK03640 447 KLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
438-923 |
1.43e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 137.78 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 438 PRT-TPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVA-KPRSIIAVALPRSAEFIAALLGV 515
Cdd:PRK08314 2 PKSlTLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGvRKGDRVLLYMQNSPQFVIAYYAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 516 VRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQSVEGWPQVARIRME---------ALDPDIRWVAPTGL------ 580
Cdd:PRK08314 82 LRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhvivaqysdYLPAEPEIAVPAWLraeppl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 581 --------------------------SHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI----LWRQrtwpLTAQDNVLhn 630
Cdd:PRK08314 162 qalapggvvawkealaaglappphtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAvgsvLWSN----STPESVVL-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 631 hsfsfdpSVWALFW----------PLLTGGTIVLAdvrTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP-FAN-DCR 698
Cdd:PRK08314 236 -------AVLPLFHvtgmvhsmnaPIYAGATVVLM---PRWDREAAARLIERYRVTHWTNIPTMVVDFLASPgLAErDLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 AVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEaTIDALYFsidkNAAGAiP----IGYPIDNTDAYIVDL-NLNPV 773
Cdd:PRK08314 306 SLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHS----NPPDR-PklqcLGIPTFGVDARVIDPeTLEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 774 PPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpnPFGNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHL 853
Cdd:PRK08314 380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFI--EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENL 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 854 LCQALELKEAIVFA---QHAG-TEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK08314 458 LYKHPAIQEACVIAtpdPRRGeTVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
452-923 |
3.39e-33 |
|
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: 135.71 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 452 AASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPT 531
Cdd:cd05923 10 AASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 532 DRIQFLIENSG-CELVITSDQQSVEGWPQvARIRMEALDPDIRWVAPTGLSHS---------DAAYLIYTSGSTGVPKGV 601
Cdd:cd05923 90 AELAELIERGEmTAAVIAVDAQVMDAIFQ-SGVRVLALSDLVGLGEPESAGPLiedpprepeQPAFVFYTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 602 VVEHRQVVNNILWrqrtwpLTAQDNVL---HNHSFSFDP-----SVWALF-WPLLTGGTIVLadVRTMEDSTAlLDLMIR 672
Cdd:cd05923 169 VIPQRAAESRVLF------MSTQAGLRhgrHNVVLGLMPlyhviGFFAVLvAALALDGTYVV--VEEFDPADA-LKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 673 HDVSVLGGVPSLLGTLIDH-PFAN-DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEatidALYFSIDKNAAG 750
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAaEFAGlKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE----AMNSLYMRDART 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 751 AiPIGYPIDNTDAYIVDLNLNPV---PPGVPGEIM--LAGQNLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSS 825
Cdd:cd05923 316 G-TEMRPGFFSEVRIVRIGGSPDealANGEEGELIvaAAADAAFTGYLNQPEATAKKL------QDGWYRTGDVGYVDPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 826 GAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLR--HLPAY 903
Cdd:cd05923 389 GDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRasELADF 468
|
490 500
....*....|....*....|
gi 37542635 904 LIPSQLLLLDELPRTATGKV 923
Cdd:cd05923 469 KRPRRYFFLDELPKNAMNKV 488
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
450-923 |
2.43e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 133.06 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 450 WVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHV-AKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPR 528
Cdd:PRK06839 7 WIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELnVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 529 LPTDRIQFLIENSGCELVITSDQQSVEGWPQVARIRMEaldPDIRWVAPTGLSHS----------DAAYLI-YTSGSTGV 597
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ---RVISITSLKEIEDRkidnfvekneSASFIIcYTSGTTGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 598 PKGVVVEHRQVVNNILWRQRTWPLTAQD-NVLHNHSFSFDPSVWALFWPLLTGGTIVLADvrtMEDSTALLDLMIRHDVS 676
Cdd:PRK06839 164 PKGAVLTQENMFWNALNNTFAIDLTMHDrSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPR---KFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 677 VLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSGGEVLNPELAHKIQKVwQADVANLYGPTEATIDALYFSIDKNAAGAIPI 754
Cdd:PRK06839 241 VVMGVPTIHQALINCSkFETtNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDARRKVGSI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 755 GYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAqrflpNPFGNGRVYaTGDLGRRWSSGAISYLGRR 834
Cdd:PRK06839 320 GKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE-----ETIQDGWLC-TGDLARVDEDGFVYIVGRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 835 DQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLL 912
Cdd:PRK06839 394 KEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLFLAKYKIPKEIVFL 473
|
490
....*....|.
gi 37542635 913 DELPRTATGKV 923
Cdd:PRK06839 474 KELPKNATGKI 484
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
467-932 |
2.45e-31 |
|
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: 130.14 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 467 HGQQLSYAELwARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELV 546
Cdd:cd05909 4 LGTSLTYRKL-LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 547 ITSDQ--------QSVEGWPQVARIRMEALDPDI--------------------RWVAPTGLSHSDAAYLIYTSGSTGVP 598
Cdd:cd05909 83 LTSKQfieklklhHLFDVEYDARIVYLEDLRAKIskadkckaflagkfppkwllRIFGVAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 599 KGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HSFSFDPSVWAlfwPLLTGGTIVLADVRTmeDSTALLDLMIRHD 674
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGAlpffHSFGLTGCLWL---PLLSGIKVVFHPNPL--DYKKIPELIYDKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 675 VSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAtidALYFSIDKNAAGAIP- 753
Cdd:cd05909 238 ATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTEC---SPVISVNTPQSPNKEg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 754 -IGYPIDNTDAYIVDL-NLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRflpnpFGNGRvYATGDLGRRWSSGAISYL 831
Cdd:cd05909 315 tVGRPLPGMEVKIVSVeTHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFA-----FGDGW-YDTGDIGKIDGEGFLTIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 832 GRRDQQVKIRGHRIelnevahllcqALELKEAIVfaqHAGTEQARLVAAIEQQPGLHSEGIK-------------QELLR 898
Cdd:cd05909 389 GRLSRFAKIAGEMV-----------SLEAIEDIL---SEILPEDNEVAVVSVPDGRKGEKIVllttttdtdpsslNDILK 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 37542635 899 H--LPAYLIPSQLLLLDELPRTATGKVDMLKLDQLA 932
Cdd:cd05909 455 NagISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
484-928 |
3.72e-31 |
|
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: 129.95 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 484 AANISQHVAKPRSI-----IAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDR-IQFLIENSGCELVITSDQQSVEGw 557
Cdd:cd17647 29 ASNIVAHYLIKTGIkrgdvVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARqNIYLGVAKPRGLIVIRAAGVVVG- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 558 pqvarirmealdPDIRwvaPTglshsdaayLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDP 637
Cdd:cd17647 108 ------------PDSN---PT---------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 638 SVWALFWPLLTGGTIVladVRTMED---STALLDLMIRHDVSVLGGVPS---LLGTLIDHPFANDCRAVKLvlsgGEVLN 711
Cdd:cd17647 164 IQRDMFTPLFLGAQLL---VPTQDDigtPGRLAEWMAKYGATVTHLTPAmgqLLTAQATTPFPKLHHAFFV----GDILT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 712 PELAHKIQKVWQ-ADVANLYGPTEATIDALYFSID---------KNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVP--G 779
Cdd:cd17647 237 KRDCLRLQTLAEnVRIVNMYGTTETQRAVSYFEVPsrssdptflKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGevG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 780 EIMLAGQNLARGYLGKPAQTAQRFLPNPFGN-----------------------GRVYATGDLGRRWSSGAISYLGRRDQ 836
Cdd:cd17647 317 EIYVRAGGLAEGYRGLPELNKEKFVNNWFVEpdhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPNGDCECCGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 837 QVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQP------------------------GLH---- 888
Cdd:cd17647 397 QVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFdkpddesfaqedvpkevstdpivkGLIgyrk 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 37542635 889 -SEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd17647 477 lIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
471-923 |
2.38e-30 |
|
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: 125.54 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELvitsd 550
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 qqsvegwpqvarirmealdpdirwvaptglshSDAAYLIYTSGSTGVPKGVVvehrQVVNNILWR----QRTWPLTAQDN 626
Cdd:cd05912 77 --------------------------------DDIATIMYTSGTTGKPKGVQ----QTFGNHWWSaigsALNLGLTEDDN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 627 VL------HNHSFSfdpsvwALFWPLLTGGTIVLADvrtMEDSTALLDLMIRHDVSVLGGVPSLLGTLID---HPFANDC 697
Cdd:cd05912 121 WLcalplfHISGLS------ILMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEilgEGYPNNL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 698 RavKLVLSGGEVLNPELAHKIQK---VWQAdvanlYGPTEATIDALYFSIDKNAAGAIPIGYPIDNTDAYIVDlnlNPVP 774
Cdd:cd05912 192 R--CILLGGGPAPKPLLEQCKEKgipVYQS-----YGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIED---DGQP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 775 PGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvyATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLL 854
Cdd:cd05912 262 PYEVGEILLKGPNVTKGYLNRPDATEESFENGWF------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 855 CQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05912 336 LSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
1064-1420 |
2.57e-30 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 128.92 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1064 FLTGATGYLGLYLIEQLL-KRTTSRVICLCRAkdaehAKARILEGLKTYridVGSEl*RVEYLTGDLALPHLGLSEHQWQ 1142
Cdd:PRK07201 4 FVTGGTGFIGRRLVSRLLdRRREATVHVLVRR-----QSLSRLEALAAY---WGAD--RVVPLVGDLTEPGLGLSEADIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 TLAEeVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVdtLLATHVPRPFIEDDapLRSAVGVP 1222
Cdd:PRK07201 74 ELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSI--AVAGDYEGVFREDD--FDEGQGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1223 VGYTGSKWVAEGVANLglRRGIPVSIFRPGLILGHTETGASQSID---YL------LVALRGFLPMgIVPDYPRIfDIVP 1293
Cdd:PRK07201 149 TPYHRTKFEAEKLVRE--ECGLPWRVYRPAVVVGDSRTGEMDKIDgpyYFfkvlakLAKLPSWLPM-VGPDGGRT-NIVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1294 VDYVAAAIVHISMQPqGRD-KFFHLFNPAPVTIRqfcDWIREFGYEFklvdfeHGRQQA--LSVPPGHLLYPL------V 1364
Cdd:PRK07201 225 VDYVADALDHLMHKD-GRDgQTFHLTDPKPQRVG---DIYNAFARAA------GAPPDArlFGFLPGFVAAPLlaalgpV 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1365 PLIRDADP----LPHRALDpdyIHEVNPALECKQTLELLASSDITLSKtTKAYAHTILRY 1420
Cdd:PRK07201 295 RRLRNAVAtqlgIPPEVLD---FVNYPTTFDSRETRAALKGSGIEVPR-LASYAPRLWDY 350
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
25-411 |
4.44e-30 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 125.16 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 25 AYPLSSEQKRLWLLAQLAGTAT---LPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKL 101
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAaynIPGALR--LRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 102 EYFD---RPPSDAD------MAELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQ------ 166
Cdd:cd19531 79 PVVDlsgLPEAEREaeaqrlAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAAlyaafl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 167 -------TEPDHQYP--AvgaiaeVFQREQtlAQDAQITEQ---WQQwgiglQ---APAATEIPTENPRPAIKGS----- 226
Cdd:cd19531 159 agrpsplPPLPIQYAdyA------VWQREW--LQGEVLERQlayWRE-----QlagAPPVLELPTDRPRPAVQSFrgarv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 227 ----DRQVHEALTAwgdqpVAEAE-------IVSSWLTVLMRWQGsQSALC---AIKVRDKAH-ANLIGP-LQTyLPVRV 290
Cdd:cd19531 226 rftlPAELTAALRA-----LARREgatlfmtLLAAFQVLLHRYSG-QDDIVvgtPVAGRNRAElEGLIGFfVNT-LVLRT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 291 DMPDGSTLAQLRLQVEEQ-LNGNDH---PsFSTLLEVCPPKRDLSRTPYFQTGLQFIAHDVEQRDFHAGNLTRLPTKQPS 366
Cdd:cd19531 299 DLSGDPTFRELLARVRETaLEAYAHqdlP-FEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGT 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 37542635 367 SDLDLFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSA 411
Cdd:cd19531 378 AKFDLTLSLTETDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEA 422
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
471-923 |
4.65e-30 |
|
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: 125.32 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD 550
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QQsvegwpqvarirMEALDpdirwvaptglshSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDnVLHN 630
Cdd:cd05973 81 AN------------RHKLD-------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED-SFWN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 631 HSfsfDPSvWA--LFW----PLLTG-GTIVLADVRTMEDStalLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCR---AV 700
Cdd:cd05973 135 AA---DPG-WAygLYYaitgPLALGhPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAGAEVPARpkgRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 701 KLVLSGGEVLNPELAHKIQKVWQADVANLYGPTE-----ATIDALYFSIDKNAAGAIPIGYPIDntdayIVDLNLNPVPP 775
Cdd:cd05973 208 RRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElgmvlANHHALEHPVHAGSAGRAMPGWRVA-----VLDDDGDELGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 776 GVPGEIMLAGQNLA----RGYLGKPAQTAqrflpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVA 851
Cdd:cd05973 283 GEPGRLAIDIANSPlmwfRGYQLPDTPAI---------DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVE 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 852 HLLCQALELKEAIVFAQ--HAGTEQAR----LVAAIEQQPGLHSEgIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05973 354 SALIEHPAVAEAAVIGVpdPERTEVVKafvvLRGGHEGTPALADE-LQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
451-934 |
6.67e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 125.69 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 451 VAASTEKSPLAVAVID--HGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPR 528
Cdd:PRK09088 1 IAFHARLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 529 LPTDRIQFLIENSGCELVITSDQqsvegwPQVARIRMEALDPDIRWV-----APTGLSHSDAAYLI-YTSGSTGVPKGVV 602
Cdd:PRK09088 81 LSASELDALLQDAEPRLLLGDDA------VAAGRTDVEDLAAFIASAdalepADTPSIPPERVSLIlFTSGTSGQPKGVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 603 VEHRQVVNNILWRQRTWPLTAQDNVLHN----HSFSFDPSVWALfwpLLTGGTIVLAD----VRTMEdSTALLDLMIRHD 674
Cdd:PRK09088 155 LSERNLQQTAHNFGVLGRVDAHSSFLCDapmfHIIGLITSVRPV---LAVGGSILVSNgfepKRTLG-RLGDPALGITHY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 675 VsvlgGVPSLLGTLIDHP-F-ANDCRAVKLVLSGGEvlnPELAHKIqKVWQAD---VANLYGPTEA-TIDALYFSIDKNA 748
Cdd:PRK09088 231 F----CVPQMAQAFRAQPgFdAAALRHLTALFTGGA---PHAAEDI-LGWLDDgipMVDGFGMSEAgTVFGMSVDCDVIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 749 AGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAI 828
Cdd:PRK09088 303 AKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-----FRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 829 SYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIV--FAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIP 906
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVvgMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVP 457
|
490 500
....*....|....*....|....*....
gi 37542635 907 SQLLLLDELPRTATGKVDMLKL-DQLAAP 934
Cdd:PRK09088 458 KHLRLVDALPRTASGKLQKARLrDALAAG 486
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
453-923 |
4.61e-29 |
|
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: 123.89 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 453 ASTEKSPLAVAVIDHG----QQLSYAELWARAALVAANIsQHVAKPRSIIAVALPRSAEFIAALLGVVRAGH----AFLP 524
Cdd:cd05931 3 AAARPDRPAYTFLDDEggreETLTYAELDRRARAIAARL-QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAiavpLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 iDPRLPTDRIQFLIENSGCELVIT--SDQQSVEGW----PQVARIRMEALD----PDIRWVAPTGLSHSDAAYLIYTSGS 594
Cdd:cd05931 82 -TPGRHAERLAAILADAGPRVVLTtaAALAAVRAFaasrPAAGTPRLLVVDllpdTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 595 TGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL----HNHSFSFdpsVWALFWPLLTGGTIVLadvrtMEDSTAL---- 666
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlpLYHDMGL---IGGLLTPLYSGGPSVL-----MSPAAFLrrpl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 667 --LDLMIRHDVSVlGGVPSllgtlidhpFAND--CRAVK------LVLS-------GGEVLNPELAHKIQKV-------W 722
Cdd:cd05931 233 rwLRLISRYRATI-SAAPN---------FAYDlcVRRVRdedlegLDLSswrvalnGAEPVRPATLRRFAEAfapfgfrP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 723 QAdVANLYGPTEATI-----------DALYFSIDKNAAGAIPI-------------GYPIDNTDAYIVDLN-LNPVPPGV 777
Cdd:cd05931 303 EA-FRPSYGLAEATLfvsggppgtgpVVLRVDRDALAGRAVAVaaddpaarelvscGRPLPDQEVRIVDPEtGRELPDGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 778 PGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNGRVY-ATGDLGRRWsSGAISYLGRRDQQVKIRG-----HRIElNEVA 851
Cdd:cd05931 382 VGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWlRTGDLGFLH-DGELYITGRLKDLIIVRGrnhypQDIE-ATAE 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 852 HlLCQALELKEAIVFA-QHAGTEQARLVAAIEQ-QPGLHSEGIKQElLRHLPAY---LIPSQLLLL--DELPRTATGKV 923
Cdd:cd05931 460 E-AHPALRPGCVAAFSvPDDGEERLVVVAEVERgADPADLAAIAAA-IRAAVARehgVAPADVVLVrpGSIPRTSSGKI 536
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
444-937 |
6.93e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 126.19 E-value: 6.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 444 QLTLTEWVAASTEKSPLAVAVIDH-GQQLSYAELWArAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAF 522
Cdd:PRK08633 614 LPPLAEAWIDTAKRNWSRLAVADStGGELSYGKALT-GALALARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 523 LPIDPRLPTDRIQFLIENSGCELVITS-----------DQQSVEGWPQVarIRMEALDPDIR-----------WVAPTGL 580
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSrkfleklknkgFDLELPENVKV--IYLEDLKAKISkvdkltallaaRLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 581 ---------SHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HSFSFdpsVWALFWPLL 647
Cdd:PRK08633 771 lkrlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSlpffHSFGL---TVTLWLPLL 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 648 TG-GTIVLADVRtmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQA 724
Cdd:PRK08633 848 EGiKVVYHPDPT---DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHplMFASLRLVVAGAEKLKPEVADAFEEKFGI 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 725 DVANLYGPTEAT----------IDALYFSIDKNAAGAipIGYPIDNTDAYIVDL-NLNPVPPGVPGEIMLAGQNLARGYL 793
Cdd:PRK08633 925 RILEGYGATETSpvasvnlpdvLAADFKRQTGSKEGS--VGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQVMKGYL 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 794 GKPAQTAQrFLPNPFGNgRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALElKEAIVFAqhagte 873
Cdd:PRK08633 1003 GDPEKTAE-VIKDIDGI-GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG-GEEVVFA------ 1073
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 874 qarlVAAIE-QQPG-----LHS--EGIKQELLRH-----LPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQLN 937
Cdd:PRK08633 1074 ----VTAVPdEKKGeklvvLHTcgAEDVEELKRAikesgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALALLG 1146
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
427-928 |
7.94e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 123.33 E-value: 7.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 427 MQQTVL-AQAHGPRTTPP-QLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPR 504
Cdd:PRK06155 1 GEPLGAgLAARAVDPLPPsERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 505 SAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQ-----QSVEGwPQVARIRMEALDPDIRWVAPTG 579
Cdd:PRK06155 81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAllaalEAADP-GDLPLPAVWLLDAPASVSVPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 580 LSHS-----------------DAAYLIYTSGSTGVPKGVVVEHRQvvnnILWRQRtwpLTAQ------DNVLHNHSFSFD 636
Cdd:PRK06155 160 WSTAplppldapapaaavqpgDTAAILYTSGTTGPSKGVCCPHAQ----FYWWGR---NSAEdleigaDDVLYTTLPLFH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 637 PSVWALFWP-LLTGGTIVLADVRTmedSTALLDLMIRHDVSV---LGG-VPSLLGTlidhPFANDCRA--VKLVLSGGev 709
Cdd:PRK06155 233 TNALNAFFQaLLAGATYVLEPRFS---ASGFWPAVRRHGATVtylLGAmVSILLSQ----PARESDRAhrVRVALGPG-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 710 LNPELAHKIQKVWQADVANLYGPTEATIdALYFSIDKNAAGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQN-- 787
Cdd:PRK06155 304 VPAALHAAFRERFGVDLLDGYGSTETNF-VIAVTHGSQRPGS--MGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpf 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 788 -LARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVF 866
Cdd:PRK06155 381 aFATGYFGMPEKTVEAW------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVF 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 867 AQHAGTEQARLVAAIEQQPGLHSEgiKQELLRH----LPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:PRK06155 455 PVPSELGEDEVMAAVVLRDGTALE--PVALVRHceprLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
461-928 |
9.74e-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: 121.43 E-value: 9.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAaNISQH--VAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIA-NVLVGelGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVITSDQqsvegwpqvarirmealdpdirwvaptgLSHS-DAAYLIYTSGSTGVPKGVVVEHRQVVNNI-LWRQ 616
Cdd:cd05958 80 DKARITVALCAHA----------------------------LTASdDICILAFTSGTTGAPKATMHFHRDPLASAdRYAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 617 RTWPLTAQDNV--LHNHSFSFDPSVWALFwPLLTGGTIVLADVRTMEDstaLLDLMIRHDVSVLGGVPSLLGTLIDHP-- 692
Cdd:cd05958 132 NVLRLREDDRFvgSPPLAFTFGLGGVLLF-PFGVGASGVLLEEATPDL---LLSAIARYKPTVLFTAPTAYRAMLAHPda 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 693 FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATidALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNP 772
Cdd:cd05958 208 AGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMF--HIFISARPGDARPGATGKPVPGYEAKVVDDEGNP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 773 VPPGVPGEIMLAGQNLARgYLGKPAQTaqrflpNPFGNGRVYaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAH 852
Cdd:cd05958 286 VPDGTIGRLAVRGPTGCR-YLADKRQR------TYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVED 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 853 LLCQALELKEAIVFaqhaGTE-QARL-------VAAIEQQPG-LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05958 358 VLLQHPAVAECAVV----GHPdESRGvvvkafvVLRPGVIPGpVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433
|
....*
gi 37542635 924 DMLKL 928
Cdd:cd05958 434 QRFAL 438
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
459-923 |
1.64e-28 |
|
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: 121.25 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARA-----ALVAANISqhvakPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDR 533
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCrrlasALAALGIS-----RGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 534 IQFLIENSGCELVITsDQQSvegwpqvariRMEAL----DPDIRWVAPTglSHSDAAYLIYTSGSTGVPKGVVVEHR--- 606
Cdd:cd12118 93 IAFILRHSEAKVLFV-DREF----------EYEDLlaegDPDFEWIPPA--DEWDPIALNYTSGTTGRPKGVVYHHRgay 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 607 --QVVNNILWRQRT-----WPLTaqdnVLHNHSFSFdpsVWALFwplLTGGTIV-LADVrtmeDSTALLDLMIRHDVSVL 678
Cdd:cd12118 160 lnALANILEWEMKQhpvylWTLP----MFHCNGWCF---PWTVA---AVGGTNVcLRKV----DAKAIYDLIEKHKVTHF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 679 GGVPSLLGTLIDhpfANDCRAVKL-----VLSGGevlNPELAHKIQKVWQA--DVANLYGPTE----ATI-------DAL 740
Cdd:cd12118 226 CGAPTVLNMLAN---APPSDARPLphrvhVMTAG---APPPAAVLAKMEELgfDVTHVYGLTEtygpATVcawkpewDEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 741 yfSIDKNAA-----G-AIPIGYPIDNTDAYIVDlnlnPVP-PGVP-GEIMLAGQNLARGYLGKPAQTAQRFlpnpfgNGR 812
Cdd:cd12118 300 --PTEERARlkarqGvRYVGLEEVDVLDPETMK----PVPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAF------RGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 813 VYATGDLGRRWSSGAISyLGRRDQQVKIR-GHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGlhSEG 891
Cdd:cd12118 368 WFHSGDLAVIHPDGYIE-IKDRSKDIIISgGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG--AKV 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 37542635 892 IKQELL----RHLPAYLIPSQlLLLDELPRTATGKV 923
Cdd:cd12118 445 TEEEIIafcrEHLAGFMVPKT-VVFGELPKTSTGKI 479
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
1063-1342 |
1.95e-28 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 117.00 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRTTsRVICLCRAKDAEHAKArileglktyridvgsEL*RVEYLTGDLAlphlglSEHQWQ 1142
Cdd:COG0451 2 ILVTGGAGFIGSHLARRLLARGH-EVVGLDRSPPGAANLA---------------ALPGVEFVRGDLR------DPEALA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 TLAEEVDVIYHNGALVNFVY-PYSALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPrpfIEDDAPLRsavgv 1221
Cdd:COG0451 60 AALAGVDAVVHLAAPAGVGEeDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEGP---IDEDTPLR----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1222 PVG-YTGSKWVAEGVANLGLRR-GIPVSIFRPGLILGHTETGAsqsIDYLLVALRGFLPMGIVPDYPRIFDIVPVDYVAA 1299
Cdd:COG0451 132 PVSpYGASKLAAELLARAYARRyGLPVTILRPGNVYGPGDRGV---LPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVAR 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 37542635 1300 AIVHISMQPQGRDKFFHLFNPAPVTIRQFCDWIRE-FGYEFKLV 1342
Cdd:COG0451 209 AIVLALEAPAAPGGVYNVGGGEPVTLRELAEAIAEaLGRPPEIV 252
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
445-923 |
1.50e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 118.45 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 445 LTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLP 524
Cdd:PRK06145 2 FNLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPRLPTDRIQFLIENSGCELVITSDQQSV---EGWPQVarIRMEALDPDIRWVAPTGL--------SHSDAAYLIYTSG 593
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEEFDAivaLETPKI--VIDAAAQADSRRLAQGGLeippqaavAPTDLVRLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 594 STGVPKGVVVEHrqvvNNILWRQR----TWPLTAQDNVL----HNHSFSFDPSVWALFWpllTGGTIvladvRTME--DS 663
Cdd:PRK06145 160 TTDRPKGVMHSY----GNLHWKSIdhviALGLTASERLLvvgpLYHVGAFDLPGIAVLW---VGGTL-----RIHRefDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 664 TALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEvLNPELahKIQKVWQ----ADVANLYGPTEATI 737
Cdd:PRK06145 228 EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDrfDLDSLAWCIGGGE-KTPES--RIRDFTRvftrARYIDAYGLTETCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 738 DALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpnpfgnGRVYATG 817
Cdd:PRK06145 305 GDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY------GDWFRSG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 818 DLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQE 895
Cdd:PRK06145 379 DVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGatLTLEALDRH 458
|
490 500
....*....|....*....|....*...
gi 37542635 896 LLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK06145 459 CRQRLASFKVPRQLKVRDELPRNPSGKV 486
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
444-924 |
3.66e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 118.06 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 444 QLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFL 523
Cdd:PRK07798 2 AWNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 524 PIDPRLPTDRIQFLIENSGCELVITSDQQSvegwPQVARIRMEAldPDIRWV-----------APTGLSHSDAA------ 586
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALVYEREFA----PRVAEVLPRL--PKLRTLvvvedgsgndlLPGAVDYEDALaagspe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 587 -----------YLIYTSGSTGVPKGVvvehrqvvnniLWRQRTWPLTA------------QDNVLHNHSFSFDP------ 637
Cdd:PRK07798 156 rdfgerspddlYLLYTGGTTGMPKGV-----------MWRQEDIFRVLlggrdfatgepiEDEEELAKRAAAGPgmrrfp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 638 --------SVWALFWPLLTGGTIVLADVRTMeDSTALLDLMIRHDVSVLGGV------PsLLGTLiDHPFANDCRAVKLV 703
Cdd:PRK07798 225 applmhgaGQWAAFAALFSGQTVVLLPDVRF-DADEVWRTIEREKVNVITIVgdamarP-LLDAL-EARGPYDLSSLFAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 704 LSGGEVLNPELAHKIQKVW-QADVANLYGPTEAtiDALYFSIdkNAAGAIPIGYPIDNTDAY--IVDLNLNPVPPGVPGE 780
Cdd:PRK07798 302 ASGGALFSPSVKEALLELLpNVVLTDSIGSSET--GFGGSGT--VAKGAVHTGGPRFTIGPRtvVLDEDGNPVEPGSGEI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 781 IMLA-GQNLARGYLGKPAQTAQRFlpnPFGNGRVYA-TGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVahllcqal 858
Cdd:PRK07798 378 GWIArRGHIPLGYYKDPEKTAETF---PTIDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEV-------- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 859 elkEAiVFAQHAGTEQA------------RLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK07798 447 ---EE-ALKAHPDVADAlvvgvpderwgqEVVAVVQLREGarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
469-821 |
4.18e-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: 116.54 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVIT 548
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 549 SDqqsvegwpqvarirmealdPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL 628
Cdd:cd05907 84 ED-------------------PD------------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 629 hnhsfSFDPSVWAL------FWPLLTGGTIVLAdvrtmEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRA--- 699
Cdd:cd05907 133 -----SFLPLAHVFerraglYVPLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGlkr 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 700 ----------VKLVLSGGEVLNPELAHKIQKVwQADVANLYGPTEATIDALYFSIDKNAAGAipIGYPIDNTDAYIVDln 769
Cdd:cd05907 203 klfdlavggrLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGT--VGKPLPGVEVRIAD-- 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 770 lnpvppgvPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGR 821
Cdd:cd05907 278 --------DGEILVRGPNVMLGYYKNPEATAEALDADGW-----LHTGDLGE 316
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
423-924 |
5.50e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 117.29 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 423 MGQQMQQTVLAQAHGPRttppqltLTEWVAASTEKSPLAVAVIDHGQQ--LSYAELWARAALVAANISQHVAKPRSIIAV 500
Cdd:PRK05852 1 MRFMGGAAPMASDFGPR-------IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 501 ALPRSAEFIAALLGVVRAGHAFLPIDPRLP----TDRIQ------FLIENSGcelVITSDQQSVEGWPQVARI------- 563
Cdd:PRK05852 74 RMGSNAEFVVALLAASRADLVVVPLDPALPiaeqRVRSQaagarvVLIDADG---PHDRAEPTTRWWPLTVNVggdsgps 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 564 -------RMEALDPDIRWVAPTGLSHSDAaYLIYTSGSTGVPKGVVVEHRQV---VNNILWRQRTWPLTAQDNVL---HN 630
Cdd:PRK05852 151 ggtlsvhLDAATEPTPATSTPEGLRPDDA-MIMFTGGTTGLPKMVPWTHANIassVRAIITGYRLSPRDATVAVMplyHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 631 HSFsfdpsVWALFWPLLTGGTIVLAdVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP----FANDCRAVKLVLSG 706
Cdd:PRK05852 230 HGL-----IAALLATLASGGAVLLP-ARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAatepSGRKPAALRFIRSC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 707 GEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAIP---IGYPIDNTDA--YIVDLNLNPVPPGVPGEI 781
Cdd:PRK05852 304 SAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTENPvvsTGLVGRSTGAqiRIVGSDGLPLPAGAVGEV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 782 MLAGQNLARGYLGKPAQTAQRFLPNPFgngrvyATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELK 861
Cdd:PRK05852 384 WLRGTTVVRGYLGDPTITAANFTDGWL------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVM 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37542635 862 EAIVFAQHAGTEQARLVAAIEQQPGLH--SEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK05852 458 EAAVFGVPDQLYGEAVAAVIVPRESAPptAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
446-936 |
2.26e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 115.54 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 446 TLTEWVAASTEKSPLAVAVID----HGQ--QLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG 519
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAvrlgTGAprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 HAFLPIDPRLPTDRIQFLIENSGCELVITSD-------QQSVEG----WPQVARI---------RMEALDPDIRWV---- 575
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKtfrgfdhAAMARRlrpeLPALRHVvvvggdgadSFEALLITPAWEqepd 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 576 APTGLSHS-----DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL------HNHSFsfdpsVWALFW 644
Cdd:PRK13295 185 APAILARLrpgpdDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILmaspmaHQTGF-----MYGLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 645 PLLTGGTIVLADVRtmeDSTALLDLMIRHDVSVlggvpsllgTLIDHPFAND-CRAVKL----------VLSGGEVLNPE 713
Cdd:PRK13295 260 PVMLGATAVLQDIW---DPARAAELIRTEGVTF---------TMASTPFLTDlTRAVKEsgrpvsslrtFLCAGAPIPGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 714 LAHKIQKVWQADVANLYGPTE---ATIDALYFSIDKNAAGAipiGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLAR 790
Cdd:PRK13295 328 LVERARAALGAKIVSAWGMTEngaVTLTKLDDPDERASTTD---GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 791 GYLGKPAQTAQRFlpnpfgNGRvYATGDLGRRWSSGAISYLGrRDQQVKIRG-HRIELNEVAHLLCQALELKEAIVFAQH 869
Cdd:PRK13295 405 GYLKRPQLNGTDA------DGW-FDTGDLARIDADGYIRISG-RSKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYP 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 870 AGTEQARLVAAIEQQPG--LHSEGIKqELLR--HLPAYLIPSQLLLLDELPRTATGKVDMLKL-DQLAAPQL 936
Cdd:PRK13295 477 DERLGERACAFVVPRPGqsLDFEEMV-EFLKaqKVAKQYIPERLVVRDALPRTPSGKIQKFRLrEMLRGEDA 547
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
498-923 |
5.25e-26 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 115.90 E-value: 5.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAG-HAFLPiDPRLPTDRIQFLIENSGCELVITSDQQSVEGWPQVARIRMEALDPDIRwVA 576
Cdd:PRK06060 58 VLLCLPDSPDLVQLLLACLARGvMAFLA-NPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAAR-VA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 577 PTG---LSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI-LWRQRTWPLTAQDNVLHN----HSFSFDPSVWalfWPLLT 648
Cdd:PRK06060 136 PGGyepMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVdAMCRKALRLTPEDTGLCSarmyFAYGLGNSVW---FPLAT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 649 GGTIVLADVRTMEDSTALLDlmIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQA-DVA 727
Cdd:PRK06060 213 GGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGiPIL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 728 NLYGPTEATIDALYFSIDKNAAGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQrflpnp 807
Cdd:PRK06060 291 DGIGSTEVGQTFVSNRVDEWRLGT--LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVA------ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 808 fgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVF----AQHAGTEQARLVAAIeq 883
Cdd:PRK06060 363 --NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVavreSTGASTLQAFLVATS-- 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 37542635 884 qpglhSEGIKQELLRH--------LPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK06060 439 -----GATIDGSVMRDlhrgllnrLSAFKVPHRFAVVDRLPRTPNGKL 481
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
472-923 |
8.68e-26 |
|
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: 114.21 E-value: 8.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 472 SYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQ 551
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 552 -----QSVEGWPQVArirmEALDP----------------DIRWV------------------APTGLSHSDAAYLIYTS 592
Cdd:cd17634 166 gvragRSVPLKKNVD----DALNPnvtsvehvivlkrtgsDIDWQegrdlwwrdliakaspehQPEAMNAEDPLFILYTS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 593 GSTGVPKGVVVEHRQVVNNILWRQR---------TWPLTAQDNVLHNHSfsfdpsvWALFWPLLTGGTIVLAD-VRTMED 662
Cdd:cd17634 242 GTTGKPKGVLHTTGGYLVYAATTMKyvfdygpgdIYWCTADVGWVTGHS-------YLLYGPLACGATTLLYEgVPNWPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 663 STALLDLMIRHDVSVLGGVPSLLGTLI----DHPFANDCRAVKLVLSGGEVLNPE---LAHKIQKVWQADVANLYGPTEA 735
Cdd:cd17634 315 PARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEGTDRSSLRILGSVGEPINPEayeWYWKKIGKEKCPVVDTWWQTET 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 736 TidalyFSIDKNAAGAIPIGY-----PIDNTDAYIVDLNLNPVPPGVPGEIMLAGQ--NLARGYLGKPAQTAQRFLPNpF 808
Cdd:cd17634 395 G-----GFMITPLPGAIELKAgsatrPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFST-F 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 809 GNgrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKE-AIVFAQHAGTEQA-----RLVAAIE 882
Cdd:cd17634 469 KG--MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEaAVVGIPHAIKGQApyayvVLNHGVE 546
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 37542635 883 QQPGLHSEgIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd17634 547 PSPELYAE-LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
451-923 |
1.91e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 112.71 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 451 VAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLP 530
Cdd:PRK07788 55 VAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 531 TDRIQFLIENSGCELVITSDQ-----QSVEgwPQVARIRMEALDPD-IRWVAPTGLS------HSDAAYL---------- 588
Cdd:PRK07788 135 GPQLAEVAAREGVKALVYDDEftdllSALP--PDLGRLRAWGGNPDdDEPSGSTDETlddliaGSSTAPLpkppkpggiv 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 589 IYTSGSTGVPKGVVVEH-------RQVVNNILWRQR-TWPLTAQdnVLHNHSFSfdpsVWALFWPLltGGTIVLadvRTM 660
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEpsplaplAGLLSRVPFRAGeTTLLPAP--MFHATGWA----HLTLAMAL--GSTVVL---RRR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 661 EDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP----FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTE-- 734
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGpevlAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEva 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 735 -ATI-DALYFSIDKNAAGAIPIGypidnTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYL-GKPAQTAQRFLpnpfgng 811
Cdd:PRK07788 362 fATIaTPEDLAEAPGTVGRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTdGRDKQIIDGLL------- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 812 rvyATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQ----ARLVAAIEQQPG- 886
Cdd:PRK07788 430 ---SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVI----GVDDeefgQRLRAFVVKAPGa 502
|
490 500 510
....*....|....*....|....*....|....*...
gi 37542635 887 -LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK07788 503 aLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKV 540
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
454-927 |
5.14e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 111.18 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 454 STEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDR 533
Cdd:PRK08316 20 SARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 534 IQFLIENSGCELVITSD-------------QQSVEGWPQVARIRmealDPDIRWVAPTGLSHS-------------DAAY 587
Cdd:PRK08316 100 LAYILDHSGARAFLVDPalaptaeaalallPVDTLILSLVLGGR----EAPGGWLDFADWAEAgsvaepdveladdDLAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 588 LIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HSFSFD----PSVWAlfwplltGGTIVLADVRT 659
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHAlplyHCAQLDvflgPYLYV-------GATNVILDAPD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 660 MEDstaLLDLMIRHDVSVLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSG-----GEVLNpELAHKIQKV--WqadvaNLY 730
Cdd:PRK08316 249 PEL---ILRTIEAERITSFFAPPTVWISLLRHPdFDTrDLSSLRKGYYGasimpVEVLK-ELRERLPGLrfY-----NCY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 731 GPTE----ATIdalyFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpn 806
Cdd:PRK08316 320 GQTEiaplATV----LGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR-- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 807 pfgnGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQAR----LVAAIE 882
Cdd:PRK08316 394 ----GGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI----GLPDPKwieaVTAVVV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 37542635 883 QQPGlhSEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKVdmLK 927
Cdd:PRK08316 466 PKAG--ATVTEDELIAHcrarLAGFKVPKRVIFVDELPRNPSGKI--LK 510
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
584-923 |
5.30e-25 |
|
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: 107.97 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL----HNHSFSFDPSVWAlfwPLLTGGTIVLADVRt 659
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpFFHTFGYKAGIVA---CLLTGATVVPVAVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 660 meDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQAD-VANLYGPTEAT 736
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKkfDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 IDALYFSIDKNAAGAIPIGYPIDNTDAYIVDlnlnpvppgvPGEIMLAGQNLARGYLGKPAQTAQRFlpnpFGNGRVYaT 816
Cdd:cd17638 155 VATMCRPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAI----DADGWLH-T 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 817 GDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTEQARLVAAIEQQpGLHSEGIK 893
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGvpdERMGEVGKAFVVARPGV-TLTEEDVI 298
|
330 340 350
....*....|....*....|....*....|
gi 37542635 894 QELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd17638 299 AWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
468-923 |
1.19e-24 |
|
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: 109.45 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVI 547
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 548 TSDQQsvegwpqvarirmealdpdirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNV 627
Cdd:cd05914 85 VSDED-------------------------------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 628 L----HNHSFsfdPSVWALFWPLLTGGTIVLADvrtmEDSTALLDLMIRHDVSVLGGVPSLLgtLIDHPFANDCR----- 698
Cdd:cd05914 134 LsilpLHHIY---PLTFTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPTLGVPVPL--VIEKIFKMDIIpkltl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 ------------------------------AVKLVLSGGEVLNPELAHKIQKVwQADVANLYGPTEaTIDALYFSIdKNA 748
Cdd:cd05914 205 kkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTE-TAPIISYSP-PNR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 749 AGAIPIGYPIDNTDAYIVDlnlnPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPnpfgNGRVYaTGDLGRRWSSGAI 828
Cdd:cd05914 282 IRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK----DGWFH-TGDLGKIDAEGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 829 SYLGRRDQQ-VKIRGHRIELNEVAHLLCQALELKEAIVFAQHaGTEQARLV--AAIEQQPGLHS----EGIKQELL---- 897
Cdd:cd05914 353 YIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE-KKLVALAYidPDFLDVKALKQrniiDAIKWEVRdkvn 431
|
490 500
....*....|....*....|....*..
gi 37542635 898 RHLPAYLIPSQLLLL-DELPRTATGKV 923
Cdd:cd05914 432 QKVPNYKKISKVKIVkEEFEKTPKGKI 458
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
470-928 |
2.12e-24 |
|
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: 109.26 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 470 QLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITS 549
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 550 D------QQSVEGWPQVAR------------------IRMEAL----DPDIRWvapTGLSHSDAAYLIYTSGSTGVPKGV 601
Cdd:cd12119 105 RdflpllEAIAPRLPTVEHvvvmtddaampepagvgvLAYEELlaaeSPEYDW---PDFDENTAAAICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 602 VVEHRQVVNN--ILWRQRTWPLTAQDNVL------HNHSfsfdpsvWAL-FWPLLTGGTIVLADVRTMEDStaLLDLMIR 672
Cdd:cd12119 182 VYSHRSLVLHamAALLTDGLGLSESDVVLpvvpmfHVNA-------WGLpYAAAMVGAKLVLPGPYLDPAS--LAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 673 HDVSVLGGVPSLLGTLIDHPFANDCR--AVKLVLSGGEVLNPELAHKIQKVWqADVANLYGPTEA---------TIDALY 741
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVPRSLIEAFEERG-VRVIHAWGMTETsplgtvarpPSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 742 FSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVP--PGVPGEIMLAGQNLARGYLGKPAQTAQRflpnpFGNGrVYATGDL 819
Cdd:cd12119 332 LSEDEQLALRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEAL-----TEDG-WLRTGDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 820 GRRWSSGaisYLGRRDQQ---VKIRGHRI---ELNEVAHlLCQAleLKEAIVFAQHAGTEQARLVAAIEQQPGlhSEGIK 893
Cdd:cd12119 406 ATIDEDG---YLTITDRSkdvIKSGGEWIssvELENAIM-AHPA--VAEAAVIGVPHPKWGERPLAVVVLKEG--ATVTA 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 37542635 894 QELLRHLPAYL----IPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd12119 478 EELLEFLADKVakwwLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
468-922 |
2.80e-24 |
|
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: 107.82 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGhaflpidprlptdRIQFLIENSgcelvi 547
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIG-------------AVAALINYN------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 548 tsdqqsvegwpqvarIRMEALDPDIRwVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQrTWPLTAQDNV 627
Cdd:cd05940 62 ---------------LRGESLAHCLN-VSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAFFA-GSGGALPSDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 628 LHN-----HSFSfdpSVWALFWPLLTGGTIVLADVRTmedSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKL 702
Cdd:cd05940 125 LYTclplyHSTA---LIVGWSACLASGATLVIRKKFS---ASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 703 VLSGGEVLNPELAHKIQKVWQ-ADVANLYGPTEATIDALYFSIDKNAAGAIPIGYPIDNTDAyIVDLNLN---------- 771
Cdd:cd05940 199 RMIFGNGLRPDIWEEFKERFGvPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLA-LVKYDLEsgepirdaeg 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 772 ---PVPPGVPGEIMLAGQNLAR--GYLgKPAQTAQRFLPNPFGNG-RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRI 845
Cdd:cd05940 278 rciKVPRGEPGLLISRINPLEPfdGYT-DPAATEKKILRDVFKKGdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 846 ELNEVAHLLCQALELKEAIVFA-QHAGTEQARLVAAIEQQPGLHSEGIK--QELLRHLPAYLIPSQLLLLDELPRTATGK 922
Cdd:cd05940 357 STTEVAAVLGAFPGVEEANVYGvQVPGTDGRAGMAAIVLQPNEEFDLSAlaAHLEKNLPGYARPLFLRLQPEMEITGTFK 436
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
448-923 |
2.96e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 109.10 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 448 TEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQH-VAKPRSIIAVALPRSaEFIAALLGVVRAGHAFLPID 526
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRgVGFGDRVLILMLNRT-EFVESVLAANMLGAIAVPVN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITSDQQSvegwPQVARIRmeALDPDIRWV-------------------------APTGLS 581
Cdd:PRK07786 99 FRLTPPEIAFLVSDCGAHVVVTEAALA----PVATAVR--DIVPLLSTVvvaggssddsvlgyedllaeagpahAPVDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 582 HSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVlhnhSFSFDP-----SVWALFWPLLTGGTIVLAD 656
Cdd:PRK07786 173 NDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDV----GFVGVPlfhiaGIGSMLPGLLLGAPTVIYP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 657 VRTMeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDcRAVKL-VLS-GGEVLNPELAHKIQKVW-QADVANLYGPT 733
Cdd:PRK07786 249 LGAF-DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALrVLSwGAAPASDTLLRQMAATFpEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 734 EATIDALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpnpfgNGRV 813
Cdd:PRK07786 327 EMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGGW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 814 YATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVF--AQHAGTEQARLVAAIEQQ-PGLHSE 890
Cdd:PRK07786 401 FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIgrADEKWGEVPVAVAAVRNDdAALTLE 480
|
490 500 510
....*....|....*....|....*....|...
gi 37542635 891 GIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK07786 481 DLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
583-923 |
3.74e-24 |
|
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: 105.42 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 583 SDAAYLIYTSGSTGVPKGVVVEHRQVV---NNILWRQRTWplTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRT 659
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFavpDILQKEGLNW--VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 660 meDSTALLDLMIRHDVSVLGGVPSLLGTLID--HPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATi 737
Cdd:cd17635 79 --TYKSLFKILTTNAVTTTCLVPTLLSKLVSelKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 738 DALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLpnpfgNGRVYaTG 817
Cdd:cd17635 156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-----DGWVN-TG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 818 DLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA----QHAGTEQARLVAAIEQQPGLHSeGIK 893
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEisdeEFGELVGLAVVASAELDENAIR-ALK 308
|
330 340 350
....*....|....*....|....*....|
gi 37542635 894 QELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
445-936 |
4.49e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 107.94 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 445 LTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIiAVALPRSAEFIAALLGVVRAGHAFLP 524
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPRLPTDRIQFLIENSGCELVITSDQQ-----SVEGwpqvARIRMEALDPDIRWVAPTGLSHSDAA----YLIYTSGST 595
Cdd:PRK07638 80 LDIKWKQDELKERLAISNADMIVTERYKlndlpDEEG----RVIEIDEWKRMIEKYLPTYAPIENVQnapfYMGFTSGST 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 596 GVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL------HNHsFSFDpSVWALFwpllTGGTIVLadVRTMEDSTALlDL 669
Cdd:PRK07638 156 GKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLiagtlvHSL-FLYG-AISTLY----VGQTVHL--MRKFIPNQVL-DK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 670 MIRHDVSVLGGVPSLLGTL------IDHPfandcraVKLVLSGGEvLNPELAHKIQKVW-QADVANLYGPTEAT-IDALY 741
Cdd:PRK07638 227 LETENISVMYTVPTMLESLykenrvIENK-------MKIISSGAK-WEAEAKEKIKNIFpYAKLYEFYGASELSfVTALV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 742 FSIDKNAAGAIpiGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQrflPNPFGNGRVYatgDLGR 821
Cdd:PRK07638 299 DEESERRPNSV--GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---LNADGWMTVR---DVGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 822 RWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPglHSEGIKQELLRHLP 901
Cdd:PRK07638 371 EDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA--TKQQLKSFCLQRLS 448
|
490 500 510
....*....|....*....|....*....|....*
gi 37542635 902 AYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQL 936
Cdd:PRK07638 449 SFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
447-923 |
6.32e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 107.00 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 447 LTEWVAASTEKSPLAVAVIDHGqqLSYAELWARAALVAANisqhVAKPRSIIAVALPrSAEFIAALLGVVRAGHAFLPID 526
Cdd:PRK07787 4 LNPAAVAAAADIADAVRIGGRV--LSRSDLAGAATAVAER----VAGARRVAVLATP-TLATVLAVVGALIAGVPVVPVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 527 PRLPTDRIQFLIENSGCELVITSDQQSVEGWPQVArirmeaLDPDIR-WVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEH 605
Cdd:PRK07787 77 PDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVP------VRLHARsWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 606 RQVVNNILWRQRTWPLTAQDNVLHN------HSFsfdpsVWALFWPLLTGGTIVladvRTMEDSTALLDLMIRHDVSVLG 679
Cdd:PRK07787 151 RAIAADLDALAEAWQWTADDVLVHGlplfhvHGL-----VLGVLGPLRIGNRFV----HTGRPTPEAYAQALSEGGTLYF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 680 GVPSLLGTLIDHP-FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAIpiGYPI 758
Cdd:PRK07787 222 GVPTVWSRIAADPeAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWV--GLPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 759 DNTDAYIVDLNLNPVPPGVP--GEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQ 836
Cdd:PRK07787 300 AGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-----FRTGDVAVVDPDGMHRIVGREST 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 837 Q-VKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDEL 915
Cdd:PRK07787 375 DlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDAL 454
|
....*...
gi 37542635 916 PRTATGKV 923
Cdd:PRK07787 455 PRNAMGKV 462
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
522-923 |
2.20e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 106.66 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 522 FLPidprLPTDRIQFLIENSGCELVI-TSDQQSVEGWPQVARIRMEAL----DPDirwvaptglshSDAAYLIYTSGSTG 596
Cdd:PRK06710 155 FLP----FPKNLLYPFVQKKQSNLVVkVSESETIHLWNSVEKEVNTGVevpcDPE-----------NDLALLQYTGGTTG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 597 VPKGVVVEHRQVVNNIL----WRQRTwpLTAQDNVLHNHSFSFDPSVWALF-WPLLTGGTIVLADVRTMEdstALLDLMI 671
Cdd:PRK06710 220 FPKGVMLTHKNLVSNTLmgvqWLYNC--KEGEEVVLGVLPFFHVYGMTAVMnLSIMQGYKMVLIPKFDMK---MVFEAIK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 672 RHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT-IDALYFSIDKNA 748
Cdd:PRK06710 295 KHKVTLFPGAPTIYIALLNSPLLKeyDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 749 AGAIpiGYPIDNTDAYIVDLNLNPV-PPGVPGEIMLAGQNLARGYLGKPAQTAQrflpnPFGNGRVYaTGDLGRRWSSGA 827
Cdd:PRK06710 375 PGSI--GVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPQIMKGYWNKPEETAA-----VLQDGWLH-TGDVGYMDEDGF 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 828 ISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGtEQARLVAAIEQQPGLHSEGIKQELLRHLPAYL 904
Cdd:PRK06710 447 FYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGvpdPYRG-ETVKAFVVLKEGTECSEEELNQFARKYLAAYK 525
|
410
....*....|....*....
gi 37542635 905 IPSQLLLLDELPRTATGKV 923
Cdd:PRK06710 526 VPKVYEFRDELPKTTVGKI 544
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
446-928 |
2.86e-23 |
|
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: 105.83 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 446 TLTEWVAASTEKSPLA----VAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGha 521
Cdd:cd05906 11 TLLELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 522 FLP-IDPRLPTDRIQFLIENSGCEL--------VITSD--QQSVEGWPQVARIRM-------EALDPDIRWVAPTGLShS 583
Cdd:cd05906 89 FVPaPLTVPPTYDEPNARLRKLRHIwqllgspvVLTDAelVAEFAGLETLSGLPGirvlsieELLDTAADHDLPQSRP-D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLhnhsfsfdpsVWAlfwPLLTGGTIV---LADVRTM 660
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFL----------NWV---PLDHVGGLVelhLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 661 ------------EDSTALLDLMIRHDVSVLGGVPSLLGTLIDH-----PFANDCRAVKLVLSGGEVLNPELAHKIQKVW- 722
Cdd:cd05906 235 cqqvhvpteeilADPLRWLDLIDRYRVTITWAPNFAFALLNDLleeieDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLe 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 723 ----QADV-ANLYGPTEA---TIDALYFSIDkNAAGAIP---IGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARG 791
Cdd:cd05906 315 pyglPPDAiRPAFGMTETcsgVIYSRSFPTY-DHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 792 YLGKPAQTAQRFLPNPFgngrvYATGDLGrrW-SSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKE-----AIV 865
Cdd:cd05906 394 YYNNPEANAEAFTEDGW-----FRTGDLG--FlDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftaaFAV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37542635 866 FAQHAGTEQARLVAAIEQQP-----GLHSEgIKQELLRHL---PAYLIPsqlLLLDELPRTATGKVDMLKL 928
Cdd:cd05906 467 RDPGAETEELAIFFVPEYDLqdalsETLRA-IRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
445-923 |
3.03e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 106.00 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 445 LTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLP 524
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPRLPTDRIQFLIENSGCELVITSDQ------QSVEGWPQVARIRMEALDPDIRWV-----APTGL----SHSDAAYLI 589
Cdd:PRK13382 123 LNTSFAGPALAEVVTREGVDTVIYDEEfsatvdRALADCPQATRIVAWTDEDHDLTVevliaAHAGQrpepTGRKGRVIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 590 YTSGSTGVPKGV-------VVEHRQVVNNILWRQRTwPLTAQDNVLHNHSFSfdpsvwALFWPLLTGGTIVLadvRTMED 662
Cdd:PRK13382 203 LTSGTTGTPKGArrsgpggIGTLKAILDRTPWRAEE-PTVIVAPMFHAWGFS------QLVLAASLACTIVT---RRRFD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 663 STALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN----DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATID 738
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVrnrySGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 ALYFSIDKNAAgaiP--IGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYL-GKPAQTAQRFLpnpfgngrvyA 815
Cdd:PRK13382 353 ATATPADLRAA---PdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTsGSTKDFHDGFM----------A 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 816 TGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHS--EGIK 893
Cdd:PRK13382 420 SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASAtpETLK 499
|
490 500 510
....*....|....*....|....*....|
gi 37542635 894 QELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK13382 500 QHVRDNLANYKVPRDIVVLDELPRGATGKI 529
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
428-924 |
4.17e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 105.07 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 428 QQTVLAQAHGPRTTPPQLTltewvaASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAE 507
Cdd:PRK06188 1 QATMADLLHSGATYGHLLV------SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 508 FIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQSVE-GWPQVARI----RMEALDP-----DI----R 573
Cdd:PRK06188 75 VLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVErALALLARVpslkHVLTLGPvpdgvDLlaaaA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 574 WVAPTGLS----HSDAAYLIYTSGSTGVPKGVVVEHRQVV--NNILWRQRTWPltAQDNVLHNHSFSFDPSvwALFWP-L 646
Cdd:PRK06188 155 KFGPAPLVaaalPPDIAGLAYTGGTTGKPKGVMGTHRSIAtmAQIQLAEWEWP--ADPRFLMCTPLSHAGG--AFFLPtL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 647 LTGGTIVLADvrtMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP--FANDCRAVKLVLSGGEVLNP-ELAHKIQKVWQ 723
Cdd:PRK06188 231 LRGGTVIVLA---KFDPAEVLRAIEEQRITATFLVPTMIYALLDHPdlRTRDLSSLETVYYGASPMSPvRLAEAIERFGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 724 AdVANLYGPTEATIDALYFS----IDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQT 799
Cdd:PRK06188 308 I-FAQYYGQTEAPMVITYLRkrdhDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 800 AQrflpnPFGNGRVYaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHllcqalelkeaiVFAQHAGTEQARLV- 878
Cdd:PRK06188 387 AE-----AFRDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVED------------VLAEHPAVAQVAVIg 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37542635 879 -----------AAIEQQPGLHSEgiKQELLRHLP----AYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK06188 449 vpdekwgeavtAVVVLRPGAAVD--AAELQAHVKerkgSVHAPKQVDFVDSLPLTALGKPD 507
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
590-928 |
6.01e-23 |
|
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: 101.97 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 590 YTSGSTGVPKGVVVEHRQVVNN---ILWRQRtwpLTAQD-----NVLHnHSFSfdpSVWALFWPLLTGGTIVLadVRTME 661
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNgyfIGERLG---LTEQDrlcipVPLF-HCFG---SVLGVLACLTHGATMVF--PSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 662 DSTALLDLMIRHDVSVLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSGGEVLNPELAHKIQKVWQ-ADVANLYGPTEAT-- 736
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFIAELEHPdFDKfDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSpv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 -----IDAlyfSIDKNAAgaiPIGYPIDNTDAYIVDLNLNPVPP-GVPGEIMLAGQNLARGYLGKPAQTAQrflpnPFGN 810
Cdd:cd05917 160 stqtrTDD---SIEKRVN---TVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAE-----AIDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 811 GRVYATGDLGRRWSSGAISYLGR-RDqqVKIRG------HRIElnevahllcQALELKEAIVFAQHAGTEQARL----VA 879
Cdd:cd05917 229 DGWLHTGDLAVMDEDGYCRIVGRiKD--MIIRGgeniypREIE---------EFLHTHPKVSDVQVVGVPDERYgeevCA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 37542635 880 AIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05917 298 WIRLKEGaeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
587-924 |
7.99e-23 |
|
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: 100.94 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 587 YLIYTSGSTGVPKGVVVEHRQ-----VVNNILWRqrtwpLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVladVRTME 661
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSwiesfVCNEDLFN-----ISGEDAILAPGPLSHSLFLYGAISALYLGGTFI---GQRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 662 DSTALLDLMIRHDVSVLGGVPSLLGTLIDHpfANDCRAVKLVLSGGEVLNPELAHKIQKVW-QADVANLYGPTEATIdaL 740
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPTMLQALART--LEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSF--I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 741 YFSIDKNAAGAIPIGYPIDNTDAYIVDLNlnpvpPGVPGEIMLAGQNLARGYLgkpaqtaqrfLPNPFGNGRVYATGDLG 820
Cdd:cd17633 152 TYNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYV----------RGGFSNPDGWMSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 821 RRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQAR---LVAAIEQQPGLHSEGIKQELL 897
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVV----GIPDARfgeIAVALYSGDKLTYKQLKRFLK 292
|
330 340
....*....|....*....|....*..
gi 37542635 898 RHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
26-425 |
8.73e-23 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 103.57 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 26 YPLSSEQKRLWLLAQLAGTAT---LPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFV-EVLERPVRLLMPTGLVKL 101
Cdd:pfam00668 5 YPLSPAQKRMWFLEKLEPHSSaynMPAVLK--LTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 102 EYFDRPPSDADMAELIGAA---------FELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLF------- 165
Cdd:pfam00668 83 EIIDISDLSESEEEEAIEAfiqrdlqspFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLAdlyqqll 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 166 -----QTEPDHQYpavgaiAEVFQREQTLAQDAQITEQ---WQQWGIGLQAPAAteIPTENPRPAiKGS----------D 227
Cdd:pfam00668 163 kgeplPLPPKTPY------KDYAEWLQQYLQSEDYQKDaayWLEQLEGELPVLQ--LPKDYARPA-DRSfkgdrlsftlD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 228 RQVHEALTAwgdqpVAEAEIV-------SSWLTVLMRWQGSQSALCAIKVRDKAHANL---IGPLQTYLPVRVDMPDGST 297
Cdd:pfam00668 234 EDTEELLRK-----LAKAHGTtlndvllAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIermVGMFVNTLPLRIDPKGGKT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 298 LAQLRLQVEEQLNG-NDHPS--FSTLLEVCPPKRDLSRTPYFQTGLQFIAHD-----VEQRDFHAGNLTRLPTKQPSSDL 369
Cdd:pfam00668 309 FSELIKRVQEDLLSaEPHQGypFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLgqdsqEEEFQLSELDLSVSSVIEEEAKY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 370 DLFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVL---SAPGEQPIATVALMGQ 425
Cdd:pfam00668 389 DLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLeqaIAHPSQPLSELDLLSD 447
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
457-923 |
1.08e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 103.80 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 457 KSPLAVAV-IDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:PRK07514 14 ADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITSDqqSVEGWpqVARI-------RMEALD--------------PDIRWVAPTGLShsDAAYLIYTSGS 594
Cdd:PRK07514 94 YFIGDAEPALVVCDP--ANFAW--LSKIaaaagapHVETLDadgtgslleaaaaaPDDFETVPRGAD--DLAAILYTSGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 595 TGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HsfsfdpsVWALFWP----LLTGGTIVLAdvrTMEDSTAL 666
Cdd:PRK07514 168 TGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHAlpifH-------THGLFVAtnvaLLAGASMIFL---PKFDPDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 667 LDLMIRhdVSVLGGVPSLLGTLIDHP-FAND-CRAVKLVLSGGEVLNPElahkIQKVWQADV--ANL--YGPTEATIdal 740
Cdd:PRK07514 238 LALMPR--ATVMMGVPTFYTRLLQEPrLTREaAAHMRLFISGSAPLLAE----THREFQERTghAILerYGMTETNM--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 741 yfsIDKNA------AGAipIGYPIDNTDAYIVDLNLN-PVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrv 813
Cdd:PRK07514 309 ---NTSNPydgerrAGT--VGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 814 YATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKE-AIVFAQHAGTEQArLVAAIEQQPG--LHSE 890
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVEsAVIGVPHPDFGEG-VTAVVVPKPGaaLDEA 457
|
490 500 510
....*....|....*....|....*....|...
gi 37542635 891 GIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK07514 458 AILAALKGRLARFKQPKRVFFVDELPRNTMGKV 490
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
498-928 |
1.12e-22 |
|
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: 104.08 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQ-----------------------QSV 554
Cdd:cd05928 70 VAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDElapevdsvasecpslktkllvseKSR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 555 EGWPQVARIRMEALDPDIrwVAPTGlsHSDAAYLIYTSGSTGVPKgvVVEHRQ-------VVNNILWRQrtwpLTAQDnV 627
Cdd:cd05928 150 DGWLNFKELLNEASTEHH--CVETG--SQEPMAIYFTSGTTGSPK--MAEHSHsslglglKVNGRYWLD----LTASD-I 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 628 LHNHSFS--FDPSVWALFWPLLTGGTIVladVRTME--DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN-DCRAVKL 702
Cdd:cd05928 219 MWNTSDTgwIKSAWSSLFEPWIQGACVF---VHHLPrfDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSyKFPSLQH 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 703 VLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIM 782
Cdd:cd05928 296 CVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGS--MGKASPPYDVQIIDDNGNVLPPGTEGDIG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 783 LAGQ-----NLARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQA 857
Cdd:cd05928 374 IRVKpirpfGLFSGYVDNPEKTAATI------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEH 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 858 LELKEAIVFAQHAGTEQARLVAAIEQQPGLHS---EGIKQELLRHLPA----YLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05928 448 PAVVESAVVSSPDPIRGEVVKAFVVLAPQFLShdpEQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
445-936 |
1.17e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 103.92 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 445 LTLTEWVAASTEksPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFL- 523
Cdd:PRK10946 25 LPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 524 ---------------PIDPRL-----------PTDRIQFLIENSGCELVIT----SDQQSVEGWpqvarirMEALDPDIr 573
Cdd:PRK10946 103 alfshqrselnayasQIEPALliadrqhalfsDDDFLNTLVAEHSSLRVVLllndDGEHSLDDA-------INHPAEDF- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 574 WVAPTGlsHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL------HNHSFSfDPSVWALFwplL 647
Cdd:PRK10946 175 TATPSP--ADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLcalpaaHNYPMS-SPGALGVF---L 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 648 TGGTIVLAdvrtmEDSTALL--DLMIRHDVSVLGGVPSLLGTLIDHPFANDCRA----VKLVLSGGEVLNPELAHKIQKV 721
Cdd:PRK10946 249 AGGTVVLA-----PDPSATLcfPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAqlasLKLLQVGGARLSETLARRIPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 722 WQADVANLYGPTEATIDalYFSIDKNAAGAIPI-GYPIDNTD-AYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQT 799
Cdd:PRK10946 324 LGCQLQQVFGMAEGLVN--YTRLDDSDERIFTTqGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 800 AQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCqalelkeaivfaQHAGTEQARLVA 879
Cdd:PRK10946 402 ASAFDANGF-----YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL------------RHPAVIHAALVS 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 880 AIEQQPGLHS-------EGIKQ-ELLRHLPA-----YLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQL 936
Cdd:PRK10946 465 MEDELMGEKScaflvvkEPLKAvQLRRFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
442-923 |
1.88e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 103.54 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 442 PPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG-- 519
Cdd:PRK05605 29 YGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGav 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 ---HAFLPIDPRLP-----------------TDRIQFLIENSGCELVITSDQqsVEGWPQVARIRM-----------EAL 568
Cdd:PRK05605 109 vveHNPLYTAHELEhpfedhgarvaivwdkvAPTVERLRRTTPLETIVSVNM--IAAMPLLQRLALrlpipalrkarAAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 569 ----DPDIRW---VAPTGL------SH-----SDAAYLIYTSGSTGVPKGVVVEHRQVVNNILwRQRTW--PLTAQDNVL 628
Cdd:PRK05605 187 tgpaPGTVPWetlVDAAIGgdgsdvSHprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAWvpGLGDGPERV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 629 HN-----HSFSFdpSVWALFWPLlTGGTIVLADVRTMEdstALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVK 701
Cdd:PRK05605 266 LAalpmfHAYGL--TLCLTLAVS-IGGELVLLPAPDID---LILDAMKKHPPTWLPGVPPLYEKIAEAAEERgvDLSGVR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 702 LVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNA-AGAIpiGYPIDNTDAYIVDLNlNP---VPPGV 777
Cdd:PRK05605 340 NAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRrPGYV--GVPFPDTEVRIVDPE-DPdetMPDGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 778 PGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvyATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQA 857
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNRPEETAKSFLDGWF------RTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 858 LELKEAIV--FAQHAGTEqaRLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK05605 491 PGVEDAAVvgLPREDGSE--EVVAAVVLEPGaaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
439-833 |
4.22e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 102.87 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 439 RTTPPQLTLTEWVAASTEKSPLAVAVI--DHG--QQLSYAELWARAALVAAN-ISQHVaKPRSIIAVALPRSAEFIAALL 513
Cdd:COG1022 5 SDVPPADTLPDLLRRRAARFPDRVALRekEDGiwQSLTWAEFAERVRALAAGlLALGV-KPGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 514 GVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQsvegwpQVARIRmEALD--PDIRWV---------------- 575
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQE------QLDKLL-EVRDelPSLRHIvvldprglrddprlls 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 576 -------------------APTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLhnhsfSFD 636
Cdd:COG1022 157 ldellalgrevadpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-----SFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 637 PSVWAL-----FWPLLTGGTIV-----------LADVR--------------------TMEDSTAL--------LDLMIR 672
Cdd:COG1022 232 PLAHVFertvsYYALAAGATVAfaespdtlaedLREVKptfmlavprvwekvyagiqaKAEEAGGLkrklfrwaLAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 673 HDVSVLGGVPSLLGTLIDHPFANdcravKLVL---------------SGGEVLNPELAHkiqkVWQA---DVANLYGPTE 734
Cdd:COG1022 312 YARARLAGKSPSLLLRLKHALAD-----KLVFsklrealggrlrfavSGGAALGPELAR----FFRAlgiPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 735 ATIDALYFSIDKNAAGAipIGYPIDNTDAYIVDlnlnpvppgvPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvY 814
Cdd:COG1022 383 TSPVITVNRPGDNRIGT--VGPPLPGVEVKIAE----------DGEILVRGPNVMKGYYKNPEATAEAFDADGW-----L 445
|
490
....*....|....*....
gi 37542635 815 ATGDLGRRWSSGAISYLGR 833
Cdd:COG1022 446 HTGDIGELDEDGFLRITGR 464
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
498-934 |
5.62e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAGHAFLPIDPrLPTDR-----------------------IQFLIENSGCELVITSDQQSV 554
Cdd:PRK08751 79 VALMMPNCLQYPIATFGVLRAGLTVVNVNP-LYTPRelkhqlidsgasvlvvidnfgttVQQVIADTPVKQVITTGLGDM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 555 EGWPQVARIR-----MEALDPD------IRW-----------VAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI 612
Cdd:PRK08751 158 LGFPKAALVNfvvkyVKKLVPEyringaIRFrealalgrkhsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 613 L----WRQRTWPLTAQDNVLHN-----HSFSFDPSvwALFWPLLTGGTIVLADVRTMEdstALLDLMIRHDVSVLGGVPS 683
Cdd:PRK08751 238 QqahqWLAGTGKLEEGCEVVITalplyHIFALTAN--GLVFMKIGGCNHLISNPRDMP---GFVKELKKTRFTAFTGVNT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 684 LLGTLIDHP-FAN-DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSID-KNAAGAipIGYPIDN 760
Cdd:PRK08751 313 LFNGLLNTPgFDQiDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTlKEYNGS--IGLPIPS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKI 840
Cdd:PRK08751 391 TDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW-----LHTGDIARMDEQGFVYIVDRKKDMILV 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 841 RGHRI---ELNEVAHLLCQALELKEAIVFAQHAGteQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPR 917
Cdd:PRK08751 466 SGFNVypnEIEDVIAMMPGVLEVAAVGVPDEKSG--EIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPK 543
|
490
....*....|....*..
gi 37542635 918 TATGKVDMLKLDQLAAP 934
Cdd:PRK08751 544 TNVGKILRRELRDAAKA 560
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
586-924 |
7.41e-22 |
|
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: 98.17 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 586 AYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTmedstA 665
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ-----A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 666 LLDLMIRHDVSVLGGVPSLLGTLIDHPFANDC-RAVKLVLSGGEVLNPELAHKIQK----VWQAdvanlYGPTEAtidal 740
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAAlKSLRAVLLGGAPIPPELLERAADrgipLYTT-----YGMTET----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 741 yfsidknaAGAIPIGYPIDNTDAYivdlnLNPVPPGV------PGEIMLAGQNLARGYLGKPaqtaqrfLPNPFGNGRVY 814
Cdd:cd17630 148 --------ASQVATKRPDGFGRGG-----VGVLLPGRelriveDGEIWVGGASLAMGYLRGQ-------LVPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 815 ATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQ 894
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRA 287
|
330 340 350
....*....|....*....|....*....|
gi 37542635 895 ELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
461-936 |
1.51e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 100.62 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIEN 540
Cdd:PRK12583 36 ALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 541 SGCELVITSD--------QQSVEGWPQVARIRMEALD----PDIRWV-----APTG------------------------ 579
Cdd:PRK12583 116 SGVRWVICADafktsdyhAMLQELLPGLAEGQPGALAcerlPELRGVvslapAPPPgflawhelqargetvsrealaerq 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 580 --LSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDN----VLHNHSFSFdpsVWALFWPLLTGGTIV 653
Cdd:PRK12583 196 asLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlcvpVPLYHCFGM---VLANLGCMTVGACLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 654 --------LADVRTMEDSTAlldlmirhdvSVLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSGGEVLNPELAHK-IQKVW 722
Cdd:PRK12583 273 ypneafdpLATLQAVEEERC----------TALYGVPTMFIAELDHPqRGNfDLSSLRTGIMAGAPCPIEVMRRvMDEMH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 723 QADVANLYGPTEATIdalyFSIDKNAAGAIP-----IGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPA 797
Cdd:PRK12583 343 MAEVQIAYGMTETSP----VSLQTTAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 798 QTAQRFlpnpFGNGRVYaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTEq 874
Cdd:PRK12583 419 ATAESI----DEDGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGvpdEKYGEE- 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 875 arLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQL 936
Cdd:PRK12583 493 --IVAWVRLHPGhaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEEL 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
564-923 |
1.99e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 100.13 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 564 RMEALDPDIrwvaptglSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILwrQRTWpltAQDNVLHN------------H 631
Cdd:PRK08974 195 RMQYVKPEL--------VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE--QAKA---AYGPLLHPgkelvvtalplyH 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 632 SFSFdpSVWALFWPLLTGGTIVLADVRtmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSGGEV 709
Cdd:PRK08974 262 IFAL--TVNCLLFIELGGQNLLITNPR---DIPGFVKELKKYPFTAITGVNTLFNALLNNEeFQElDFSSLKLSVGGGMA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 710 LNPELAHKIQKVWQADVANLYGPTEAT--IDALYFSIDKNAAGaipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQN 787
Cdd:PRK08974 337 VQQAVAERWVKLTGQYLLEGYGLTECSplVSVNPYDLDYYSGS---IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 788 LARGYLGKPAQTAqrflpNPFGNGRVyATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKE-AIVF 866
Cdd:PRK08974 414 VMLGYWQRPEATD-----EVIKDGWL-ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEvAAVG 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 867 AQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK08974 488 VPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
442-800 |
2.50e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 99.67 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 442 PPQLTLTEWVAASTEKSPLAVAVID--HGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG 519
Cdd:PLN02246 20 PNHLPLHDYCFERLSEFSDRPCLIDgaTGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 HAFLPIDPRLPTDRIQFLIENSGCELVITsdqQSvegwPQVARIRMEALDPDIRWVA----PTGLSH------------- 582
Cdd:PLN02246 100 AVTTTANPFYTPAEIAKQAKASGAKLIIT---QS----CYVDKLKGLAEDDGVTVVTiddpPEGCLHfseltqadenelp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 583 ------SDAAYLIYTSGSTGVPKGVVVEHRQVVNNI----------LWrqrtwpLTAQDNVL------HNHSFSfdpSVw 640
Cdd:PLN02246 173 eveispDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaqqvdgenpnLY------FHSDDVILcvlpmfHIYSLN---SV- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 641 aLFWPLLTGGTIVLadvrtME--DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVLNPELAH 716
Cdd:PLN02246 243 -LLCGLRVGAAILI-----MPkfEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEkyDLSSIRMVLSGAAPLGKELED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 717 KIQ-KVWQADVANLYGPTEA-TIDALY-------FSIDKNAAGAIpigypIDNTDAYIVDLNLN-PVPPGVPGEIMLAGQ 786
Cdd:PLN02246 317 AFRaKLPNAVLGQGYGMTEAgPVLAMClafakepFPVKSGSCGTV-----VRNAELKIVDPETGaSLPRNQPGEICIRGP 391
|
410
....*....|....
gi 37542635 787 NLARGYLGKPAQTA 800
Cdd:PLN02246 392 QIMKGYLNDPEATA 405
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
460-839 |
4.68e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 99.20 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 460 LAVAVIDHG--------QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG------------ 519
Cdd:PRK09274 23 LAVAVPGGRgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGavpvlvdpgmgi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 ------------HAFLPIdPRLPTDRIQFLIENSGCELVITSDQQSVEGWPQVARIRM--EALDPDIRWVAPTglshsDA 585
Cdd:PRK09274 103 knlkqclaeaqpDAFIGI-PKAHLARRLFGWGKPSVRRLVTVGGRLLWGGTTLATLLRdgAAAPFPMADLAPD-----DM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 586 AYLIYTSGSTGVPKGVVVEHRQvvnnilwrqrtwpLTAQDNVLHNHsFSFDPS--------VWALFWPLLtGGTIVLADv 657
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGM-------------FEAQIEALRED-YGIEPGeidlptfpLFALFGPAL-GMTSVIPD- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 658 rtME-------DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCR--AVKLVLSGGEVLNPELAHKIQKVW--QADV 726
Cdd:PRK09274 241 --MDptrpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKlpSLRRVISAGAPVPIAVIERFRAMLppDAEI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 727 ANLYGPTEA----TI---DALYFSIDKNAAGA-IPIGYPIDNTDAYIVDLNLNP---------VPPGVPGEIMLAGQNLA 789
Cdd:PRK09274 319 LTPYGATEAlpisSIesrEILFATRAATDNGAgICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVAGPMVT 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 37542635 790 RGYLGKPAQTAQRFLPNPFGnGRVYATGDLGRRWSSGAISYLGRRDQQVK 839
Cdd:PRK09274 399 RSYYNRPEATRLAKIPDGQG-DVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
451-923 |
5.95e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.53 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 451 VAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLP 530
Cdd:PRK13383 41 LAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 531 TDRIQFLIENSGCELVITSDQ--QSVEGW--------PQVARIRMEALDPDirwVAPTGlshsdaAYLIYTSGSTGVPKG 600
Cdd:PRK13383 121 SDALAAALRAHHISTVVADNEfaERIAGAddavavidPATAGAEESGGRPA---VAAPG------RIVLLTSGTTGKPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 601 V-----VVEHRQVVNNILWRQRTWP---LTAQDNVLHNHSFSFdpsvwaLFWPLLTGGTIVladVRTMEDSTALLDLMIR 672
Cdd:PRK13383 192 VprapqLRSAVGVWVTILDRTRLRTgsrISVAMPMFHGLGLGM------LMLTIALGGTVL---THRHFDAEAALAQASL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 673 HDVSVLGGVPSLLGTLIDHP----FANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNA 748
Cdd:PRK13383 263 HRADAFTAVPVVLARILELPprvrARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 749 AGAIpIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGkpaqtaqrflpnpfGNGR-----VYATGDLGRRW 823
Cdd:PRK13383 343 APET-VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD--------------GGGKavvdgMTSTGDMGYLD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 824 SSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQELLRHLP 901
Cdd:PRK13383 408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGsgVDAAQLRDYLKDRVS 487
|
490 500
....*....|....*....|..
gi 37542635 902 AYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK13383 488 RFEQPRDINIVSSIPRNPTGKV 509
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
468-923 |
1.29e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.59 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHVA-KPRSIIAVALPRSAEFIAALLGVVRAG----------------HAFLPIDPR-- 528
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLQQHTDlVPGDRIAVQMPNVLQYPIAVFGALRAGlivvntnplytaremrHQFKDSGARal 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 529 -------------LPTDRIQFLIENSGCELvitsdQQSVEGW------------------PQVARIRMEALDPDIRWVAP 577
Cdd:PRK12492 127 vylnmfgklvqevLPDTGIEYLIEAKMGDL-----LPAAKGWlvntvvdkvkkmvpayhlPQAVPFKQALRQGRGLSLKP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 578 TGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI----------------LWRQRTWPLTAQDNVLHNHSFSFDpsvwa 641
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraclsqlgpdgqpLMKEGQEVMIAPLPLYHIYAFTAN----- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 642 LFWPLLTGGTIVLadVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSGGEVLNPELAHKIQ 719
Cdd:PRK12492 277 CMCMMVSGNHNVL--ITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPgFKDlDFSALKLTNSGGTALVKATAERWE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 720 KVWQADVANLYGPTEATIDAlyfsiDKNAAGAIP----IGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGK 795
Cdd:PRK12492 355 QLTGCTIVEGYGLTETSPVA-----STNPYGELArlgtVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 796 PAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKE--AIVFAQHAGTE 873
Cdd:PRK12492 430 PEATAEALDAEGW-----FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANcaAIGVPDERSGE 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 37542635 874 QARLVaAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK12492 505 AVKLF-VVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
1063-1334 |
1.38e-20 |
|
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187539 [Multi-domain] Cd Length: 318 Bit Score: 94.27 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRTTsRVICLCRAKDaehaKARILEGLktyridvgsel*RVEYLTGDLALPHlglsehqwq 1142
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQGY-RVRALVRSGS----DAVLLDGL------------PVEVVEGDLTDAA--------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 TLA---EEVDVIYHNGALVNFVYPY-SALKATNVGGTQAILELACTARLKSVQYVSTVDtllATHVPRPFIEDDAPLRSA 1218
Cdd:cd05228 55 SLAaamKGCDRVFHLAAFTSLWAKDrKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIA---ALGGPPDGRIDETTPWNE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1219 VGVPVGYTGSKWVAEGVANLGLRRGIPVSIFRPGLILG-HTETGASQSIDyLLVALRGFLPmGIVPDYpriFDIVPVDYV 1297
Cdd:cd05228 132 RPFPNDYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFGpGDEGPTSTGLD-VLDYLNGKLP-AYPPGG---TSFVDVRDV 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 37542635 1298 AAAivHISMQPQGRDKFFHLFNPAPVTIRQFCDWIRE 1334
Cdd:cd05228 207 AEG--HIAAMEKGRRGERYILGGENLSFKQLFETLAE 241
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
437-927 |
2.02e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 97.25 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 437 GPRTTPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAanisqHVAKPRSI-----IAVALPRSAEFIAA 511
Cdd:PRK08279 29 ALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYA-----HWAAARGVgkgdvVALLMENRPEYLAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 512 LLGVVRAG----------------HAFLPIDPRL---------PTDRIQFLIENSGCELVITSDQ-QSVEGWPQVARirM 565
Cdd:PRK08279 104 WLGLAKLGavvallntqqrgavlaHSLNLVDAKHlivgeelveAFEEARADLARPPRLWVAGGDTlDDPEGYEDLAA--A 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 566 EALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQD---NVL---HNHSFSFDPSV 639
Cdd:PRK08279 182 AAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDvlyCCLplyHNTGGTVAWSS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 640 walfwPLLTGGTIVLA----------DVRtmedstalldlmiRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEV 709
Cdd:PRK08279 262 -----VLAAGATLALRrkfsasrfwdDVR-------------RYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 710 LNPElahkiqkVWQA--------DVANLYGPTEATIdALY--FSIDkNAAGAIP---------IGYPIDnTDAYIVDLN- 769
Cdd:PRK08279 324 LRPD-------IWDEfqqrfgipRILEFYAASEGNV-GFInvFNFD-GTVGRVPlwlahpyaiVKYDVD-TGEPVRDADg 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 770 -LNPVPPGVPGEimLAGQNLAR----GYlGKPAQTAQRFLPNPFGNGRVY-ATGDLGRRWSSGAISYLGRRDQQVKIRGH 843
Cdd:PRK08279 394 rCIKVKPGEVGL--LIGRITDRgpfdGY-TDPEASEKKILRDVFKKGDAWfNTGDLMRDDGFGHAQFVDRLGDTFRWKGE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 844 RIELNEVAHLLCQALELKEAIVFA-QHAGTEQARLVAAI--EQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTAT 920
Cdd:PRK08279 471 NVATTEVENALSGFPGVEEAVVYGvEVPGTDGRAGMAAIvlADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGT 550
|
570
....*....|
gi 37542635 921 ---GKVDMLK 927
Cdd:PRK08279 551 fkyRKVDLRK 560
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
471-932 |
2.29e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 95.71 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD 550
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QqsvegwpqvarirmealdpdirwvaptglSHSDAAYLIY-TSGSTGVPKgvVVEHRQvvnnilwrqRTWP--------- 620
Cdd:cd05974 81 N-----------------------------THADDPMLLYfTSGTTSKPK--LVEHTH---------RSYPvghlstmyw 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 621 --LTAQDNVLHNHSFSFDPSVWALFWPLLTGGTIVLADVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCR 698
Cdd:cd05974 121 igLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 AVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDAlyfsidKNAAGAI----PIGYPIDNTDAYIVDLNLNPVp 774
Cdd:cd05974 201 KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV------GNSPGQPvkagSMGRPLPGYRVALLDPDGAPA- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 775 pgVPGEIMLA-GQN----LARGYLGKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNE 849
Cdd:cd05974 274 --TEGEVALDlGDTrpvgLMKGYAGDPDKTAHAM------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 850 VAHLLCQALELKEAIVF----AQHAGTEQARLVAAIEQQPglhSEGIKQELLRHLPAYLIPSQ---LLLLDELPRTATGK 922
Cdd:cd05974 346 LESVLIEHPAVAEAAVVpspdPVRLSVPKAFIVLRAGYEP---SPETALEIFRFSRERLAPYKrirRLEFAELPKTISGK 422
|
490
....*....|
gi 37542635 923 VDMLKLDQLA 932
Cdd:cd05974 423 IRRVELRRRE 432
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
451-923 |
3.25e-20 |
|
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: 96.41 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 451 VAASTEKSPLAVAVI---DHG--QQLSYAELwARAALVAANISQHVAKPRS-IIAVALPRSAEFIAALLGVVRAGHAFLP 524
Cdd:cd05970 23 VDAMAKEYPDKLALVwcdDAGeeRIFTFAEL-ADYSDKTANFFKAMGIGKGdTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPRLPTDRIQFLIENSGCELVITSDQQSV-------------------------EGWPQVARIRMEAlDPDI-RWVAPT 578
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEDNIpeeiekaapecpskpklvwvgdpvpEGWIDFRKLIKNA-SPDFeRPTANS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 579 GLSHSDAAYLIYTSGSTGVPKgvVVEHrqvvnnilwrQRTWPL----TA------QDNVLHnhsFSFDPSVWA------L 642
Cdd:cd05970 181 YPCGEDILLVYFSSGTTGMPK--MVEH----------DFTYPLghivTAkywqnvREGGLH---LTVADTGWGkavwgkI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 643 FWPLLTGGTIVLADVRtMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN-DCRAVKLVLSGGEVLNPELAHKIQKV 721
Cdd:cd05970 246 YGQWIAGAAVFVYDYD-KFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRyDLSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 722 WQADVANLYGPTEATIDALYFSIDKNAAGAI--PI-GYPIDntdayIVDLNLNPVPPGVPGEIMLAGQN-----LARGYL 793
Cdd:cd05970 325 TGIKLMEGFGQTETTLTIATFPWMEPKPGSMgkPApGYEID-----LIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 794 GKPAQTAQRFLPNpfgngrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA----QH 869
Cdd:cd05970 400 KDAEKTAEVWHDG------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGvpdpIR 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 870 AGTEQARLVAAIEQQPGlhsEGIKQELLRHL----PAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05970 474 GQVVKATIVLAKGYEPS---EELKKELQDHVkkvtAPYKYPRIVEFVDELPKTISGKI 528
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
584-924 |
3.32e-20 |
|
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: 94.37 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVvvehrqvvnniLWRQRTWPLTAQDNVLH-----------------NHSFSFDP--------S 638
Cdd:cd05924 4 DDLYILYTGGTTGMPKGV-----------MWRQEDIFRMLMGGADFgtgeftpsedahkaaaaAAGTVMFPapplmhgtG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 639 VWALFWPLLTGGTIVLADVRTmeDSTALLDLMIRHDVSVLGGV-PSLLGTLID-----HPFanDCRAVKLVLSGGEVLNP 712
Cdd:cd05924 73 SWTAFGGLLGGQTVVLPDDRF--DPEEVWRTIEKHKVTSMTIVgDAMARPLIDalrdaGPY--DLSSLFAISSGGALLSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 713 ELAHKIQK-VWQADVANLYGPTEATidalyFSIDKNAAGAIPIGYPID--NTDAYIVDLNLNPVPPGVPGEIMLAGQ-NL 788
Cdd:cd05924 149 EVKQGLLElVPNITLVDAFGSSETG-----FTGSGHSAGSGPETGPFTraNPDTVVLDDDGRVVPPGSGGVGWIARRgHI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 789 ARGYLGKPAQTAQRFlpnPFGNGRVYA-TGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAhllcQALELKEAIVFA 867
Cdd:cd05924 224 PLGYYGDEAKTAETF---PEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVE----EALKSHPAVYDV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37542635 868 QHAGTEQARL---VAAIEQ-QPGLHSEGikQELLRH----LPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd05924 297 LVVGRPDERWgqeVVAVVQlREGAGVDL--EELREHcrtrIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
440-932 |
3.73e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 96.35 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 440 TTPPQLTLTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG 519
Cdd:PRK06164 5 AAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 HAFLPIDPRLPTDRIQFLIENSGCELVITS---------------DQQSVEGWPQVARIRMEALD-PD---IRWVAPTGL 580
Cdd:PRK06164 85 ATVIAVNTRYRSHEVAHILGRGRARWLVVWpgfkgidfaailaavPPDALPPLRAIAVVDDAADAtPApapGARVQLFAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 581 -------------SHSDAAYLIYT-SGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHSFSFDPSVWALFWPL 646
Cdd:PRK06164 165 pdpappaaageraADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 647 LTGGTIVLADVRtmeDSTALLDLMIRHDVSvlggvpsllgtlidHPFANDCRAVKLVLSGGE-------------VLNPE 713
Cdd:PRK06164 245 AGGAPLVCEPVF---DAARTARALRRHRVT--------------HTFGNDEMLRRILDTAGEradfpsarlfgfaSFAPA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 714 LAHKIQKVWQADV--ANLYGPTEatIDALYFSIDKNAAGAIPI---GYPID-NTDAYIVDLNLNPV-PPGVPGEIMLAGQ 786
Cdd:PRK06164 308 LGELAALARARGVplTGLYGSSE--VQALVALQPATDPVSVRIeggGRPASpEARVRARDPQDGALlPDGESGEIEIRAP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 787 NLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHllcqALELKEAIVF 866
Cdd:PRK06164 386 SLMRGYLDNPDATARALTDDGY-----FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH----ALEALPGVAA 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 867 AQHAGTE---QARLVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATG---KVDMLKLDQLA 932
Cdd:PRK06164 457 AQVVGATrdgKTVPVAFVIPTDGasPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
468-923 |
5.24e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 95.99 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHV-AKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPrLPTDRI---QF------- 536
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQQHTdLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNP-LYTAREmehQFndsgaka 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 537 -------------LIENSGCELVITSDQQSVEgwPQVARIRMEALDPDI------------------------RWVAPTG 579
Cdd:PRK05677 126 lvclanmahlaekVLPKTGVKHVIVTEVADML--PPLKRLLINAVVKHVkkmvpayhlpqavkfndalakgagQPVTEAN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 580 LSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILwrQRTWPLTAQDN-----------VLHNHSFSFDPSVWalfwpLLT 648
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML--QCRALMGSNLNegceiliaplpLYHIYAFTFHCMAM-----MLI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 649 GG-TIVLADVRtmeDSTALLDLMIRHDVSVLGGVPSLLGTLI-DHPFAN-DCRAVKLVLSGGEVLNPELAHKIQKVWQAD 725
Cdd:PRK05677 277 GNhNILISNPR---DLPAMVKELGKWKFSGFVGLNTLFVALCnNEAFRKlDFSALKLTLSGGMALQLATAERWKEVTGCA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 726 VANLYGPTEATIDALYFSIDKNAAGAIpiGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLP 805
Cdd:PRK05677 354 ICEGYGMTETSPVVSVNPSQAIQVGTI--GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 806 NPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKE--AIVFAQHAGTEQARLVAAIEQ 883
Cdd:PRK05677 432 DGW-----LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcaAIGVPDEKSGEAIKVFVVVKP 506
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 37542635 884 QPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK05677 507 GETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKI 546
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
463-923 |
7.21e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 95.47 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 463 AVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPrLPTDR-IQFLIENS 541
Cdd:PRK07059 41 AFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNP-LYTPReLEHQLKDS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 542 GCELVI-----TSDQQSVEGWPQVARI---------------------RMEALDPdiRW-------------------VA 576
Cdd:PRK07059 120 GAEAIVvlenfATTVQQVLAKTAVKHVvvasmgdllgfkghivnfvvrRVKKMVP--AWslpghvrfndalaegarqtFK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 577 PTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILwRQRTWPLTAQDNVLHNHSFSFdpsVWALfwPL-----LT--- 648
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEAWLQPAFEKKPRPDQLNF---VCAL--PLyhifaLTvcg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 649 ------GGTIVL-ADVRtmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP-FAN-DCRAVKLVLSGGEVLNPELAHKIQ 719
Cdd:PRK07059 272 llgmrtGGRNILiPNPR---DIPGFIKELKKYQVHIFPAVNTLYNALLNNPdFDKlDFSKLIVANGGGMAVQRPVAERWL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 720 KVWQADVANLYGPTE----AT---IDALYFSidknaaGAipIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGY 792
Cdd:PRK07059 349 EMTGCPITEGYGLSEtspvATcnpVDATEFS------GT--IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 793 LGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRI---ELNEVAHLLCQALELKEAIVFAQH 869
Cdd:PRK07059 421 WNRPDETAKVMTADGF-----FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVypnEIEEVVASHPGVLEVAAVGVPDEH 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 37542635 870 AGtEQARLVaAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK07059 496 SG-EAVKLF-VVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKI 547
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
469-881 |
1.01e-19 |
|
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: 94.35 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVIt 548
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 549 sdqqsVEGwpqvarirmealDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVL 628
Cdd:cd17640 83 -----VEN------------DSD------------DLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 629 hnhsfSFDPSvWALF------WPLLTGGTIVLADVRTMEDstallDLMiRHDVSVLGGVPSLLGTL---IDHPFANDCRA 699
Cdd:cd17640 134 -----SILPI-WHSYersaeyFIFACGCSQAYTSIRTLKD-----DLK-RVKPHYIVSVPRLWESLysgIQKQVSKSSPI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 700 VKLV----LSGGEVLNP-----ELAHKIQKVWQA---DVANLYGPTEATIDALYFSIDKNAAGAipIGYPIDNTDAYIVD 767
Cdd:cd17640 202 KQFLflffLSGGIFKFGisgggALPPHVDTFFEAigiEVLNGYGLTETSPVVSARRLKCNVRGS--VGRPLPGTEIKIVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 768 LNLN-PVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNgrvyaTGDLGRRWSSGAISYLGR-RDQQVKIRGHRI 845
Cdd:cd17640 280 PEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN-----TGDLGWLTCGGELVLTGRaKDTIVLSNGENV 354
|
410 420 430
....*....|....*....|....*....|....*.
gi 37542635 846 ELNEVAHLLCQALELKEAIVFAQhagtEQARLVAAI 881
Cdd:cd17640 355 EPQPIEEALMRSPFIEQIMVVGQ----DQKRLGALI 386
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
28-240 |
2.35e-19 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 88.94 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 28 LSSEQKRLWLLAQLAGTATLPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEYFDR- 106
Cdd:COG4908 1 LSPAQKRFLFLEPGSNAYNIPAVLR--LEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDLs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 107 --PPSDAD------MAELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQT----------- 167
Cdd:COG4908 79 alPEPEREaeleelVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALyaallegeppp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 168 --EPDHQYpavgaiAEVFQREQTLAQDAQITEQWQQWGIGLQ-APAATEIPTENPRPAIKGS---------DRQVHEALT 235
Cdd:COG4908 159 lpELPIQY------ADYAAWQRAWLQSEALEKQLEYWRQQLAgAPPVLELPTDRPRPAVQTFrgatlsftlPAELTEALK 232
|
....*
gi 37542635 236 AWGDQ 240
Cdd:COG4908 233 ALAKA 237
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
426-933 |
5.22e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 93.10 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 426 QMQQTVLAQAHGPRTTPPQLTLTewvAAsteKSPLAVAVI--------DHGQQLSYAELWARAALVAANISQHVAKPRSI 497
Cdd:PRK07529 12 AIEAVPLAARDLPASTYELLSRA---AA---RHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAGHAFlPIDPRLPTDRIQFLIENSGCELVIT-SDQQSVEGWPQVARIRME---------- 566
Cdd:PRK07529 86 VAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTlGPFPGTDIWQKVAEVLAAlpelrtvvev 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 567 --------------------------------ALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILW 614
Cdd:PRK07529 165 dlarylpgpkrlavplirrkaharildfdaelARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 615 RQRTWPLTAQDNVLHN----HSFSFDPSVWAlfwPLLTGGTIVLA------DVRTMEDSTALLDlmiRHDVSVLGGVPSL 684
Cdd:PRK07529 245 GALLLGLGPGDTVFCGlplfHVNALLVTGLA---PLARGAHVVLAtpqgyrGPGVIANFWKIVE---RYRINFLSGVPTV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 685 LGTLIDHPF-ANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT-IDALYFSIDKNAAGAIpiGYPIDNTD 762
Cdd:PRK07529 319 YAALLQVPVdGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATcVSSVNPPDGERRIGSV--GLRLPYQR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 763 AYIVDLN-----LNPVPPGVPGEIMLAGQNLARGYLgKPAQTAqrflpNPFGNGRVYATGDLGRRWSSGAISYLGRRdQQ 837
Cdd:PRK07529 397 VRVVILDdagryLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNK-----GLWLEDGWLNTGDLGRIDADGYFWLTGRA-KD 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 838 VKIR-GHRIELNEVAhllcQALELKEAIVFA-------QHAGteqaRL-VAAIEQQPGlhSEGIKQELLRHLPAYL---- 904
Cdd:PRK07529 470 LIIRgGHNIDPAAIE----EALLRHPAVALAaavgrpdAHAG----ELpVAYVQLKPG--ASATEAELLAFARDHIaera 539
|
570 580 590
....*....|....*....|....*....|
gi 37542635 905 -IPSQLLLLDELPRTATGKVDMLKLDQLAA 933
Cdd:PRK07529 540 aVPKHVRILDALPKTAVGKIFKPALRRDAI 569
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
466-1040 |
7.45e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 93.69 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 466 DHGQQLSYAELWARAALVAANIsQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDP-----RLPTDRIQFLIEN 540
Cdd:PRK05691 36 GEGVVLSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesarRHHQERLLSIIAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 541 SGCELVITS----------DQQSVEGWPQVarIRMEALDPDI--RWVAPTgLSHSDAAYLIYTSGSTGVPKGVVVEHRQV 608
Cdd:PRK05691 115 AEPRLLLTVadlrdsllqmEELAAANAPEL--LCVDTLDPALaeAWQEPA-LQPDDIAFLQYTSGSTALPKGVQVSHGNL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 609 V-NNILWRQRTWPLTAQDNVL-------HNHS---------FSFDPSV-----WALFWPLL-------TGGTIV------ 653
Cdd:PRK05691 192 VaNEQLIRHGFGIDLNPDDVIvswlplyHDMGliggllqpiFSGVPCVlmspaYFLERPLRwleaiseYGGTISggpdfa 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 654 --LADVRTMEDSTALLDLMiRHDVSVLGGVPSLLGTLidhpfanDCRAVKLVLSGgevLNPElahKIQKVWQADVANLY- 730
Cdd:PRK05691 272 yrLCSERVSESALERLDLS-RWRVAYSGSEPIRQDSL-------ERFAEKFAACG---FDPD---SFFASYGLAEATLFv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 731 -------GPTEATIDALYFSIDKNAAGAIPI----GYPIDNTDAYIVDLN-LNPVPPGVPGEIMLAGQNLARGYLGKPAQ 798
Cdd:PRK05691 338 sggrrgqGIPALELDAEALARNRAEPGTGSVlmscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 799 TAQRFLPNpfgNGRVY-ATGDLGRRwSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELkeaivfaqhagTEQARL 877
Cdd:PRK05691 418 SAKTFVEH---DGRTWlRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEV-----------VRKGRV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 878 VA-AIEQQpGLHSEGIKQELLRHL-----PAYLI--------------PSQLLLLD--ELPRTATGKV---------DML 926
Cdd:PRK05691 483 AAfAVNHQ-GEEGIGIAAEISRSVqkilpPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLqrsacrlrlADG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 927 KLDQLAA-PQLNDAGGTECRAPRTDLEQSVMTDFAQVLGLTAVTPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFF 1005
Cdd:PRK05691 562 SLDSYALfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLF 641
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 37542635 1006 LTPTPAAVAQAIEIYRREGLT-----ALLSRQHA--QTLEQD 1040
Cdd:PRK05691 642 EAPTLAAFSAAVARQLAGGGAaqaaiARLPRGQAlpQSLAQN 683
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
467-923 |
1.18e-18 |
|
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: 91.78 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 467 HGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELV 546
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 547 ITSD---------------QQSVEGWPQVARIRME---------ALDPDIRW-----VAPTGLSHS---DAAYLIYTSGS 594
Cdd:cd05968 168 ITADgftrrgrevnlkeeaDKACAQCPTVEKVVVVrhlgndftpAKGRDLSYdeekeTAGDGAERTeseDPLMIIYTSGT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 595 TGVPKGVVVEHRqvvnnilwrqrTWPLTAQDNVlhNHSFSFDPS--------------VWALFWPLLTGGTIVLAD-VRT 659
Cdd:cd05968 248 TGKPKGTVHVHA-----------GFPLKAAQDM--YFQFDLKPGdlltwftdlgwmmgPWLIFGGLILGATMVLYDgAPD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 660 MEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP----FANDCRAVKLVLSGGEVLNPELAHKIQKVWQAD---VANLYGP 732
Cdd:cd05968 315 HPKADRLWRMVEDHEITHLGLSPTLIRALKPRGdapvNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGrnpIINYSGG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 733 TEAtidalyfsidknaAGAI----------PIGY--PIDNTDAYIVDLNLNPVPPGVpGEIMLAGQ--NLARGYLGKPA- 797
Cdd:cd05968 395 TEI-------------SGGIlgnvlikpikPSSFngPVPGMKADVLDESGKPARPEV-GELVLLAPwpGMTRGFWRDEDr 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 798 --QTAQRFLPNpfgngrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQA 875
Cdd:cd05968 461 ylETYWSRFDN------VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGE 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 876 RLVAAIEQQPGL-HSEGIKQELL----RHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:cd05968 535 AIVCFVVLKPGVtPTEALAEELMervaDELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
469-838 |
2.54e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 89.83 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRI-QFLIEnsgcelvi 547
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLkQCLQE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 548 tSDQQSVEGWPQvarirmeALDPdirwvaptglshsdaAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNV 627
Cdd:cd05910 73 -AEPDAFIGIPK-------ADEP---------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 628 LHnhsfSFDPsvWALFWPLLtGGTIVLADVRTME----DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCR--AVK 701
Cdd:cd05910 130 LA----TFPL--FALFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITlpSLR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 702 LVLSGGEVLNPELAHKIQKVW--QADVANLYGPTEATIDALYFSIDKNAAGAIP--------IGYPIDNTDAYIVDLNLN 771
Cdd:cd05910 203 RVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSIGSRELLATTTAAtsggagtcVGRPIPGVRVRIIEIDDE 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 772 P---------VPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPfGNGRVYATGDLGRRWSSGAISYLGRRDQQV 838
Cdd:cd05910 283 PiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN-SEGFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
469-937 |
3.49e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 89.95 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPI----DPRLPTDRIqfliENSGCE 544
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRL----EDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 545 LVITSD----QQSVEGWPQVARI------------------RMEALDP--DIRWVAPTglshsDAAYLIYTSGSTGVPKG 600
Cdd:PRK04319 148 VLITTPalleRKPADDLPSLKHVllvgedveegpgtldfnaLMEQASDefDIEWTDRE-----DGAILHYTSGSTGKPKG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 601 VVVEHRQVV--------------NNILWrqrtwpLTAqdnvlhnhsfsfDP-----SVWALFWPLLTGGTIVLADVR-TM 660
Cdd:PRK04319 223 VLHVHNAMLqhyqtgkyvldlheDDVYW------CTA------------DPgwvtgTSYGIFAPWLNGATNVIDGGRfSP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 661 EDSTALLDlmiRHDVSVLGGVPSLLGTLI---DHPFAN-DCRAVKLVLSGGEVLNPELAHKIQKV---------WQadva 727
Cdd:PRK04319 285 ERWYRILE---DYKVTVWYTAPTAIRMLMgagDDLVKKyDLSSLRHILSVGEPLNPEVVRWGMKVfglpihdnwWM---- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 728 nlygpTEatidalyfsidknaAGAIPI-------------GYPIDNTDAYIVDLNLNPVPPGVPGEIML-AG-QNLARGY 792
Cdd:PRK04319 358 -----TE--------------TGGIMIanypamdikpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 793 LGKPAQTAQRFLpnpfgnGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGT 872
Cdd:PRK04319 419 WNNPEKYESYFA------GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 873 EQARLVAAIEQQPGLH-SEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKVdMLKLdqLAAPQLN 937
Cdd:PRK04319 493 RGEIIKAFVALRPGYEpSEELKEEIRGFvkkgLGAHAAPREIEFKDKLPKTRSGKI-MRRV--LKAWELG 559
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
460-923 |
7.60e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 88.60 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 460 LAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIE 539
Cdd:PRK12406 1 MYATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 540 NSGCELVITSDQQ---------------SVEGWPQVA---RIRMEALDP---DIRW-------VAPTGLSHSDAAYLIYT 591
Cdd:PRK12406 81 DSGARVLIAHADLlhglasalpagvtvlSVPTPPEIAaayRISPALLTPpagAIDWegwlaqqEPYDGPPVPQPQSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 592 SGSTGVPKGV-----VVEHRQVVNNIlwRQRTWPLTAQDNVLHN----HSfsfDPSVWALFWPLLtGGTIVLadvRTMED 662
Cdd:PRK12406 161 SGTTGHPKGVrraapTPEQAAAAEQM--RALIYGLKPGIRALLTgplyHS---APNAYGLRAGRL-GGVLVL---QPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 663 STALLDLMIRHDVSVLGGVPSLLGTLIDHPFA----NDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATID 738
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrakYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 ALYFSIDknaAGAIP--IGYPIDNTDAYIVDLNLNPVPPGVPGEI-MLAGQNLARGYLGKPAQTAQrflpnpFGNGRVYA 815
Cdd:PRK12406 312 TFATSED---ALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIySRIAGNPDFTYHNKPEKRAE------IDRGGFIT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 816 TGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQAR----LVAAIEQQPG--LHS 889
Cdd:PRK12406 383 SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVF----GIPDAEfgeaLMAVVEPQPGatLDE 458
|
490 500 510
....*....|....*....|....*....|....
gi 37542635 890 EGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
27-416 |
8.55e-18 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 87.71 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQLAGT-ATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEYFD 105
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPsATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 106 RPPSDADMAELIGAA----FELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSL------------QRIAQTLFQTEP 169
Cdd:cd19538 83 KEVDEEELESEINEAvrypFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLapltrdlskayrARCKGEAPELAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 170 -DHQYpavgAIAEVFQREQ---TLAQDAQITEQWQQWGIGLQ-APAATEIPTENPRPA---IKGS------DRQVHEALT 235
Cdd:cd19538 163 lPVQY----ADYALWQQELlgdESDPDSLIARQLAYWKKQLAgLPDEIELPTDYPRPAessYEGGtltfeiDSELHQQLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 236 AwgdqpVAEAEIVSSWLtVLmrwqgsQSALCAIKVR-----------------DKAHANLIGPLQTYLPVRVDMPDGSTL 298
Cdd:cd19538 239 Q-----LAKDNNVTLFM-VL------QAGFAALLTRlgagtdipigspvagrnDDSLEDLVGFFVNTLVLRTDTSGNPSF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 299 AQLRLQVEEQ-LNGNDH---PsFSTLLEVCPPKRDLSRTPYFQtgLQFIAHDVEQRDFhagNLTRLPTK-QP----SSDL 369
Cdd:cd19538 307 RELLERVKETnLEAYEHqdiP-FERLVEALNPTRSRSRHPLFQ--IMLALQNTPQPSL---DLPGLEAKlELrtvgSAKF 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 370 DLFISCW-----VSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSAPGEQP 416
Cdd:cd19538 381 DLTFELReqyndGTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
584-924 |
1.09e-17 |
|
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: 86.17 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQD---NVL---HnhsfsfdpsVWALFWPLLT---GGTIVL 654
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADvylNMLplfH---------IAGLNLALATfhaGGANVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 655 advrtME--DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSggeVLNPELAHKIQKVWQADVANLY 730
Cdd:cd17637 72 -----MEkfDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSgvDLSSLRHVLG---LDAPETIQRFEETTGATFWSLY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 731 GPTEaTIDALYFSIDKNAAGAIpiGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQrflpnPFGN 810
Cdd:cd17637 144 GQTE-TSGLVTLSPYRERPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAY-----TFRN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 811 GRvYATGDLGRRWSSGAISYLGRRDQQ--VKIRGHRIELNEVahllcqalelKEAIVfaQHAGTEQARLVAAIEQQPGlh 888
Cdd:cd17637 216 GW-HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEV----------EKVIL--EHPAIAEVCVIGVPDPKWG-- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 889 sEGIK-------------QELLRHLPA----YLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17637 281 -EGIKavcvlkpgatltaDELIEFVGSriarYKKPRYVVFVEALPKTADGSID 332
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
26-410 |
1.22e-17 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 87.46 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 26 YPLSSEQKRLWLLAQLAGTAT-LPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRL-LMPTGLVKLEY 103
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVvLDKTVRFRIEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 104 FD---RPPSDADMAELIGAA----FELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQ------TEPD 170
Cdd:cd19066 82 IDlrnLADPEARLLELIDQIqqtiYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSvydaaeRQKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 171 HQYPAVGAIAEVFQREQTLAQDAQITEQ---WQQWGIGLQAPAATeiPTEnPRPAIKGSDRQVHeaLTAWGDQPVAEAE- 246
Cdd:cd19066 162 TLPPPVGSYADYAAWLEKQLESEAAQADlayWTSYLHGLPPPLPL--PKA-KRPSQVASYEVLT--LEFFLRSEETKRLr 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 247 -------------IVSSWLTVLMRWQGSQ--SALCAIKVR-DKAHANLIGPLQTYLPVRVDMPDGSTLAQLRLQVEEQLN 310
Cdd:cd19066 237 evaresgttptqlLLAAFALALKRLTASIdvVIGLTFLNRpDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 311 G---NDHPSFSTLLEVCPPKRDLSRTPYFQTGLQFI---AHDVEQRDFHAGNLTRLPTKQPSSDLDLFISCwVSDGTLGL 384
Cdd:cd19066 317 EaieHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKnnqQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASE-DPDGDLLL 395
|
410 420
....*....|....*....|....*.
gi 37542635 385 TLDYDCAVLNSSQVEVLAQALISVLS 410
Cdd:cd19066 396 RLEYSRGVYDERTIDRFAERYMTALR 421
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
469-923 |
1.23e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 88.63 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANIsQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPI-DPRLP--TDRIQFLIENSGCEL 545
Cdd:PRK07769 54 RDLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 546 VITSD------QQSVEGWPQVARIRMEALD--PD---IRWVAPTgLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILW 614
Cdd:PRK07769 133 ILTTTdsaegvRKFFRARPAKERPRVIAVDavPDevgATWVPPE-ANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 615 -----------RQRTW-P-------LTAQDNVLHNHSFSF-DPSVWA---LFW-------PLLTGGTIVLADVRTMEDST 664
Cdd:PRK07769 212 vidalegqegdRGVSWlPffhdmglITVLLPALLGHYITFmSPAAFVrrpGRWirelarkPGGTGGTFSAAPNFAFEHAA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 665 ALldlmirhdvsvlgGVPSllgtliDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVW------QADVANLYGPTEATI- 737
Cdd:PRK07769 292 AR-------------GLPK------DGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFapyglpPTAIKPSYGMAEATLf 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 738 -----------------DAL----YFSIDKNAAGAIP---IGYPIDNTDAYIVDLN-LNPVPPGVPGEIMLAGQNLARGY 792
Cdd:PRK07769 353 vsttpmdeeptviyvdrDELnagrFVEVPADAPNAVAqvsAGKVGVSEWAVIVDPEtASELPDGQIGEIWLHGNNIGTGY 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 793 LGKPAQTAQRF-------LPNPFGNG-----RVYATGDLGrRWSSGAISYLGRRDQQVKI--RGH---RIELNE------ 849
Cdd:PRK07769 433 WGKPEETAATFqnilksrLSESHAEGapddaLWVRTGDYG-VYFDGELYITGRVKDLVIIdgRNHypqDLEYTAqeatka 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 850 -----VAHLLCQALELKEAIVFAQHAG--------TEQARLVAaiEQQPGLH-------SEGIKQEL-LRHlpaYLIPSQ 908
Cdd:PRK07769 512 lrtgyVAAFSVPANQLPQVVFDDSHAGlkfdpedtSEQLVIVA--ERAPGAHkldpqpiADDIRAAIaVRH---GVTVRD 586
|
570
....*....|....*..
gi 37542635 909 LLLLD--ELPRTATGKV 923
Cdd:PRK07769 587 VLLVPagSIPRTSSGKI 603
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
582-933 |
2.46e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 85.61 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 582 HSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHS-FSFDPSVWALFWPLLTGGTIVLADVRTM 660
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 661 EDSTALLD---LMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT- 736
Cdd:cd05944 81 RNPGLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 IDALYFSIDKNAAGAipIGYPIDNTDAYIVDLN-----LNPVPPGVPGEIMLAGQNLARGYLgkpaqtAQRFLPNPFGNG 811
Cdd:cd05944 161 LVAVNPPDGPKRPGS--VGLRLPYARVRIKVLDgvgrlLRDCAPDEVGEICVAGPGVFGGYL------YTEGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 812 RVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAhllcQALELKEAIVFAQHAGTEQARL----VAAIEQQPGL 887
Cdd:cd05944 233 GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIE----EALLRHPAVAFAGAVGQPDAHAgelpVAYVQLKPGA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 37542635 888 HSEgiKQELLRHLPAYL-----IPSQLLLLDELPRTATGKVDMLKLDQLAA 933
Cdd:cd05944 309 VVE--EEELLAWARDHVperaaVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
468-928 |
2.87e-17 |
|
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: 86.71 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVI 547
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 548 TSDQQsvegwpqvarirmeALDPDIRWVAPT--GLSHSDAAYLIYTSGSTGVPKGVVVEHrqvvnnilwrQRTWPLTAqd 625
Cdd:cd05939 81 FNLLD--------------PLLTQSSTEPPSqdDVNFRDKLFYIYTSGTTGLPKAAVIVH----------SRYYRIAA-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 626 nvLHNHSFSFDPS-VWALFWPLL-TGGTIVLADVRTMEDSTALL----------DLMIRHDVSVLGGVPSLLGTLIDHPF 693
Cdd:cd05939 135 --GAYYAFGMRPEdVVYDCLPLYhSAGGIMGVGQALLHGSTVVIrkkfsasnfwDDCVKYNCTIVQYIGEICRYLLAQPP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 694 ANDCRAVKLVLSGGEVLNPElahkiqkVWQ--------ADVANLYGPTEATIDALYFSIDKNAAGAIPIG----YPI--- 758
Cdd:cd05939 213 SEEEQKHNVRLAVGNGLRPQ-------IWEqfvrrfgiPQIGEFYGATEGNSSLVNIDNHVGACGFNSRIlpsvYPIrli 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 759 ---DNTDAYIVDLNLNPVP--PGVPGEimLAGQNLAR-------GYLGKPAqTAQRFLPNPFGNG-RVYATGDLGRRWSS 825
Cdd:cd05939 286 kvdEDTGELIRDSDGLCIPcqPGEPGL--LVGKIIQNdplrrfdGYVNEGA-TNKKIARDVFKKGdSAFLSGDVLVMDEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 826 GAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA-QHAGTE-QARLVAAIEQQPGLHSEGIKQELLRHLPAY 903
Cdd:cd05939 363 GYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGvEVPGVEgRAGMAAIVDPERKVDLDRFSAVLAKSLPPY 442
|
490 500
....*....|....*....|....*...
gi 37542635 904 LIPSQLLLLDELPRTAT---GKVDMLKL 928
Cdd:cd05939 443 ARPQFIRLLPEVDKTGTfklQKTDLQKE 470
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
420-923 |
4.88e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.19 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 420 VALMGQQMQQTVLAQAHGPRTTPPQLTLTEWVAASTEKSPLAVAVIDH--GQQLSYAELWARAALVAANISQHVAKPRSI 497
Cdd:PLN02330 3 MEIQKQEDNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD-----------------QQSVEG---W 557
Cdd:PLN02330 83 VVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkglglpvivlgEEKIEGavnW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 558 PQVarirMEALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI---LWRQRTwPLTAQDNVLHNHSFS 634
Cdd:PLN02330 163 KEL----LEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcssLFSVGP-EMIGQVVTLGLIPFF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 635 FDPSVWAL-FWPLLTGGTIVLA---DVRTmedstaLLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKL----VLSG 706
Cdd:PLN02330 238 HIYGITGIcCATLRNKGKVVVMsrfELRT------FLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklqaIMTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 707 GEVLNPELAHKIQKVW-QADVANLYGPTEATIDALYFSIDKNAAGAI---PIGYPIDNTDAYIVDL-NLNPVPPGVPGEI 781
Cdd:PLN02330 312 AAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHGDPEKGHGIAkknSVGFILPNLEVKFIDPdTGRSLPKNTPGEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 782 MLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELK 861
Cdd:PLN02330 392 CVRSQCVMQGYYNNKEETDRTIDEDGW-----LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37542635 862 EAIVFA---QHAGTEQARLVaAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PLN02330 467 DAAVVPlpdEEAGEIPAACV-VINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKI 530
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
469-924 |
6.02e-17 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 85.89 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALvAANI--SQHVAKPRSIiAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELV 546
Cdd:PRK08008 36 RRYSYLELNEEINR-TANLfySLGIRKGDKV-ALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 547 ITSDqqsvEGWPQVARIRMEALDPD-----IRWVAPT----------------------GLSHSDAAYLIYTSGSTGVPK 599
Cdd:PRK08008 114 VTSA----QFYPMYRQIQQEDATPLrhiclTRVALPAddgvssftqlkaqqpatlcyapPLSTDDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 600 GVVVEHRqvvnNIL-------WRQRtwpLTAQDNVLHNH-SFSFDPSVWALFWPLLTGGTIVLADVRTmedSTALLDLMI 671
Cdd:PRK08008 190 GVVITHY----NLRfagyysaWQCA---LRDDDVYLTVMpAFHIDCQCTAAMAAFSAGATFVLLEKYS---ARAFWGQVC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 672 RHDVSVLGGVPSLLGTLIDHPFANDCRAVKLV-------LSGGEVLNPELAHKIQkvwqadVANLYGPTEATIDALyfsi 744
Cdd:PRK08008 260 KYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfylnLSDQEKDAFEERFGVR------LLTSYGMTETIVGII---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 745 dknaaGAIP--------IGYPIDNTDAYIVDLNLNPVPPGVPGEIML---AGQNLARGYLGKPAQTAQRFLPnpfgNGRV 813
Cdd:PRK08008 330 -----GDRPgdkrrwpsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEA----DGWL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 814 YaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEG 891
Cdd:PRK08008 401 H-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGetLSEEE 479
|
490 500 510
....*....|....*....|....*....|...
gi 37542635 892 IKQELLRHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK08008 480 FFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
26-416 |
6.79e-17 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 84.73 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 26 YPLSSEQKRLWLLAQL-AGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEYF 104
Cdd:cd19533 2 LPLTSAQRGVWFAEQLdPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 105 D-RPPSDAD------MAELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSL----QRIAQ--TLFQTEPDH 171
Cdd:cd19533 82 DlSGDPDPEgaaqqwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFalfgQRVAEiyTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 172 QYPAVGAIAEVFQREQTLAQDAQITEQWQQWG---IGLQAPAATEIPTENPRPAI--------KGSDRQVHEALTAWGdq 240
Cdd:cd19533 162 PPAPFGSFLDLVEEEQAYRQSERFERDRAFWTeqfEDLPEPVSLARRAPGRSLAFlrrtaelpPELTRTLLEAAEAHG-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 241 pvaeaeivSSWLTVLM--------RWQGSQSALCAIKVR---DKAHANLIGPLQTYLPVRVDMPDGSTLAQLRLQVEEQL 309
Cdd:cd19533 240 --------ASWPSFFIalvaaylhRLTGANDVVLGVPVMgrlGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 310 NGN-DHPSFSTLLEVcppkRDLSRT----PYFQTGLQFIAHDVEQRDFHAGNLTRLPTKQPSSDLDLFISCWVSDGTLGL 384
Cdd:cd19533 312 RSLlRHQRYRYEDLR----RDLGLTgelhPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYDRDDESGLRI 387
|
410 420 430
....*....|....*....|....*....|..
gi 37542635 385 TLDYDCAVLNSSQVEVLAQALISVLSAPGEQP 416
Cdd:cd19533 388 DFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
462-923 |
7.33e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 85.77 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 462 VAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENS 541
Cdd:PRK08162 35 PAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 542 GCELVITS------------------------DQQSVEGWPQVARIRMEAL----DPDIRWVAPTglSHSDAAYLIYTSG 593
Cdd:PRK08162 115 EAKVLIVDtefaevarealallpgpkplvidvDDPEYPGGRFIGALDYEAFlasgDPDFAWTLPA--DEWDAIALNYTSG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 594 STGVPKGVVVEHR----QVVNNILwrqrTWPLTaqdnvlhNHSF------SFDPSVWALFWPL-LTGGTIV-LADVrtme 661
Cdd:PRK08162 193 TTGNPKGVVYHHRgaylNALSNIL----AWGMP-------KHPVylwtlpMFHCNGWCFPWTVaARAGTNVcLRKV---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 662 DSTALLDLMIRHDVSVLGGVPSLLGTLI---DHPFANDCRAVKLVLSGGevlnPELAHKIQKVWQA--DVANLYGPTE-- 734
Cdd:PRK08162 258 DPKLIFDLIREHGVTHYCGAPIVLSALInapAEWRAGIDHPVHAMVAGA----APPAAVIAKMEEIgfDLTHVYGLTEty 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 735 --ATI-------DALYFS--IDKNAAGAIPigYPIDNtDAYIVDLN-LNPVPPG--VPGEIMLAGQNLARGYLGKPAQTA 800
Cdd:PRK08162 334 gpATVcawqpewDALPLDerAQLKARQGVR--YPLQE-GVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 801 QRFlpnpfgNGRVYATGDLGRRWSSGAIsylgrrdqQVKIR--------GHRIELNEVAHLLCQALELKEAIVFAQHAGT 872
Cdd:PRK08162 411 EAF------AGGWFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDPK 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 37542635 873 EQARLVAAIEQQPGLHSEGikQELLRH----LPAYLIPSQlLLLDELPRTATGKV 923
Cdd:PRK08162 477 WGEVPCAFVELKDGASATE--EEIIAHcrehLAGFKVPKA-VVFGELPKTSTGKI 528
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
467-843 |
9.35e-17 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 85.56 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 467 HGQQLSYAELWARAALVAANIsQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPI-DPRLP--TDRIQFLIENSGC 543
Cdd:PRK12476 65 CAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 544 ELVITSD--QQSVEGW----PQVARIRMEALD--PDIRWV--APTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNIL 613
Cdd:PRK12476 144 TVVLTTTaaAEAVEGFlrnlPRLRRPRVIAIDaiPDSAGEsfVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 614 wrQRTWPLTAQDNVLHNHSF---SFDPSVWALFWPLLTGGTIvladvrTMEDSTALLDLMIR---------HDVSVLGGV 681
Cdd:PRK12476 224 --QMILSIDLLDRNTHGVSWlplYHDMGLSMIGFPAVYGGHS------TLMSPTAFVRRPQRwikalsegsRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 682 PSLLGTLIDH---PFAN---DCRAVKLVLsGGEVLNPELAHKIQKVW------QADVANLYGPTEATI-----------D 738
Cdd:PRK12476 296 PNFAYEWAAQrglPAEGddiDLSNVVLII-GSEPVSIDAVTTFNKAFapyglpRTAFKPSYGIAEATLfvatiapdaepS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 ALYFSIDKNAAG-AIPI-------------GYPIDNTDAYIVDLNL-NPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRF 803
Cdd:PRK12476 375 VVYLDREQLGAGrAVRVaadapnavahvscGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTF 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 804 -------LP------NPFGNGRVYATGDLGrRWSSGAISYLGRRDQQVKIRGH 843
Cdd:PRK12476 455 gaklqsrLAegshadGAADDGTWLRTGDLG-VYLDGELYITGRIADLIVIDGR 506
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
27-402 |
1.38e-16 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 83.97 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQLA-GTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVL-ERPVRLLMPTGLVKLEYF 104
Cdd:cd19539 3 PLSFAQERLWFIDQGEdGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 105 DRPPSDADMA--------ELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLfqtepDHQYPAV 176
Cdd:cd19539 83 DLSDPDSDRErrleellrERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDL-----AALYAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 177 GAIAEvfQREQTLAQDAQITEQWQQ--------------WGIGLQAPAATEIPTENPRPA---IKGSDRQ------VHEA 233
Cdd:cd19539 158 RKGPA--APLPELRQQYKEYAAWQRealaapraaelldfWRRRLRGAEPTALPTDRPRPAgfpYPGADLRfeldaeLVAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 234 LTAwgdqpVAEAEIVS-------SWLTVLMRWQGSQSALCAIKVRDKAHANL---IGPLQTYLPVRVDMPDGSTLAQL-- 301
Cdd:cd19539 236 LRE-----LAKRARSSlfmvllaAYCVLLRRYTGQTDIVVGTPVAGRNHPRFestVGFFVNLLPLRVDVSDCATFRDLia 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 302 ---RLQVEEQLNGnDHPsFSTLLEVCPPKRDLSRTPYFQTGLQFI-AHDVEQRDfhAGNLTRLPTKQPSSD--LDLFISC 375
Cdd:cd19539 311 rvrKALVDAQRHQ-ELP-FQQLVAELPVDRDAGRHPLVQIVFQVTnAPAGELEL--AGGLSYTEGSDIPDGakFDLNLTV 386
|
410 420
....*....|....*....|....*..
gi 37542635 376 WVSDGTLGLTLDYDCAVLNSSQVEVLA 402
Cdd:cd19539 387 TEEGTGLRGSLGYATSLFDEETIQGFL 413
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
459-923 |
2.67e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 83.94 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARA-ALVAANISQHVAKPRSIIaVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFL 537
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVdALAAALAARGVRKGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 538 IENSGCELVITSDqqsveGWPQVARIrMEALDPDIRWV-----APTGLS-------------------HSDAAYLIYTSG 593
Cdd:PRK07470 100 AEASGARAMICHA-----DFPEHAAA-VRAASPDLTHVvaiggARAGLDyealvarhlgarvanaavdHDDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 594 STGVPKGVVVEHRQ---VVNNILwrQRTWP-LTAQDNVLHNHSFSFDPSVWALFwPLLTGGTIVLADVRTMEDSTAlLDL 669
Cdd:PRK07470 174 TTGRPKAAVLTHGQmafVITNHL--ADLMPgTTEQDASLVVAPLSHGAGIHQLC-QVARGAATVLLPSERFDPAEV-WAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 670 MIRHDVSVLGGVPSLLGTLIDHPFAN--DCRAVKLVLSGGEVL---NPELA-HKIQKVwqadVANLYGPTEATID----- 738
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVEHPAVDryDHSSLRYVIYAGAPMyraDQKRAlAKLGKV----LVQYFGLGEVTGNitvlp 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 -ALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvyATG 817
Cdd:PRK07470 326 pALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------RTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 818 DLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPG--LHSEGIKQE 895
Cdd:PRK07470 400 DLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGapVDEAELLAW 479
|
490 500
....*....|....*....|....*...
gi 37542635 896 LLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK07470 480 LDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
442-923 |
4.24e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 83.52 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 442 PPqlTLTEWVAASTEKSPLAVAV--IDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG 519
Cdd:PRK05857 13 PS--TVLDRVFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 520 HAFLPIDPRLP----------TDRIQFLIeNSGCELVITSDQQSVEGWPQV-----ARIRMEALDPDIRWVAPT-GLSHS 583
Cdd:PRK05857 91 AIAVMADGNLPiaaierfcqiTDPAAALV-APGSKMASSAVPEALHSIPVIavdiaAVTRESEHSLDAASLAGNaDQGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQ--VVNNILwrqRTWPLTAQDNVLHNHSFSFDPS-----VWALFWPLLTGGTIVLAD 656
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVLLANRTffAVPDIL---QKEGLNWVTWVVGETTYSPLPAthiggLWWILTCLMHGGLCVTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 657 vrtmEDSTALLDLMIRHDVSVLGGVPSLLGTLIDH--PFANDCRAVKLVLSGGevlNPELAHKIQKVWQADV--ANLYGP 732
Cdd:PRK05857 247 ----ENTTSLLEILTTNAVATTCLVPTLLSKLVSElkSANATVPSLRLVGYGG---SRAIAADVRFIEATGVrtAQVYGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 733 TEATIDALYF-----SIDKNAAGAipIGYPIDNTDAYIVDLN-LNP-VPPGVP----GEIMLAGQNLARGYLGKPAQTaQ 801
Cdd:PRK05857 320 SETGCTALCLptddgSIVKIEAGA--VGRPYPGVDVYLAATDgIGPtAPGAGPsasfGTLWIKSPANMLGYWNNPERT-A 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 802 RFLPNPFGNgrvyaTGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTEQARLV 878
Cdd:PRK05857 397 EVLIDGWVN-----TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEipdEEFGALVGLAV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 37542635 879 AAIEQQPGLHSEGIKQELL----RHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK05857 472 VASAELDESAARALKHTIAarfrRESEPMARPSTIVIVTDIPRTQSGKV 520
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
468-922 |
1.59e-15 |
|
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: 80.94 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAAN-ISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELV 546
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWlHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 547 ItsdqqsvegwpqvarirmeaLDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVvehrqvvnnILWRqRTWP---LTA 623
Cdd:cd05937 83 I--------------------VDPD------------DPAILIYTSGTTGLPKAAA---------ISWR-RTLVtsnLLS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 624 QDNVLHNHSFSFDP--------SVWALFWPLLTGGTIVLA----------DVRtmeDSTAlldlmirhdvSVLGGVPSLL 685
Cdd:cd05937 121 HDLNLKNGDRTYTCmplyhgtaAFLGACNCLMSGGTLALSrkfsasqfwkDVR---DSGA----------TIIQYVGELC 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 686 GTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQ-ADVANLYGPTEATIDALYFSIDKNAAGAI----PIGYPIDN 760
Cdd:cd05937 188 RYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNvPEIGEFYAATEGVFALTNHNVGDFGAGAIghhgLIRRWKFE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVDLNLNP--------------VPPGVPGEIMLA----GQNLARGYLGKPAQTAQRFLPNPFGNGRVY-ATGDLGR 821
Cdd:cd05937 268 NQVVLVKMDPETddpirdpktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYfRTGDLLR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 822 RWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA----QHAGteQARLVA-AIEQQPGLHSEGIKQEL 896
Cdd:cd05937 348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpGHDG--RAGCAAiTLEESSAVPTEFTKSLL 425
|
490 500 510
....*....|....*....|....*....|
gi 37542635 897 LRH----LPAYLIPSQLLLLDELPRTATGK 922
Cdd:cd05937 426 ASLarknLPSYAVPLFLRLTEEVATTDNHK 455
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
27-411 |
6.98e-15 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 78.62 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQLAGTAT---LPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEy 103
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAaynIPLALR--LTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 104 FDRPPSDAD-----MAELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQ--------TEPD 170
Cdd:cd19540 80 LTVVDVTEDelaarLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATayaarragRAPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 171 HQYPAVG-AIAEVFQREqTLA----QDAQITEQWQQW-----GiglqAPAATEIPTENPRPAIKGS---------DRQVH 231
Cdd:cd19540 160 WAPLPVQyADYALWQRE-LLGdeddPDSLAARQLAYWretlaG----LPEELELPTDRPRPAVASYrggtveftiDAELH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 232 EALTAwgdqpVAEAEIVsswlTVLMRWQGSQSALCA-------IKV------R-DKAHANLIGPLQTYLPVRVDMPDGST 297
Cdd:cd19540 235 ARLAA-----LAREHGA----TLFMVLHAALAVLLSrlgagddIPIgtpvagRgDEALDDLVGMFVNTLVLRTDVSGDPT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 298 LAQLRLQVEEQ-LNGNDHP--SFSTLLEVCPPKRDLSRTPYFQTGLQFiaHDVEQRDFHAGNLT--RLPTKQPSSDLDLF 372
Cdd:cd19540 306 FAELLARVRETdLAAFAHQdvPFERLVEALNPPRSTARHPLFQVMLAF--QNTAAATLELPGLTvePVPVDTGVAKFDLS 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 37542635 373 ISC------WVSDGTLGLTLDYDCAVLNSSQVEVLAQALISVLSA 411
Cdd:cd19540 384 FTLterrdaDGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEA 428
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
458-922 |
3.09e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 77.42 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 458 SPLAVAVI--DHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:PRK13391 10 TPDKPAVImaSTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITSDQQS------------VEGWPQV----ARIRMEALDPDIRWVAPTGL-SHSDAAYLIYTSGSTGVP 598
Cdd:PRK13391 90 YIVDDSGARALITSAAKLdvarallkqcpgVRHRLVLdgdgELEGFVGYAEAVAGLPATPIaDESLGTDMLYSSGTTGRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 599 KGVVVE--HRQVVNNIlwrqrtwPLTAqdnVLHNhSFSFDP-SVW----------ALFWPLLT---GGTIVLadvrtME- 661
Cdd:PRK13391 170 KGIKRPlpEQPPDTPL-------PLTA---FLQR-LWGFRSdMVYlspaplyhsaPQRAVMLVirlGGTVIV-----MEh 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 662 -DSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN----DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT 736
Cdd:PRK13391 234 fDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVrdkyDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 ----IDALYFSIDKNAAGAIPIGypidntDAYIVDLNLNPVPPGVPGEIMLAGQNLARgYLGKPAQTAQRFLPNPfgngr 812
Cdd:PRK13391 314 gftaCDSEEWLAHPGTVGRAMFG------DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDG----- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 813 VYAT-GDLGRRWSSGAIsYLGRRDQQVKIRGH-RIELNEVAHLLCQALELKEAIVFA---QHAGTEqarlVAAIEQ--QP 885
Cdd:PRK13391 382 TWSTvGDIGYVDEDGYL-YLTDRAAFMIISGGvNIYPQEAENLLITHPKVADAAVFGvpnEDLGEE----VKAVVQpvDG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 37542635 886 GLHSEGIKQELL----RHLPAYLIPSQLLLLDELPRTATGK 922
Cdd:PRK13391 457 VDPGPALAAELIafcrQRLSRQKCPRSIDFEDELPRLPTGK 497
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
459-923 |
3.63e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.19 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 459 PLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLI 538
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 539 ENSGCELVI-----------------------------------TSDQQSVEGWPQVARIRMEAL----DPDIRWVAPTG 579
Cdd:PLN02479 114 EHSKSEVVMvdqefftlaeealkilaekkkssfkppllivigdpTCDPKSLQYALGKGAIEYEKFletgDPEFAWKPPAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 580 LSHSDAayLIYTSGSTGVPKGVVVEHR-----QVVNNILWRQR-------TWPLtaqdnvlhnhsfsFDPSVWALFWPL- 646
Cdd:PLN02479 194 EWQSIA--LGYTSGTTASPKGVVLHHRgaylmALSNALIWGMNegavylwTLPM-------------FHCNGWCFTWTLa 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 647 -LTGGTIVLADVRTmedsTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDC----RAVKLVLSGGEVLNPELAHKIQKV 721
Cdd:PLN02479 259 aLCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlplpRVVHVMTAGAAPPPSVLFAMSEKG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 722 WQadVANLYGPTE----ATIDALYFSIDK---------NA-AGAIPIGypIDNTDayIVDL-NLNPVPP--GVPGEIMLA 784
Cdd:PLN02479 335 FR--VTHTYGLSEtygpSTVCAWKPEWDSlppeeqarlNArQGVRYIG--LEGLD--VVDTkTMKPVPAdgKTMGEIVMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 785 GQNLARGYLGKPAQTAQrflpnPFGNGRvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAI 864
Cdd:PLN02479 409 GNMVMKGYLKNPKANEE-----AFANGW-FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAS 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 865 VFAQHAGTEQARLVAAIEQQPGLHSEG---IKQELLR----HLPAYLIPSQlLLLDELPRTATGKV 923
Cdd:PLN02479 483 VVARPDERWGESPCAFVTLKPGVDKSDeaaLAEDIMKfcreRLPAYWVPKS-VVFGPLPKTATGKI 547
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
471-839 |
4.19e-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: 76.87 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD 550
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 qqsvegwpqvarirmealdpdirwvaptglSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWP--LTAQDNVL 628
Cdd:cd17639 86 ------------------------------KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 629 H----NHSFSFDPSVWALFWplltGGTIVLADVRTMEDST--------------------ALLDlMIRHDV-SVLGGVPS 683
Cdd:cd17639 136 AylplAHIFELAAENVCLYR----GGTIGYGSPRTLTDKSkrgckgdltefkptlmvgvpAIWD-TIRKGVlAKLNPMGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 684 LLGTLIDH---------------PFAND-----CRA-----VKLVLSGGEVLNPElAHKIQKVWQADVANLYGPTE---- 734
Cdd:cd17639 211 LKRTLFWTayqsklkalkegpgtPLLDElvfkkVRAalggrLRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTEtcag 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 735 ATIdALYFSIDKNAAGAipigyPIDNTDAYIVD---LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPnpfgnG 811
Cdd:cd17639 290 GTV-QDPGDLETGRVGP-----PLPCCEIKLVDweeGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDG-----D 358
|
410 420
....*....|....*....|....*...
gi 37542635 812 RVYATGDLGRRWSSGAISYLGRRDQQVK 839
Cdd:cd17639 359 GWFHTGDIGEFHPDGTLKIIDRKKDLVK 386
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
456-837 |
4.41e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 76.45 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQ 535
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 536 FLIENSGCELVITSDQQSVEGWPQVARIRMEALDPDIRWvaptglSHSDAAYLIYTSGSTGVPKGVVVEHRQ-------V 608
Cdd:PRK09029 94 ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAW------QPQRLATMTLTSGSTGLPKAAVHTAQAhlasaegV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 609 VNNIlwrqrtwPLTAQDNVLhnhsFS---FDPS----VWAlfWpLLTGGTIVladVRTMEDstalLDLMIRhDVSVLGGV 681
Cdd:PRK09029 168 LSLM-------PFTAQDSWL----LSlplFHVSgqgiVWR--W-LYAGATLV---VRDKQP----LEQALA-GCTHASLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 682 PSLLGTLIDHPFANdcRAVKLVLSGGEVLNPELAHKIQKV----WQAdvanlYGPTEA--TIDAlyfsidKNAAGAIPIG 755
Cdd:PRK09029 226 PTQLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQAEQQgircWCG-----YGLTEMasTVCA------KRADGLAGVG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 756 YPIDNTDAYIVDlnlnpvppgvpGEIMLAGQNLARGYlgkpaqtaqrflpnpFGNGRV---------YATGDLGrRWSSG 826
Cdd:PRK09029 293 SPLPGREVKLVD-----------GEIWLRGASLALGY---------------WRQGQLvplvndegwFATRDRG-EWQNG 345
|
410
....*....|.
gi 37542635 827 AISYLGRRDQQ 837
Cdd:PRK09029 346 ELTILGRLDNL 356
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
461-922 |
2.18e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.55 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIEN 540
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 541 SGCELVITSD------QQSVEGWPQVARIRM---EALDPDIRWVA------PTGLS-HSDAAYLIYTSGSTGVPKGVVVE 604
Cdd:PRK08276 82 SGAKVLIVSAaladtaAELAAELPAGVPLLLvvaGPVPGFRSYEEalaaqpDTPIAdETAGADMLYSSGTTGRPKGIKRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 605 HR-----QVVNNILWRQRTWPLTAQDNV------LHnHSfsfDPSVWALfWPLLTGGTIVLadvrtME--DSTALLDLMI 671
Cdd:PRK08276 162 LPgldpdEAPGMMLALLGFGMYGGPDSVylspapLY-HT---APLRFGM-SALALGGTVVV-----MEkfDAEEALALIE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 672 RHDVSVLGGVPSLLGTLIDHPFA----NDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALyfsIDKN 747
Cdd:PRK08276 232 RYRVTHSQLVPTMFVRMLKLPEEvrarYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTV---ITSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 748 AAGAIP--IGYPIDNTdAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSS 825
Cdd:PRK08276 309 DWLAHPgsVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW-----VTVGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 826 GAIsYLGRRDQQVKIRGH-RIELNEVAHLLCQALELKEAIVF-AQHAGTEQaRLVAAIEQQPG-LHSEGIKQELLRH--- 899
Cdd:PRK08276 383 GYL-YLTDRKSDMIISGGvNIYPQEIENLLVTHPKVADVAVFgVPDEEMGE-RVKAVVQPADGaDAGDALAAELIAWlrg 460
|
490 500
....*....|....*....|....
gi 37542635 900 -LPAYLIPSQLLLLDELPRTATGK 922
Cdd:PRK08276 461 rLAHYKCPRSIDFEDELPRTPTGK 484
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
471-863 |
3.29e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.08 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHvakPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSd 550
Cdd:PRK06334 46 LSYNQVRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTS- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QQSVEGWPQV---------ARIRMEALDPD--------------------IRWVAPTGLSHSDAAYLIYTSGSTGVPKGV 601
Cdd:PRK06334 122 KQLMQHLAQThgedaeypfSLIYMEEVRKElsfwekcrigiymsipfewlMRWFGVSDKDPEDVAVILFTSGTEKLPKGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 602 VVEHRQVVNNILWRQRTWPLTAQDNVLH----NHSFSFDPSvwALFwPLLTGGTIVLAdvRTMEDSTALLDLMIRHDVSV 677
Cdd:PRK06334 202 PLTHANLLANQRACLKFFSPKEDDVMMSflppFHAYGFNSC--TLF-PLLSGVPVVFA--YNPLYPKKIVEMIDEAKVTF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 678 LGGVPSLLGTLIDHPFANDC--RAVKLVLSGGEVLNPELAHKIQKVW-QADVANLYGPTEATiDALYFSIDKNAAGAIPI 754
Cdd:PRK06334 277 LGSTPVFFDYILKTAKKQESclPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECS-PVITINTVNSPKHESCV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 755 GYPIDNTDAYIVDLNLN-PVPPGVPGEIMLAGQNLARGYLGkpAQTAQRFLpnPFGNGRVYATGDLGRRWSSGAISYLGR 833
Cdd:PRK06334 356 GMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLG--EDFGQGFV--ELGGETWYVTGDLGYVDRHGELFLKGR 431
|
410 420 430
....*....|....*....|....*....|
gi 37542635 834 RDQQVKIRGHRIELNEVAHLLCQALELKEA 863
Cdd:PRK06334 432 LSRFVKIGAEMVSLEALESILMEGFGQNAA 461
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
586-930 |
7.88e-13 |
|
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: 72.91 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 586 AYLIYTSGSTGVPKGVVVEHRQVVNNIL-------WRQR----TW-PLT----------------AQDNVLHNHSFSFDP 637
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFailnsteWKTKdrilSWmPLThdmgliafhlapliagMNQYLMPTRLFIRRP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 638 SVWalfwplltggtivladvrtmedstalLDLMIRHDVSVLG----GVPSLLGTLIDHPFAN-DCRAVKLVLSGGEVLNP 712
Cdd:cd05908 189 ILW--------------------------LKKASEHKATIVSspnfGYKYFLKTLKPEKANDwDLSSIRMILNGAEPIDY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 713 ELAHKI------QKVWQADVANLYGPTEATIDA------LYFSI--------------------DKNAAGAIPIGYPIDN 760
Cdd:cd05908 243 ELCHEFldhmskYGLKRNAILPVYGLAEASVGAslpkaqSPFKTitlgrrhvthgepepevdkkDSECLTFVEVGKPIDE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 761 TDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGrRWSSGAISYLGRRDQQVKI 840
Cdd:cd05908 323 TDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW-----LKTGDLG-FIRNGRLVITGREKDIIFV 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 841 RGHRIELNEVAHLLCQ--ALEL-KEAIVFAQHAGTEQARLVAAIEQQPGL-HSEGIKQELLRHLPAY--LIPSQLLLLDE 914
Cdd:cd05908 397 NGQNVYPHDIERIAEEleGVELgRVVACGVNNSNTRNEEIFCFIEHRKSEdDFYPLGKKIKKHLNKRggWQINEVLPIRR 476
|
410
....*....|....*.
gi 37542635 915 LPRTATGKVDMLKLDQ 930
Cdd:cd05908 477 IPKTTSGKVKRYELAQ 492
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
456-923 |
1.10e-12 |
|
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: 72.59 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 456 EKSPLAVAVI------DHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAG--HA--FLPI 525
Cdd:cd05966 64 KERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavHSvvFAGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 526 DPRLPTDRIqfliENSGCELVITSDQQS---------------VEGWPQV----------ARIRMEAlDPDIRW------ 574
Cdd:cd05966 144 SAESLADRI----NDAQCKLVITADGGYrggkviplkeivdeaLEKCPSVekvlvvkrtgGEVPMTE-GRDLWWhdlmak 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 575 ----VAPTGLSHSDAAYLIYTSGSTGVPKGVVveHRQVvNNILWRQRTwpltaqdnvlhnHSFSFDPSVWALFW------ 644
Cdd:cd05966 219 qspeCEPEWMDSEDPLFILYTSGSTGKPKGVV--HTTG-GYLLYAATT------------FKYVFDYHPDDIYWctadig 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 645 -----------PLLTGGTIVLAD-VRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLI----DHPFANDCRAVKLVLSGGE 708
Cdd:cd05966 284 witghsyivygPLANGATTVMFEgTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMkfgdEWVKKHDLSSLRVLGSVGE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 709 VLNPELAHKIQKV------------WQadvanlygpTE---ATIDALyfsidknaAGAIPI-----GYPIDNTDAYIVDL 768
Cdd:cd05966 364 PINPEAWMWYYEVigkercpivdtwWQ---------TEtggIMITPL--------PGATPLkpgsaTRPFFGIEPAILDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 769 NLNPVPPGVPGeiMLAGQN----LARGYLGKPaqtaQRFLP---NPFGNgrVYATGDLGRRWSSGAISYLGRRDQQVKIR 841
Cdd:cd05966 427 EGNEVEGEVEG--YLVIKRpwpgMARTIYGDH----ERYEDtyfSKFPG--YYFTGDGARRDEDGYYWITGRVDDVINVS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 842 GHRIELNEVAHLLCQALELKE-AIVFAQHAGTEQArLVAAIEQQPGLH-SEGIKQELLRH----LPAYLIPSQLLLLDEL 915
Cdd:cd05966 499 GHRLGTAEVESALVAHPAVAEaAVVGRPHDIKGEA-IYAFVTLKDGEEpSDELRKELRKHvrkeIGPIATPDKIQFVPGL 577
|
....*...
gi 37542635 916 PRTATGKV 923
Cdd:cd05966 578 PKTRSGKI 585
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
27-416 |
2.46e-12 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 70.97 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQLA-GTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVlERPVR---LLMPTGLVKLE 102
Cdd:cd19546 6 PATAGQLRTWLLARLDeETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGD-GGDVHqriLDADAARPELP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 103 YFdrPPSDADMAELIGAA----FELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTL---FQTEPDHQYPA 175
Cdd:cd19546 85 VV--PATEEELPALLADRaahlFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLaaaYGARREGRAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 176 VGAIAEVFQR----EQTLAQDAQ-----ITEQWQQWGIGLQ-APAATEIPTENPRPAIK---------GSDRQVHEALTA 236
Cdd:cd19546 163 RAPLPLQFADyalwERELLAGEDdrdslIGDQIAYWRDALAgAPDELELPTDRPRPVLPsrragavplRLDAEVHARLME 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 237 wgdqpVAEAE------IVSSWLTVLMRWQGSQSALC--AIKVRDKAHANL---IGPLQTYLPVRVDMPDGST----LAQL 301
Cdd:cd19546 243 -----AAESAgatmftVVQAALAMLLTRLGAGTDVTvgTVLPRDDEEGDLegmVGPFARPLALRTDLSGDPTfrelLGRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 302 RLQVEEQLNGNDHPsFSTLLEVCPPKRDLSRTPYFQTGLQFIAHDVEQRD---FHAGNLTRLPTKQPSSDLDLFISC--W 376
Cdd:cd19546 318 REAVREARRHQDVP-FERLAELLALPPSADRHPVFQVALDVRDDDNDPWDapeLPGLRTSPVPLGTEAMELDLSLALteR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 37542635 377 VSDGT----LGLTLDYDCAVLNSSQVEVLAQALISVLSAPGEQP 416
Cdd:cd19546 397 RNDDGdpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
432-940 |
3.95e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 70.61 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 432 LAQAHGPRTTPP-QLTLTEWVAASTEKSPLAVAVIDHGQQL--SYAELWAR-----AALVAANIS--QHVAkprsIIAva 501
Cdd:PRK08315 2 LSYVRGPTDVPLlEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEvdalaKGLLALGIEkgDRVG----IWA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 502 lPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSD------------------------------- 550
Cdd:PRK08315 76 -PNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADgfkdsdyvamlyelapelatcepgqlqsarl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 ----------QQSVEG---WPQVARIRMEALDPDIRWVAPTgLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQR 617
Cdd:PRK08315 155 pelrrviflgDEKHPGmlnFDELLALGRAVDDAELAARQAT-LDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 618 TWPLTAQDNV-----LHnHSF---------------------SFDPSVwalfwplltggtiVLADVRTmEDSTALldlmi 671
Cdd:PRK08315 234 AMKLTEEDRLcipvpLY-HCFgmvlgnlacvthgatmvypgeGFDPLA-------------TLAAVEE-ERCTAL----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 672 rHdvsvlgGVPSLLGTLIDHP-FAndcravKLVLS-------GGEVLNPELAHK-IQKVWQADVANLYGPTEA----TID 738
Cdd:PRK08315 294 -Y------GVPTMFIAELDHPdFA------RFDLSslrtgimAGSPCPIEVMKRvIDKMHMSEVTIAYGMTETspvsTQT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 739 ALYFSIDKNAAgaiPIGYPIDNTDAYIVDLNLN-PVPPGVPGEIMLAGQNLARGYLGKPAQTAQ-----RFLpnpfgngr 812
Cdd:PRK08315 361 RTDDPLEKRVT---TVGRALPHLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTAEaidadGWM-------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 813 vyATGDLGRRWSSGAISYLGRrdqqVK---IRG----HRIELNEV--AHllcqalelkEAIVFAQHAGTEQAR----LVA 879
Cdd:PRK08315 430 --HTGDLAVMDEEGYVNIVGR----IKdmiIRGgeniYPREIEEFlyTH---------PKIQDVQVVGVPDEKygeeVCA 494
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37542635 880 AIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQLNDAG 940
Cdd:PRK08315 495 WIILRPGatLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQA 557
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
468-928 |
4.29e-12 |
|
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: 70.40 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 468 GQQLSYAELWARAALVAANISQHVA-KPRSIIAVALPRSAEFIAALLGVVRAG--HAFLP-------------------- 524
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGlRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 ---------IDPRLPTDR-----IQFLIENSGCELVIT----SDQQSVEGWPQvarirmeALDPDIRWVAPtglshsdAA 586
Cdd:cd05938 83 vvapelqeaVEEVLPALRadgvsVWYLSHTSNTEGVISlldkVDAASDEPVPA-------SLRAHVTIKSP-------AL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 587 YlIYTSGSTGVPKGVVVEHRQVvnnilWR----QRTWPLTAQDNVLHN----HSFSFdpsVWALFWPLLTGGTIVLadvR 658
Cdd:cd05938 149 Y-IYTSGTTGLPKAARISHLRV-----LQcsgfLSLCGVTADDVIYITlplyHSSGF---LLGIGGCIELGATCVL---K 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 659 TMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHK-IQKVWQADVANLYGPTEATI 737
Cdd:cd05938 217 PKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREfLRRFGPIRIREFYGSTEGNI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 738 DALYFSIDKNAAGAIPIGY-----------------PIDNTDAYIVdlnlnPVPPGVPGEIM--LAGQNLARGYLGKPAQ 798
Cdd:cd05938 297 GFFNYTGKIGAVGRVSYLYkllfpfelikfdvekeePVRDAQGFCI-----PVAKGEPGLLVakITQQSPFLGYAGDKEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 799 TAQRFLPNPFGNGRVY-ATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARL 877
Cdd:cd05938 372 TEKKLLRDVFKKGDVYfNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRI 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 37542635 878 -VAAIEQQPGLHSEGIK--QELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:cd05938 452 gMAAVKLKPGHEFDGKKlyQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
730-924 |
5.62e-12 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 68.87 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 730 YGPTEATIDALYFSIDKNAAGAIpiGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFlpnpfg 809
Cdd:cd17636 143 YGQTEVMGLATFAALGGGAIGGA--GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT------ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 810 NGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQARLV----AAIEQQP 885
Cdd:cd17636 215 RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI----GVPDPRWAqsvkAIVVLKP 290
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 37542635 886 GLHSEgiKQELLRH----LPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:cd17636 291 GASVT--EAELIEHcrarIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
461-923 |
7.00e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIEN 540
Cdd:PRK13390 15 AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 541 SGCELVITS---DQQSVE-GWPQVARI----RMEAL---DPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVV--VEHRQ 607
Cdd:PRK13390 95 SGARVLVASaalDGLAAKvGADLPLRLsfggEIDGFgsfEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKGIQpdLPGRD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 608 VvnnilwRQRTWPLTAQDNVLHNHS-----FSFDPSVWA--LFWPLLT---GGTIVLAdvrTMEDSTALLDLMIRHDVSV 677
Cdd:PRK13390 175 V------DAPGDPIVAIARAFYDISesdiyYSSAPIYHAapLRWCSMVhalGGTVVLA---KRFDAQATLGHVERYRITV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 678 LGGVPSLLGTLI----DHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEA----TIDALYFSIDKNAA 749
Cdd:PRK13390 246 TQMVPTMFVRLLkldaDVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAhgmtFIDSPDWLAHPGSV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 750 GAIPIGypidntDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLP-NPFGNgrvyATGDLGRRWSSGAI 828
Cdd:PRK13390 326 GRSVLG------DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPaHPFWT----TVGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 829 sYLGRRDQQVKIRGH-RIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLH-SEGIKQELLRHLPA---- 902
Cdd:PRK13390 396 -YLADRKSFMIISGGvNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRgSDELARELIDYTRSriah 474
|
490 500
....*....|....*....|.
gi 37542635 903 YLIPSQLLLLDELPRTATGKV 923
Cdd:PRK13390 475 YKAPRSVEFVDELPRTPTGKL 495
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
461-935 |
9.91e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.44 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 461 AVAVIDHGQQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIEN 540
Cdd:PLN02860 23 AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 541 SGCELVITSdqQSVEGWP---QVARIR-------MEALDPDI---------------RWVAPTGLSHS----DAAYLIYT 591
Cdd:PLN02860 103 VRPVMLVTD--ETCSSWYeelQNDRLPslmwqvfLESPSSSVfiflnsflttemlkqRALGTTELDYAwapdDAVLICFT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 592 SGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----H--SFSfdpSVWALfwpLLTGGTIVLadVRTMEDSTA 665
Cdd:PLN02860 181 SGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTaplcHigGLS---SALAM---LMVGACHVL--LPKFDAKAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 666 LlDLMIRHDVSVLGGVPSLLGTLI--------DHPFandcRAVKLVLSGGEVLNPELAHKIQKVW-QADVANLYGPTEA- 735
Cdd:PLN02860 253 L-QAIKQHNVTSMITVPAMMADLIsltrksmtWKVF----PSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEAc 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 736 ---TIDALYFSIDKNAAGAIPIGYPIDNTDAYI------------VDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTA 800
Cdd:PLN02860 328 sslTFMTLHDPTLESPKQTLQTVNQTKSSSVHQpqgvcvgkpaphVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 801 QRfLPNPFGngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQARL--- 877
Cdd:PLN02860 408 SV-LSNDGW----LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV----GVPDSRLtem 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37542635 878 -VAAI-----------EQQPGLHSEGIKQELLRH------LPAYLIPSQLLLL-DELPRTATGKV--DMLKLDQLAAPQ 935
Cdd:PLN02860 479 vVACVrlrdgwiwsdnEKENAKKNLTLSSETLRHhcreknLSRFKIPKLFVQWrKPFPLTTTGKIrrDEVRREVLSHLQ 557
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
566-924 |
1.44e-11 |
|
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: 68.56 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 566 EALDPDIRWVAPTGLS-------HSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRqRTWPLTA---QDNVL------- 628
Cdd:cd05929 101 GALDGLEDYEAAEGGSpetpiedEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTL-MAAALGFgpgADSVYlspaply 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 629 HNHsfsfdPSVWAlFWPLLTGGTIVLadvrtME--DSTALLDLMIRHDVSVLGGVPSLLGTLIDHP----FANDCRAVKL 702
Cdd:cd05929 180 HAA-----PFRWS-MTALFMGGTLVL-----MEkfDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPeavrNAYDLSSLKR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 703 VLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT----IDALYFSIDKNAAGAIPIGypidntDAYIVDLNLNPVPPGVP 778
Cdd:cd05929 249 VIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQgltiINGEEWLTHPGSVGRAVLG------KVHILDEDGNEVPPGEI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 779 GEIMLAGqNLARGYLGKPAQTAQRFlpnpfgNGRVYAT-GDLGRRWSSGAIsYLGRRDQQVKIRGHR-IELNEVAHLLCQ 856
Cdd:cd05929 323 GEVYFAN-GPGFEYTNDPEKTAAAR------NEGGWSTlGDVGYLDEDGYL-YLTDRRSDMIISGGVnIYPQEIENALIA 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 857 ALELKEAIVF-AQHAGTEQaRLVAAIEQQPG-LHSEGIKQELLRHLPAYL----IPSQLLLLDELPRTATGKVD 924
Cdd:cd05929 395 HPKVLDAAVVgVPDEELGQ-RVHAVVQPAPGaDAGTALAEELIAFLRDRLsrykCPRSIEFVAELPRDDTGKLY 467
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
471-820 |
1.52e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 68.82 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHvAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPidprLPT-------DRIQFLIENSGC 543
Cdd:PRK05850 36 LTWSQLYRRTLNVAEELRRH-GSTGDRAVILAPQGLEYIVAFLGALQAGLIAVP----LSVpqggahdERVSAVLRDTSP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 544 ELVITSDQ---------QSVEGWPQVARIRMEALDPDI-RWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNil 613
Cdd:PRK05850 111 SVVLTTSAvvddvteyvAPQPGQSAPPVIEVDLLDLDSpRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAN-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 614 wrqrtwpltaqdnvlhnhsfsFDPSVWALFWPllTGGTIVLadvrtmeDSTALLDLMIRHD--------VSVLGGVPSLL 685
Cdd:PRK05850 189 ---------------------FEQLMSDYFGD--TGGVPPP-------DTTVVSWLPFYHDmglvlgvcAPILGGCPAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 686 GTLI----------------DHPFA---N------------------DCRAVKLVLSGGEVLNPELAHKIQKVWQAdvAN 728
Cdd:PRK05850 239 TSPVaflqrparwmqllasnPHAFSaapNfafelavrktsdddmaglDLGGVLGIISGSERVHPATLKRFADRFAP--FN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 729 L--------YGPTEATI-----------DALYFSIDKNAAG-AIP---------IGYPIDNTDAY-IVDLNLN-PVPPGV 777
Cdd:PRK05850 317 LretairpsYGLAEATVyvatrepgqppESVRFDYEKLSAGhAKRcetgggtplVSYGSPRSPTVrIVDPDTCiECPAGT 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 37542635 778 PGEIMLAGQNLARGYLGKPAQTAQRF---LPNPFG---NGRVYATGDLG 820
Cdd:PRK05850 397 VGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtpEGPWLRTGDLG 445
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
946-1018 |
1.89e-11 |
|
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: 61.02 E-value: 1.89e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 946 APRTDLEQSVMTDFAQVLGLTA--VTPDTDFFEQ-GGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAIE 1018
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLE 76
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
584-932 |
3.26e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 68.20 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HSFSFDPSvwaLFWPLLTGGTIVL----A 655
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSAlplfHSFGLTVG---LFTPLLTGAEVFLypspL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 656 DVRTMEdstallDLMIRHDVSVLGGVPSLLGTL--IDHPFanDCRAVKLVLSGGEvlnpELAHKIQKVWQaDVANL---- 729
Cdd:PRK08043 443 HYRIVP------ELVYDRNCTVLFGTSTFLGNYarFANPY--DFARLRYVVAGAE----KLQESTKQLWQ-DKFGLrile 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 730 -YGPTEAtidALYFSID-KNAAGAIPIGYPIDNTDAYIVdlnlnPVpPGVP--GEIMLAGQNLARGYL--GKPAQTAQRF 803
Cdd:PRK08043 510 gYGVTEC---APVVSINvPMAAKPGTVGRILPGMDARLL-----SV-PGIEqgGRLQLKGPNIMNGYLrvEKPGVLEVPT 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 804 LPNPFGNGRV--YATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVaAI 881
Cdd:PRK08043 581 AENARGEMERgwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALV-LF 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 37542635 882 EQQPGLHSEGIKQELLRH-LPAYLIPSQLLLLDELPRTATGKVDMLKLDQLA 932
Cdd:PRK08043 660 TTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
427-932 |
4.80e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 67.35 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 427 MQQTVLAQAHGPRTTPpqltlTEWVAASTEKSPLAVAVIDHGQQLSYAELWARAALVAAN-ISQHVAKpRSIIAVALPRS 505
Cdd:PLN03102 1 MDNLALCEANNVPLTP-----ITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASlISLNITK-NDVVSVLAPNT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 506 AEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELV---------------ITSDQQSVEGWPQV--------AR 562
Cdd:PLN03102 75 PAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILfvdrsfeplarevlhLLSSEDSNLNLPVIfiheidfpKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 563 IRMEALDPD--IRWVAPTGLSHS---------DAAYLIYTSGSTGVPKGVVVEHRQVVNNIL-----WRQRTWPLTAQD- 625
Cdd:PLN03102 155 PSSEELDYEclIQRGEPTPSLVArmfriqdehDPISLNYTSGTTADPKGVVISHRGAYLSTLsaiigWEMGTCPVYLWTl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 626 NVLHNHSFSFDPSVWAlfwpllTGGTIVLADVRTMEDSTALLDLmirHDVSVLGGVPSLLGTLIDHPFANDC-RAVKL-V 703
Cdd:PLN03102 235 PMFHCNGWTFTWGTAA------RGGTSVCMRHVTAPEIYKNIEM---HNVTHMCCVPTVFNILLKGNSLDLSpRSGPVhV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 704 LSGGevlNPELAHKIQKVWQA--DVANLYGPTEATIDALYFS-------IDKNAAGAIPIGYPIDNTDAYIVDLNLNPVP 774
Cdd:PLN03102 306 LTGG---SPPPAALVKKVQRLgfQVMHAYGLTEATGPVLFCEwqdewnrLPENQQMELKARQGVSILGLADVDVKNKETQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 775 PGVP------GEIMLAGQNLARGYLGKPAQTAQrflpnPFGNGRVyATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELN 848
Cdd:PLN03102 383 ESVPrdgktmGEIVIKGSSIMKGYLKNPKATSE-----AFKHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 849 EVAHLLCQALELKEAIVFAQHAGT-----------EQARLVAAIEQQPGLHSEGIKQELLR-HLPAYLIPSQLLLLDELP 916
Cdd:PLN03102 457 EVENVLYKYPKVLETAVVAMPHPTwgetpcafvvlEKGETTKEDRVDKLVTRERDLIEYCReNLPHFMCPRKVVFLQELP 536
|
570
....*....|....*.
gi 37542635 917 RTATGKVDMLKLDQLA 932
Cdd:PLN03102 537 KNGNGKILKPKLRDIA 552
|
|
| UDP_G4E_3_SDR_e |
cd05240 |
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ... |
1063-1302 |
2.08e-10 |
|
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187551 [Multi-domain] Cd Length: 306 Bit Score: 63.54 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLlkrttsrviclcrakdaeHAKARILEGLKTYRIDVGSEL*RVEYLTGDLALPHLGLSEHQwq 1142
Cdd:cd05240 1 ILVTGAAGGLGRLLARRL------------------AASPRVIGVDGLDRRRPPGSPPKVEYVRLDIRDPAAADVFRE-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 tlaEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVdtllATHVPRP----FIEDDAPLRSA 1218
Cdd:cd05240 61 ---READAVVHLAFILDPPRDGAERHRINVDGTQNVLDACAAAGVPRVVVTSSV----AVYGAHPdnpaPLTEDAPLRGS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1219 VGVPvgYTGSKWVAEGVANLGLRR--GIPVSIFRPGLILGhtetgasQSIDYLLVALRG--FLPMGIVPDYPriFDIVPV 1294
Cdd:cd05240 134 PEFA--YSRDKAEVEQLLAEFRRRhpELNVTVLRPATILG-------PGTRNTTRDFLSprRLPVPGGFDPP--FQFLHE 202
|
....*...
gi 37542635 1295 DYVAAAIV 1302
Cdd:cd05240 203 DDVARALV 210
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
431-923 |
2.13e-10 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 65.25 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 431 VLAQAHGPRTTP--PQLTLTEWVAaSTEKSPLAVAVIDH--GQQLSYAELWARAALVAANISQHVA-KPRSIIAVALPRS 505
Cdd:PLN02574 24 IYSSKHPPVPLPsdPNLDAVSFIF-SHHNHNGDTALIDSstGFSISYSELQPLVKSMAAGLYHVMGvRQGDVVLLLLPNS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 506 AEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQ---------SVEGWPQVARIRMEALD-PDIRW- 574
Cdd:PLN02574 103 VYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENveklsplgvPVIGVPENYDFDSKRIEfPKFYEl 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 575 --------VAPTgLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNN----ILWRQRTWPLTAQDNVLHNHSFSFDPSVWAL 642
Cdd:PLN02574 183 ikedfdfvPKPV-IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvelfVRFEASQYEYPGSDNVYLAALPMFHIYGLSL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 643 F-WPLLT-GGTIVladVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLID--HPFANDC-RAVKLVLSGGEVLNPELAHK 717
Cdd:PLN02574 262 FvVGLLSlGSTIV---VMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKkaKGVCGEVlKSLKQVSCGAAPLSGKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 718 -IQKVWQADVANLYGPTEAT-IDALYFSIDKNAAGAiPIGYPIDNTDAYIVDLNLNP-VPPGVPGEIMLAGQNLARGYLG 794
Cdd:PLN02574 339 fVQTLPHVDFIQGYGMTESTaVGTRGFNTEKLSKYS-SVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLN 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 795 KPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAqhAGTEQ 874
Cdd:PLN02574 418 NPKATQSTIDKDGW-----LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA--VPDKE 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 875 AR--LVAAIEQQPG--LHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PLN02574 491 CGeiPVAFVVRRQGstLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKI 543
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
469-882 |
2.24e-10 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 65.14 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVIT 548
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 549 SDQQSV----EGWPQVARIR------------------------------MEALDPDIRWVAPTGLSHSDAAYLIYTSGS 594
Cdd:cd17641 90 EDEEQVdkllEIADRIPSVRyviycdprgmrkyddprlisfedvvalgraLDRRDPGLYEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 595 TGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVlhnhsFSFDPSVW------ALFWPLLTGGTI---------------- 652
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEY-----VSVLPLPWigeqmySVGQALVCGFIVnfpeepetmmedlrei 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 653 --------------VLADVRT-MEDSTALLDLMIRHDVSV--------LGGVPSLLGTLIDHPFANDC-----------R 698
Cdd:cd17641 245 gptfvllpprvwegIAADVRArMMDATPFKRFMFELGMKLglraldrgKRGRPVSLWLRLASWLADALlfrplrdrlgfS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 699 AVKLVLSGGEVLNPElahkIQKVWQA---DVANLYGPTEATidALYFSidkNAAGAIP---IGYPIDNTDAYIVDLnlnp 772
Cdd:cd17641 325 RLRSAATGGAALGPD----TFRFFHAigvPLKQLYGQTELA--GAYTV---HRDGDVDpdtVGVPFPGTEVRIDEV---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 773 vppgvpGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGR-RDQQVKIRGHRIELNEVA 851
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGW-----LHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIE 460
|
490 500 510
....*....|....*....|....*....|.
gi 37542635 852 HLLCQALELKEAIVFaqhaGTEQARLVAAIE 882
Cdd:cd17641 461 NKLKFSPYIAEAVVL----GAGRPYLTAFIC 487
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
469-933 |
3.08e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 64.80 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 469 QQLSYAELWARAALVAANISQHVAKPR-SIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCElVI 547
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGdQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE-VI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 548 TSDQQSVEgwpQVARIRMEAldPDIRWVAPTG-----------------------------------LSHSDAAYLIYTS 592
Cdd:PRK05620 116 VADPRLAE---QLGEILKEC--PCVRAVVFIGpsdadsaaahmpegikvysyealldgrstvydwpeLDETTAAAICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 593 GSTGVPKGVVVEHRQvvnniLWRQrTWPLTAQDNVLHNHSFSF---DPSVWALFW--PL---LTGGTIVLADVRTMEDST 664
Cdd:PRK05620 191 GTTGAPKGVVYSHRS-----LYLQ-SLSLRTTDSLAVTHGESFlccVPIYHVLSWgvPLaafMSGTPLVFPGPDLSAPTL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 665 A--LLDLMIRhdvsVLGGVPSLLGTLIDHPFANDCRAVKL--VLSGGEVLNPELAhkiqKVWQA----DVANLYGPTEAT 736
Cdd:PRK05620 265 AkiIATAMPR----VAHGVPTLWIQLMVHYLKNPPERMSLqeIYVGGSAVPPILI----KAWEErygvDVVHVWGMTETS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 ---------------IDALYfsidKNAAGAIPIG--YPIDNTDAYIVDLNLNpvppgvPGEIMLAGQNLARGYLGKPAQT 799
Cdd:PRK05620 337 pvgtvarppsgvsgeARWAY----RVSQGRFPASleYRIVNDGQVMESTDRN------EGEIQVRGNWVTASYYHSPTEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 800 ----AQRFLPNPFGNGRV-------YATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQ 868
Cdd:PRK05620 407 gggaASTFRGEDVEDANDrftadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 869 HAGTEQARLVAAIEQQPGLH-----SEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAA 933
Cdd:PRK05620 487 PDDKWGERPLAVTVLAPGIEptretAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
470-610 |
3.76e-10 |
|
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: 64.29 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 470 QLSYAELWARAALVAANISQHV-AKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVIT 548
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVgLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 549 SD--------------QQS----VEGWPQ---VARIRMEALDPDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQ 607
Cdd:cd05905 94 VEaclkglpkkllkskTAAeiakKKGWPKildFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
...
gi 37542635 608 VVN 610
Cdd:cd05905 174 LLA 176
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
741-1018 |
5.03e-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: 62.46 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 741 YFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGnGRVYATGDLG 820
Cdd:COG3433 7 PPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYP-AQPGRQADDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 821 RRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLR-- 898
Cdd:COG3433 86 RLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAal 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 899 --HLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQLNDAGGTECRAPRTDLEQSVMTDFAQVLGLTA--VTPDTDF 974
Cdd:COG3433 166 dkVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGVDPeeIDPDDNL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 37542635 975 FEQGGNSILLTRLAGTLSaKYQVQIPLHEFFLTPTPAAVAQAIE 1018
Cdd:COG3433 246 FDLGLDSIRLMQLVERWR-KAGLDVSFADLAEHPTLAAWWALLA 288
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-411 |
7.94e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 57 GTVDLAVVQQNLSAWIAHSESLRSLFVEV----------LERPVRLLMPTGLVKLEYFDRppsdadMAELIGAAFELDKG 126
Cdd:PRK12316 3669 EALDAAALEAALQALVEHHDALRLRFVEDaggwtaehlpVELGGALLWRAELDDAEELER------LGEEAQRSLDLADG 3742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 127 PLLRAFITRTAAQQHELHLVGHPIVVDEPS-------LQRIAQTLFQTEPDHQYPAVGAIAEVFQREQTLAQDAQITEQW 199
Cdd:PRK12316 3743 PLLRALLATLADGSQRLLLVIHHLVVDGVSwrilledLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAEL 3822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 200 QQWGIGLQApAATEIPTENPRPAIkgSDRQVHEALTAWG---------DQPVAEAEIVSSWL-----TVLMRWQGSQSAL 265
Cdd:PRK12316 3823 AYWQEQLQG-VSSELPCDHPQGAL--QNRHAASVQTRLDreltrrllqQAPAAYRTQVNDLLltalaRVVCRWTGEASAL 3899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 266 CAIK-------VRDKAHANLIGPLQTYLPVRvdMPDGSTLAQLRLQVEEQLNG--NDHPSFSTL--LEVCPPKRDLSRTP 334
Cdd:PRK12316 3900 VQLEghgredlFADIDLSRTVGWFTSLFPVR--LSPVEDLGASIKAIKEQLRAipNKGIGFGLLryLGDEESRRTLAGLP 3977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 335 YFQTGLQFIAH-----DVEQRDFHAGNLTRLPTKQPSSDLD--LFISCWVSDGTLGLTLDYDCAVLNSSQVEVLAQALIS 407
Cdd:PRK12316 3978 VPRITFNYLGQfdgsfDEEMALFVPAGESAGAEQSPDAPLDnwLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAA 4057
|
....
gi 37542635 408 VLSA 411
Cdd:PRK12316 4058 ELTA 4061
|
|
| SDR_e |
cd08946 |
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ... |
1063-1317 |
1.23e-09 |
|
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 212494 [Multi-domain] Cd Length: 200 Bit Score: 59.62 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRTtSRVICLCRAkdaehakarileglktyridvgsel*rveyltgdlalphlglsehqwq 1142
Cdd:cd08946 1 ILVTGGAGFIGSHLVRRLLERG-HEVVVIDRL------------------------------------------------ 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 tlaeevDVIYHNGALVNFVYPYS---ALKATNVGGTQAILELACTARLKSVQYVSTvdTLLATHVPRPFIEDDAPLRsav 1219
Cdd:cd08946 32 ------DVVVHLAALVGVPASWDnpdEDFETNVVGTLNLLEAARKAGVKRFVYASS--ASVYGSPEGLPEEEETPPR--- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1220 gvPV-GYTGSKWVAEGVAN-LGLRRGIPVSIFRPGLILG-HTETGASQSIDYLL--VALRGFLPMGIVPDYPRifDIVPV 1294
Cdd:cd08946 101 --PLsPYGVSKLAAEHLLRsYGESYGLPVVILRLANVYGpGQRPRLDGVVNDFIrrALEGKPLTVFGGGNQTR--DFIHV 176
|
250 260
....*....|....*....|...
gi 37542635 1295 DYVAAAIVHISMQPQGRDKFFHL 1317
Cdd:cd08946 177 DDVVRAILHALENPLEGGGVYNI 199
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
953-1012 |
1.27e-09 |
|
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: 55.26 E-value: 1.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 953 QSVMTDFAQVLGLTA--VTPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAA 1012
Cdd:pfam00550 1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
565-939 |
1.34e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.42 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 565 MEALDPDIRWvaPTgLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILwrQRTWP----LTAQDNVLhnhsfsfdPSV- 639
Cdd:PRK07008 161 VGAQDGDYDW--PR-FDENQASSLCYTSGTTGNPKGALYSHRSTVLHAY--GAALPdamgLSARDAVL--------PVVp 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 640 ------WALFWPL-LTGGTIVLADVRTmeDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFANDCRAVKL--VLSGGEVL 710
Cdd:PRK07008 228 mfhvnaWGLPYSApLTGAKLVLPGPDL--DGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLrrTVIGGSAC 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 711 NPELAHKIQKVWQADVANLYGPTE----ATIDALyfsidKNAAGAIPI----------GYPIDNTDAYIVDLNLNPVP-P 775
Cdd:PRK07008 306 PPAMIRTFEDEYGVEVIHAWGMTEmsplGTLCKL-----KWKHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPwD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 776 GVP-GEIMLAGQNLARGYLGKPAqtaqrflpNPFGNGRvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLL 854
Cdd:PRK07008 381 GKAfGDLQVRGPWVIDRYFRGDA--------SPLVDGW-FPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 855 CQALELKEAIVFAQHAGTEQARLVAAIEQQPGlhSEGIKQELLRH----LPAYLIPSQLLLLDELPRTATGKVDMLKL-D 929
Cdd:PRK07008 452 VAHPAVAEAACIACAHPKWDERPLLVVVKRPG--AEVTREELLAFyegkVAKWWIPDDVVFVDAIPHTATGKLQKLKLrE 529
|
410
....*....|
gi 37542635 930 QLAAPQLNDA 939
Cdd:PRK07008 530 QFRDYVLPTA 539
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
583-928 |
2.02e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.21 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 583 SDAAYLIYTSGSTGVPKGVVvehrqvvnnilwrqrtwpLTAQDNVLH---NHSFSFDPSVWALFWP-------------L 646
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAM------------------LTAAALTASadaTHDRLGGPGQWLLALPahhiaglqvlvrsV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 647 LTGGTIVLADVRTMEDSTALLDLmirhdVSVLGG-------VPSLLGTLIDHPFANDC-RAVKLVLSGGEVLNPELAHKI 718
Cdd:PRK07824 97 IAGSEPVELDVSAGFDPTALPRA-----VAELGGgrrytslVPMQLAKALDDPAATAAlAELDAVLVGGGPAPAPVLDAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 719 QKVwQADVANLYGPTEAtidalyfsidknAAGAIPIGYPIDNTDAYIVDlnlnpvppgvpGEIMLAGQNLARGYLGKPAq 798
Cdd:PRK07824 172 AAA-GINVVRTYGMSET------------SGGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 799 taqrflPNPFGNGRVYATGDLGRrWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFaqhaGTEQARL- 877
Cdd:PRK07824 227 ------PDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF----GLPDDRLg 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 878 ---VAAIEQQPGLHS--EGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:PRK07824 296 qrvVAAVVGDGGPAPtlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
498-923 |
2.13e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.59 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 498 IAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITsdqqsveGWPQVARIRMEALDPDirwvaP 577
Cdd:PRK08308 35 FAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLY-------GESDFTKLEAVNYLAE-----E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 578 TGLshsdaayLIYTSGSTGVPKGVvvehrqvvnnilwrQRTWplTAQDNVLHNHSFSFD------PSVWAlfwP------ 645
Cdd:PRK08308 103 PSL-------LQYSSGTTGEPKLI--------------RRSW--TEIDREIEAYNEALNceqdetPIVAC---Pvthsyg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 646 LLTGgtiVLADVR--------TMEDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAnDCRAVKLVLSGgEVLNPELAHK 717
Cdd:PRK08308 157 LICG---VLAALTrgskpviiTNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPG-TFQFHAVMTSG-TPLPEAWFYK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 718 IQKVWQAdVANLYGPTEATIdalyFSIDKNAAGAIPIGYPIDNTDayiVDLNLNPvppGVPGEIMLAGqnlargylgkpa 797
Cdd:PRK08308 232 LRERTTY-MMQQYGCSEAGC----VSICPDMKSHLDLGNPLPHVS---VSAGSDE---NAPEEIVVKM------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 798 qtaqrflpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARL 877
Cdd:PRK08308 289 ------------GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERV 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 37542635 878 VAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKV 923
Cdd:PRK08308 357 KAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
402-920 |
2.40e-09 |
|
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: 61.70 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 402 AQALISVLSAPGE---QPIATValMGQQMQQTVLAQ-AHGPRTTPPQLTLTewvaasteksplaVAVIDHGQQLSYAELW 477
Cdd:cd17632 10 LEAVTEAIRRPGLrlaQIIATV--MTGYADRPALGQrATELVTDPATGRTT-------------LRLLPRFETITYAELW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 478 ARA-ALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITS------D 550
Cdd:cd17632 75 ERVgAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSaehldlA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 551 QQSVEGWPQVARI-----------RMEALDPDIRWVAPTGL------------------------SHSDA-AYLIYTSGS 594
Cdd:cd17632 155 VEAVLEGGTPPRLvvfdhrpevdaHRAALESARERLAAVGIpvttltliavrgrdlppaplfrpePDDDPlALLIYTSGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 595 TGVPKGVVVEHRQVVNniLWRQRTW-----PLTAQdnVLHNHSFSFDPSVWALFWPLLTGGTIVLA---DVRTMEDSTAL 666
Cdd:cd17632 235 TGTPKGAMYTERLVAT--FWLKVSSiqdirPPASI--TLNFMPMSHIAGRISLYGTLARGGTAYFAaasDMSTLFDDLAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 667 L------------DLMIRHDVSVL------GGVPSLLGTLIDHPFANDCRAVKLV--LSGGEVLNPELAHKIQKVWQADV 726
Cdd:cd17632 311 VrptelflvprvcDMLFQRYQAELdrrsvaGADAETLAERVKAELRERVLGGRLLaaVCGSAPLSAEMKAFMESLLDLDL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 727 ANLYGPTEatidalyfsidknaAGAIPIgypidntDAYIV-----DLNLNPVP---------PGVPGEIMLAGQNLARGY 792
Cdd:cd17632 391 HDGYGSTE--------------AGAVIL-------DGVIVrppvlDYKLVDVPelgyfrtdrPHPRGELLVKTDTLFPGY 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 793 LGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKI-RGhriELNEVAHLlcqalelkEAIVFAQ--- 868
Cdd:cd17632 450 YKRPEVTAEVFDEDGF-----YRTGDVMAELGPDRLVYVDRRNNVLKLsQG---EFVTVARL--------EAVFAASplv 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 869 -----HAGTEQARLVAAIEQQPGlhsegikqELLRHLPAYLIPSqllLLDELPRTAT 920
Cdd:cd17632 514 rqifvYGNSERAYLLAVVVPTQD--------ALAGEDTARLRAA---LAESLQRIAR 559
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
470-611 |
2.62e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.56 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 470 QLSYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGhaFLPIDPRLPT---------DRIQFLIEN 540
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAG--LVPVPLPLPMgfggresyiAQLRGMLAS 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 541 SGCELVITSD------QQSVEGWPQVARIRMEALD-PDIRWVAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNN 611
Cdd:PRK09192 127 AQPAAIITPDellpwvNEATHGNPLLHVLSHAWFKaLPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN 204
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
439-933 |
4.69e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 61.13 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 439 RTTPPQLTLTEWVA-ASTEKSPLAVAVID-HGQQLSYAELWARAAlVAANISQHVAKPRSIIAVALPRSAEFIAALLGVV 516
Cdd:PRK06814 625 ETSDYDRTLFEALIeAAKIHGFKKLAVEDpVNGPLTYRKLLTGAF-VLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQ 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 517 RAGhaflpidpRLPTdRIQFL--IEN--SGCEL-----VITSDQ--------QSVEGWPQVAR-IRMEALDPDIRW---- 574
Cdd:PRK06814 704 SAG--------RVPA-MINFSagIANilSACKAaqvktVLTSRAfiekarlgPLIEALEFGIRiIYLEDVRAQIGLadki 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 575 ----------VAPTGLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HSFSfdpsvw 640
Cdd:PRK06814 775 kgllagrfplVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNAlpvfHSFG------ 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 641 alfwplLTGGTI--VLADVRT-MEDSTalLDLMIRHDVSVLGGVPSLLGTliD----------HPFanDCRAVKLVLSGG 707
Cdd:PRK06814 849 ------LTGGLVlpLLSGVKVfLYPSP--LHYRIIPELIYDTNATILFGT--DtflngyaryaHPY--DFRSLRYVFAGA 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 708 EVLNPElahkIQKVWQAD----VANLYGPTEatidalyfsidknAAGAIPIGYPIDN---TDAYI---VDLNLNPVpPGV 777
Cdd:PRK06814 917 EKVKEE----TRQTWMEKfgirILEGYGVTE-------------TAPVIALNTPMHNkagTVGRLlpgIEYRLEPV-PGI 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 778 P--GEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLlc 855
Cdd:PRK06814 979 DegGRLFVRGPNVMLGYLRAENPGVLEPPADGW-----YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEL-- 1051
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 856 qALELKEAivfAQHA------GTEQARLVAAIEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLD 929
Cdd:PRK06814 1052 -AAELWPD---ALHAavsipdARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVT 1127
|
....
gi 37542635 930 QLAA 933
Cdd:PRK06814 1128 KLAE 1131
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
431-821 |
5.03e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 60.83 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 431 VLAQAHGPRTTPPQLT--LTEWVAASTEKSPLAVAVIDHGQ--QLSYAELWARAALVAANISQHVAKPRSIIAVALPRSA 506
Cdd:PRK12582 37 VIKSRHPLGPYPRSIPhlLAKWAAEAPDRPWLAQREPGHGQwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 507 EFIAALLGVVRAGHAFLPIDPR---LPTD--RIQFLIENSGCELVItsdqqsVEGWPQVARIRMEALDPDIRWVAPTG-- 579
Cdd:PRK12582 117 EHALMTLAAMQAGVPAAPVSPAyslMSHDhaKLKHLFDLVKPRVVF------AQSGAPFARALAALDLLDVTVVHVTGpg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 580 --------------------------LSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLH---- 629
Cdd:PRK12582 191 egiasiafadlaatpptaavaaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVsldw 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 630 ---NHSFSFDpsvwALFWPLL-TGGTIVLADVRTMedsTALLDLMIR--HDVS--VLGGVPSLLGTLIDHPFAND--CRA 699
Cdd:PRK12582 271 mpwNHTMGGN----ANFNGLLwGGGTLYIDDGKPL---PGMFEETIRnlREISptVYGNVPAGYAMLAEAMEKDDalRRS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 700 V----KLVLSGGEVLNPELAHKIQKVWQADVA------NLYGPTEA--TIDALYFSIDKNAAgaipIGYPIDNtdayiVD 767
Cdd:PRK12582 344 FfknlRLMAYGGATLSDDLYERMQALAVRTTGhripfyTGYGATETapTTTGTHWDTERVGL----IGLPLPG-----VE 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 37542635 768 LNLNPVppGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGR 821
Cdd:PRK12582 415 LKLAPV--GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-----YRLGDAAR 461
|
|
| Arna_like_SDR_e |
cd05257 |
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ... |
1063-1251 |
7.88e-09 |
|
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187567 [Multi-domain] Cd Length: 316 Bit Score: 58.85 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLkRTTSRVICLCrakdaehakarILEGLKTYRIDVGSEL*RVEYLTGDLalphlgLSEHQWQ 1142
Cdd:cd05257 2 VLVTGADGFIGSHLTERLL-REGHEVRALD-----------IYNSFNSWGLLDNAVHDRFHFISGDV------RDASEVE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 TLAEEVDVIYHNGALVNFVYPYSA---LKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHvPRPFIEDDaPLRSAV 1219
Cdd:cd05257 64 YLVKKCDVVFHLAALIAIPYSYTAplsYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQ-DVPIDEDH-PLLYIN 141
|
170 180 190
....*....|....*....|....*....|...
gi 37542635 1220 GVPVGYTGSKWVAEGVA-NLGLRRGIPVSIFRP 1251
Cdd:cd05257 142 KPRSPYSASKQGADRLAySYGRSFGLPVTIIRP 174
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
587-850 |
9.23e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 60.14 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 587 YLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHNHS----FSFDPsvwALFWPLLTGGTIVLAD---VRT 659
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSsigwVSFHG---FLYGSLSLGNTFVMFEggiIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 660 MEDSTALLDLMIRHDVSVLGGVPSLLGTLIDH-PFAN------DCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGP 732
Cdd:PTZ00237 335 KHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATiirskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 733 TEATIDALY----FSIDKNAAG--AIPIGYPIDNTDAyiVDLNLN---------PVPPGvpgeimlagqnLARGYLGKPA 797
Cdd:PTZ00237 415 TEIGITYLYcyghINIPYNATGvpSIFIKPSILSEDG--KELNVNeigevafklPMPPS-----------FATTFYKNDE 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 798 QTAQRFLPNPfgngRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEV 850
Cdd:PTZ00237 482 KFKQLFSKFP----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTI 530
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
450-869 |
9.81e-09 |
|
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: 60.02 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 450 WVAASTEKSplavavidhgQQLSYAELWARAALVAANISQH-VAKPRSIIaVALPRSAEFIAALLGVVRAG--HA--FLP 524
Cdd:cd05967 72 YDSPVTGTE----------RTYTYAELLDEVSRLAGVLRKLgVVKGDRVI-IYMPMIPEAAIAMLACARIGaiHSvvFGG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 525 IDPRLPTDRIqfliENSGCELVITSD-----QQSVE------------GWPQVARI-------RMEALDP--DIRW---- 574
Cdd:cd05967 141 FAAKELASRI----DDAKPKLIVTAScgiepGKVVPykplldkalelsGHKPHHVLvlnrpqvPADLTKPgrDLDWsell 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 575 -----VAPTGLSHSDAAYLIYTSGSTGVPKGVVVE---HRQVVNnilWRQRTWPLTAQDNV---------LHNHSFSfdp 637
Cdd:cd05967 217 akaepVDCVPVAATDPLYILYTSGTTGKPKGVVRDnggHAVALN---WSMRNIYGIKPGDVwwaasdvgwVVGHSYI--- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 638 sVWAlfwPLLTGGTIVLAD---VRTmEDSTALLDLMIRHDVSVLGGVPSLLGTL------IDHPFANDCRAVKLVLSGGE 708
Cdd:cd05967 291 -VYG---PLLHGATTVLYEgkpVGT-PDPGAFWRVIEKYQVNALFTAPTAIRAIrkedpdGKYIKKYDLSSLRTLFLAGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 709 VLNPELAHKIQKVWQADVANLYGPTEA--TIDALYFSIDKNAAGAIPIGYPIDNTDAYIVDLNLNPVPPGVPGEIMLAGQ 786
Cdd:cd05967 366 RLDPPTLEWAENTLGVPVIDHWWQTETgwPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 787 nLARGYLGKPAQTAQRFLPNPFGNGR-VYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIV 865
Cdd:cd05967 446 -LPPGCLLTLWKNDERFKKLYLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV 524
|
....
gi 37542635 866 FAQH 869
Cdd:cd05967 525 VGVR 528
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
591-922 |
1.32e-08 |
|
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: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 591 TSGSTGVPKgVVVEHRQVVNNILWRQ----RTWPLTAQDnVLHNhSFSFDPSVWALFwplLTGG------TIVLAdvrTM 660
Cdd:COG1541 91 SSGTTGKPT-VVGYTRKDLDRWAELFarslRAAGVRPGD-RVQN-AFGYGLFTGGLG---LHYGaerlgaTVIPA---GG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 661 EDSTALLDLMIRHDVSVLGGVPSLLGTLIDHPFAN--DCRA--VKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT 736
Cdd:COG1541 162 GNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEgiDPRDlsLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 IDALYFSIDKNaagaipiGYPIDNTDAY--IVDLN-LNPVPPGVPGEIMLAGqnlargyLGKpaqTAQ---Rflpnpfgn 810
Cdd:COG1541 242 PGVAYECEAQD-------GLHIWEDHFLveIIDPEtGEPVPEGEEGELVVTT-------LTK---EAMpliR-------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 811 grvYATGDLGrRWSSGA---------ISY-LGRRDQQVKIRGHRIELNEVAHLLCQALEL-KEAIVFAQHAGtEQARLVA 879
Cdd:COG1541 297 ---YRTGDLT-RLLPEPcpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVgPEYQIVVDREG-GLDELTV 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 37542635 880 AIEQQPGLHSEGIKQELLRHLPAYL-IPSQLLLL--DELPRTaTGK 922
Cdd:COG1541 372 RVELAPGASLEALAEAIAAALKAVLgLRAEVELVepGSLPRS-EGK 416
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
1062-1277 |
2.01e-08 |
|
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187671 [Multi-domain] Cd Length: 354 Bit Score: 57.90 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1062 VVFLTGATGYLGLYLIEQLLKRTTS----RVICLCRAKDAEHAKARILegLKTYridvgsel*rVEYLTGDLalphlgLS 1137
Cdd:cd09811 1 VCLVTGGGGFLGQHIIRLLLERKEElkeiRVLDKAFGPELIEHFEKSQ--GKTY----------VTDIEGDI------KD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1138 EHQWQTLAEEVDVIYHNGALVNFVYP--YSALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPRPFI--EDDA 1213
Cdd:cd09811 63 LSFLFRACQGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFngVEDT 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1214 PLRSAvgVPVGYTGSKWVAEGV---AN-LGLRRGIPV--SIFRPGLILGHTETGASQSIDYLLVaLRGFL 1277
Cdd:cd09811 143 PYEDT--STPPYASSKLLAENIvlnANgAPLKQGGYLvtCALRPMYIYGEGSHFLTEIFDFLLT-NNGWL 209
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
571-946 |
2.21e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 58.76 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 571 DIRWVaptglSHSDAAYLIYTSGSTGVPKGVVvehrqvvnnilwrQRTWPLTAQDNVLHNHSFSFDPSvwALFW------ 644
Cdd:PLN02654 268 EVEWV-----DAEDPLFLLYTSGSTGKPKGVL-------------HTTGGYMVYTATTFKYAFDYKPT--DVYWctadcg 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 645 -----------PLLTGGTIVLAD-VRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLI---DHPFANDCRAVKLVL-SGGE 708
Cdd:PLN02654 328 witghsyvtygPMLNGATVLVFEgAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLgSVGE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 709 VLNPElahkiqkVWQAdVANLYGPTEATIDALYFSIDKNA------AGAIP-----IGYPIDNTDAYIVDLNLNPVPPGV 777
Cdd:PLN02654 408 PINPS-------AWRW-FFNVVGDSRCPISDTWWQTETGGfmitplPGAWPqkpgsATFPFFGVQPVIVDEKGKEIEGEC 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 778 PGEIMLAGQ--NLARGYLGKPAQTAQRFLpNPFGNgrVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLC 855
Cdd:PLN02654 480 SGYLCVKKSwpGAFRTLYGDHERYETTYF-KPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 856 QALELKEAIVFA-QHAGTEQA--RLVAAIEQQPglHSEGIKQELL----RHLPAYLIPSQLLLLDELPRTATGKVDMLKL 928
Cdd:PLN02654 557 SHPQCAEAAVVGiEHEVKGQGiyAFVTLVEGVP--YSEELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
410
....*....|....*...
gi 37542635 929 DQLAAPQLNDAGGTECRA 946
Cdd:PLN02654 635 RKIASRQLDELGDTSTLA 652
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
471-834 |
3.08e-08 |
|
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: 58.00 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 471 LSYAELWARAALVAANISQHVAK--PRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVIT 548
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 549 SDQQSVEGWPQVARIRMEALDPDIRwvaPTglsHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNI-----LWRqRTWPLTA 623
Cdd:cd05927 86 DAGVKVYSLEEFEKLGKKNKVPPPP---PK---PEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfkILE-ILNKINP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 624 QDNVLhnhSF-----SFDPSVWALFwpLLTGGTIVL--ADVRT-MEDSTAL-----------LDLM---IRHDVSVLGGV 681
Cdd:cd05927 159 TDVYI---SYlplahIFERVVEALF--LYHGAKIGFysGDIRLlLDDIKALkptvfpgvprvLNRIydkIFNKVQAKGPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 682 PSLL--------------GTLIDHPFA-----NDCRA-----VKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAT- 736
Cdd:cd05927 234 KRKLfnfalnyklaelrsGVVRASPFWdklvfNKIKQalggnVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 IDALYFSIDKNAAgaiPIGYPIDNTDAYIVD---LNLNPVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrv 813
Cdd:cd05927 314 GATLTLPGDTSVG---HVGGPLPCAEVKLVDvpeMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGW----- 385
|
410 420
....*....|....*....|.
gi 37542635 814 YATGDLGRRWSSGAISYLGRR 834
Cdd:cd05927 386 LHTGDIGEWLPNGTLKIIDRK 406
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
26-411 |
4.64e-08 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 56.93 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 26 YPLSSEQKRLwLLAQLAGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERpvRLLMPTGLVKLEyfd 105
Cdd:cd19542 2 YPCTPMQEGM-LLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAE--GTFLQVVLKSLD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 106 rPP------SDADMAELIGAAFE---LDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQ------TEPD 170
Cdd:cd19542 76 -PPieevetDEDSLDALTRDLLDdptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAayngqlLPPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 171 HQYPAVgaiaeVFQREQTLAQDAQitEQWQQWgigLQAPAATEIPTENPRPAIKGSDRQV---HEALTAWGDQP-VAEAE 246
Cdd:cd19542 155 PPFSDY-----ISYLQSQSQEESL--QYWRKY---LQGASPCAFPSLSPKRPAERSLSSTrrsLAKLEAFCASLgVTLAS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 247 IV-SSWLTVLMRWQGSQSALCAIKV--RDKAHAN---LIGPLQTYLPVRVDMPDGSTLAQLRLQVEEQL---NGNDHPSF 317
Cdd:cd19542 225 LFqAAWALVLARYTGSRDVVFGYVVsgRDLPVPGiddIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYlrsLPHQHLSL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 318 STLLEVCppkRDLSRTPYFQTGLQFI-AHDVEQRDFHAGNLTRLPTKQPSSDLDLFISCWVSDGTLGLTLDYDCAVLNSS 396
Cdd:cd19542 305 REIQRAL---GLWPSGTLFNTLVSYQnFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEE 381
|
410
....*....|....*
gi 37542635 397 QVEVLAQALISVLSA 411
Cdd:cd19542 382 QAEELLEQFDDILEA 396
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
646-937 |
4.80e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 646 LLTGGTIVLADVRTMEDSTALLdlmIRHDVSVLGGVPSLLGTLIDHPfANDCRAVKLVLSGGEVLNPELAHKiQKVWQAD 725
Cdd:PRK07445 182 FLTGGKLVILPYKRLKSGQELP---PNPSDFFLSLVPTQLQRLLQLR-PQWLAQFRTILLGGAPAWPSLLEQ-ARQLQLR 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 726 VANLYGPTE--ATIDALyfSIDKNAAGAIPIGYPIDNTDayiVDLNLNPVppgvpGEIMLAGQNLARGYLgkpaqtaqrf 803
Cdd:PRK07445 257 LAPTYGMTEtaSQIATL--KPDDFLAGNNSSGQVLPHAQ---ITIPANQT-----GNITIQAQSLALGYY---------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 804 lPNPFGNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTeqaRLVAA 880
Cdd:PRK07445 317 -PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGlpdPHWGE---VVTAI 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 881 -IEQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGKVDMLKLDQLAAPQLN 937
Cdd:PRK07445 393 yVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
1063-1361 |
7.40e-08 |
|
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187552 [Multi-domain] Cd Length: 331 Bit Score: 55.90 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRTTSRVICLCRAKDAEHAKARILEGLktyridvgsel*rvEYLTGDLAlpHLGLSEHQwq 1142
Cdd:cd05241 2 VLVTGGSGFFGERLVKQLLERGGTYVRSFDIAPPGEALSAWQHPNI--------------EFLKGDIT--DRNDVEQA-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 tlAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPR------PFIEDDAPLr 1216
Cdd:cd05241 64 --LSGADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFGGQNIHngdetlPYPPLDSDM- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1217 savgvpvgYTGSKWVAE-GVANLGLRRGIPVSIFRPGLILGHTETGASQSIDYllVALRGFlpmgivpDYPRI------F 1289
Cdd:cd05241 141 --------YAETKAIAEiIVLEANGRDDLLTCALRPAGIFGPGDQGLVPILFE--WAEKGL-------VKFVFgrgnnlV 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 1290 DIVPVDYVAAAIVHIS---MQPQG-RDKFFHLFNPAPVTIRQF-CDWIREFGYEFKLVdfehgrqqalSVPPGHLLY 1361
Cdd:cd05241 204 DFTYVHNLAHAHILAAaalVKGKTiSGQTYFITDAEPHNMFELlRPVWKALGFGSRPK----------IRLSGPLAY 270
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
27-153 |
1.59e-07 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 55.54 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQ-LAGTATLPVTVRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLE--RPVRLLMPTGLVKLEY 103
Cdd:cd19532 3 PMSFGQSRFWFLQQyLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdgEPMQGVLASSPLRLEH 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 104 fdRPPSDAD-----MAELIGAAFELDKGPLLRAFITRTAAQQHELhLVG-HPIVVD 153
Cdd:cd19532 83 --VQISDEAeveeeFERLKNHVYDLESGETMRIVLLSLSPTEHYL-IFGyHHIAMD 135
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
472-939 |
2.11e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.53 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 472 SYAELWARAALVAANISQHVAKPRSIIAVALPRSAEFIAALLGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVIT--- 548
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 549 --------SDQ-QSVEGW---------PQVA-------RIRMEALDPDIRWvapTGLSHSDAAYLIYTSGSTGVPKGVVV 603
Cdd:PRK06018 121 fvpilekiADKlPSVERYvvltdaahmPQTTlknavayEEWIAEADGDFAW---KTFDENTAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 604 EHR-QVVNNILWRQR-TWPLTAQDNVLHNHSFsFDPSVWAL-FWPLLTGGTIVLADVRTmeDSTALLDLMIRHDVSVLGG 680
Cdd:PRK06018 198 SHRsNVLHALMANNGdALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGAKL--DGASVYELLDTEKVTFTAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 681 VPSLLGTLIDHPFANDCR--AVKLVLSGGEVLnPELAHKIQKVWQADVANLYGPTE----ATIDALYFSIDKNAAGA--- 751
Cdd:PRK06018 275 VPTVWLMLLQYMEKEGLKlpHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEmsplGTLAALKPPFSKLPGDArld 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 752 --IPIGYPIDNTDAYIVDLNLNPVP--PGVPGEIMLAGQNLARGYLGKPAqtaqrflpNPFGNGRVYATGDLGRRWSSGA 827
Cdd:PRK06018 354 vlQKQGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGPAVAAAYYRVDG--------EILDDDGFFDTGDVATIDAYGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 828 ISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFAQHAGTEQARLVAAIEQQPGlhSEGIKQELLRHLPA----Y 903
Cdd:PRK06018 426 MRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG--ETATREEILKYMDGkiakW 503
|
490 500 510
....*....|....*....|....*....|....*..
gi 37542635 904 LIPSQLLLLDELPRTATGKVDMLKL-DQLAAPQLNDA 939
Cdd:PRK06018 504 WMPDDVAFVDAIPHTATGKILKTALrEQFKDYKLPTA 540
|
|
| NDUFA9_like_SDR_a |
cd05271 |
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ... |
1062-1337 |
2.73e-07 |
|
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187579 [Multi-domain] Cd Length: 273 Bit Score: 53.79 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1062 VVFLTGATGYLGLYLIEQLLKRTtSRVICLCRAkdaEHAKARILeglktyridVGSEL*RVEYLTGDLAlphlglSEHQW 1141
Cdd:cd05271 2 VVTVFGATGFIGRYVVNRLAKRG-SQVIVPYRC---EAYARRLL---------VMGDLGQVLFVEFDLR------DDESI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1142 QTLAEEVDVIYHngaLVNFVYPYSA--LKATNVGGTQAILELACTARLKsvQYVstvdtllatHVprpfieddaplrSAV 1219
Cdd:cd05271 63 RKALEGSDVVIN---LVGRLYETKNfsFEDVHVEGPERLAKAAKEAGVE--RLI---------HI------------SAL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1220 GV----PVGYTGSKWVAEGVanlgLRRGIP-VSIFRPGLILGHtetgASQSIDYLLVALRgFLPMGIVPDYP-RIFDIVP 1293
Cdd:cd05271 117 GAdansPSKYLRSKAEGEEA----VREAFPeATIVRPSVVFGR----EDRFLNRFAKLLA-FLPFPPLIGGGqTKFQPVY 187
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 37542635 1294 VDYVAAAIVHISMQPQGRDKFFHLFNPAPVTIRQFCDWIREFGY 1337
Cdd:cd05271 188 VGDVAEAIARALKDPETEGKTYELVGPKVYTLAELVELLRRLGG 231
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
583-834 |
3.87e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 54.62 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 583 SDAAYLIYTSGSTGVPKGVVVEHRQVVNNI-LWRQRtwpltAQDNVLHNHSFSFDP------SVWALFWPLLTGGTIVLa 655
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAeAMFVA-----AEFDVETDVMVSWLPlfhdmgMVGFLTVPMYFGAELVK- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 656 dVRTME--DSTAL-LDLMIRHDVSVLGGvP----SLLGTLI---DHPFANDCRAVKLVLSGGEVLNPelahkiqkvwqAD 725
Cdd:PRK07768 226 -VTPMDflRDPLLwAELISKYRGTMTAA-PnfayALLARRLrrqAKPGAFDLSSLRFALNGAEPIDP-----------AD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 726 VANL-----------------YGPTEAT----------------IDALYFSIDKNAAGA--------IPIGYPIDNTDAY 764
Cdd:PRK07768 293 VEDLldagarfglrpeailpaYGMAEATlavsfspcgaglvvdeVDADLLAALRRAVPAtkgntrrlATLGPPLPGLEVR 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 765 IVDLNLNPVPPGVPGEIMLAGQNLARGYLG----KPAQTAQRFlpnpfgngrvYATGDLGRRWSSGAISYLGRR 834
Cdd:PRK07768 373 VVDEDGQVLPPRGVGVIELRGESVTPGYLTmdgfIPAQDADGW----------LDTGDLGYLTEEGEVVVCGRV 436
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
1063-1328 |
4.74e-07 |
|
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];
Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 52.16 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRtTSRVICLCRakDAEHAKARILEGlktyridvgsel*rVEYLTGDLALPhlglsehqwQ 1142
Cdd:COG0702 2 ILVTGATGFIGRRVVRALLAR-GHPVRALVR--DPEKAAALAAAG--------------VEVVQGDLDDP---------E 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1143 TLA---EEVDVIYHngaLVNFVYPYSAlkATNVGGTQAILELACTARLKSVQYVSTVDTllathvprpfieDDAPlrsav 1219
Cdd:COG0702 56 SLAaalAGVDAVFL---LVPSGPGGDF--AVDVEGARNLADAAKAAGVKRIVYLSALGA------------DRDS----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1220 gvPVGYTGSKWVAEGVanlgLRR-GIPVSIFRPGLILGhtetGASQSIDYLLVALRGFLPMGIVPDYPrifdiVPVDYVA 1298
Cdd:COG0702 114 --PSPYLRAKAAVEEA----LRAsGLPYTILRPGWFMG----NLLGFFERLRERGVLPLPAGDGRVQP-----IAVRDVA 178
|
250 260 270
....*....|....*....|....*....|
gi 37542635 1299 AAIVHISMQPQGRDKFFHLFNPAPVTIRQF 1328
Cdd:COG0702 179 EAAAAALTDPGHAGRTYELGGPEALTYAEL 208
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
569-923 |
5.99e-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: 53.97 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 569 DPDIRWVAPtgLSHSDAAYLIYTSGSTGVPKGVVVEHRQVVNN-----ILWRQRTWPLTAQDNVLHnhsfSFDPSVWALF 643
Cdd:cd05915 141 LGEEADPVR--VPERAACGMAYTTGTTGLPKGVVYSHRALVLHslaasLVDGTALSEKDVVLPVVP----MFHVNAWCLP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 644 WPLLTGGTIVLAdVRTMEDSTALLDLMIRHDVSVLGGVPSLLGTLidhpfANDCRAVK-------LVLSGGEVlNPELAH 716
Cdd:cd05915 215 YAATLVGAKQVL-PGPRLDPASLVELFDGEGVTFTAGVPTVWLAL-----ADYLESTGhrlktlrRLVVGGSA-APRSLI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 717 KIQKVWQADVANLYGPTEA---TIDALYF----------SIDKNAAGAIpigypidNTDAYIVDLnLNPVPPGVPGE--- 780
Cdd:cd05915 288 ARFERMGVEVRQGYGLTETspvVVQNFVKshleslseeeKLTLKAKTGL-------PIPLVRLRV-ADEEGRPVPKDgka 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 781 ---IMLAGQNLARGYL-GKPAQTAQRFlpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQ 856
Cdd:cd05915 360 lgeVQLKGPWITGGYYgNEEATRSALT------PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMG 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 857 ALELKEAIVFAQHAGTEQARLVAAIEQQpglHSEGIKQELLRHLPAYL-----IPSQLLLLDELPRTATGKV 923
Cdd:cd05915 434 HPKVKEAAVVAIPHPKWQERPLAVVVPR---GEKPTPEELNEHLLKAGfakwqLPDAYVFAEEIPRTSAGKF 502
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
1063-1196 |
1.60e-06 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 50.76 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRtTSRVICLCRAKDAEHAKAriLEGLKTYRIDVGSEL*RVEYltgdlalphlgLSEHQwq 1142
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEK-GYEVIGLDRLTSASNTAR--LADLRFVEGDLTDRDALEKL-----------LADVR-- 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 37542635 1143 tlaeeVDVIYHNGAL----VNFVYPySALKATNVGGTQAILELACTARLKSVQYVSTV 1196
Cdd:pfam01370 65 -----PDAVIHLAAVggvgASIEDP-EDFIEANVLGTLNLLEAARKAGVKRFLFASSS 116
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
584-821 |
1.74e-06 |
|
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: 52.43 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 584 DAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWP-LTAQDNVL-----HNHSFSFDPSVWALFWpllTGGTIVLADV 657
Cdd:cd05921 166 TVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPfFGEEPPVLvdwlpWNHTFGGNHNFNLVLY---NGGTLYIDDG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 658 RTM-----EDSTALLDLMIRHDVSVLGGVPSLLGTLIDHP------FANdcraVKLVLSGGEVLNPELAHKIQKVWQADV 726
Cdd:cd05921 243 KPMpggfeETLRNLREISPTVYFNVPAGWEMLVAALEKDEalrrrfFKR----LKLMFYAGAGLSQDVWDRLQALAVATV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 727 ------ANLYGPTEATIDALYFSIDKNAAGAipIGYPIDNTDAYIvdlnlnpVPPGVPGEIMLAGQNLARGYLGKPAQTA 800
Cdd:cd05921 319 geripmMAGLGATETAPTATFTHWPTERSGL--IGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTA 389
|
250 260
....*....|....*....|.
gi 37542635 801 QRFLPNPFgngrvYATGDLGR 821
Cdd:cd05921 390 QAFDEEGF-----YCLGDAAK 405
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
27-160 |
3.00e-06 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 51.49 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 27 PLSSEQKRLWLLAQLAGTAT---LPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEY 103
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTflnLLLVCH--IKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 104 FD-----RPPSDAD--MAELIGAAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRI 160
Cdd:cd20483 81 IDlseaaDPEAALDqlVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSI 144
|
|
| PLN02503 |
PLN02503 |
fatty acyl-CoA reductase 2 |
1050-1195 |
3.22e-06 |
|
fatty acyl-CoA reductase 2
Pssm-ID: 215279 [Multi-domain] Cd Length: 605 Bit Score: 51.79 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1050 DGLPHANWYQPSVVFLTGATGYLGLYLIEQLLkRT---TSRVICLCRAKDAEHAKARI------LEGLKTYRIDVGSE-- 1118
Cdd:PLN02503 109 DGIGIAEFLRGKNFLITGATGFLAKVLIEKIL-RTnpdVGKIYLLIKAKDKEAAIERLknevidAELFKCLQETHGKSyq 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1119 ---L*RVEYLTGDLALPHLGLSEHQWQTLAEEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELA--CTaRLKSVQYV 1193
Cdd:PLN02503 188 sfmLSKLVPVVGNVCESNLGLEPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAkkCK-KLKLFLQV 266
|
..
gi 37542635 1194 ST 1195
Cdd:PLN02503 267 ST 268
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
462-924 |
6.31e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.80 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 462 VAVIDHGQQLSYAELWARAALVAANISQHVAKPRSI-IAVALPRSAEFIAALLGVVRAGHAFLPIDPrlpTDRIQFL--- 537
Cdd:PRK13388 18 IAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNT---TRRGAALaad 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 538 IENSGCELVITSDQQsvegwpqvaRIRMEALD-PDIR--------W---VAPTGLSH-------SDAAYLIYTSGSTGVP 598
Cdd:PRK13388 95 IRRADCQLLVTDAEH---------RPLLDGLDlPGVRvldvdtpaYaelVAAAGALTphrevdaMDPFMLIFTSGTTGAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 599 KGVVVEHRQVVnnILWRQRT--WPLTAQDnVLHN-----HSfsfdPSVWALFWPLL-TGGTIVLadVRTMEDSTALLDLM 670
Cdd:PRK13388 166 KAVRCSHGRLA--FAGRALTerFGLTRDD-VCYVsmplfHS----NAVMAGWAPAVaSGAAVAL--PAKFSASGFLDDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 671 iRHDVSVLGGVPSLLGTLIDHPFANDCRAVKLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEAtidALYFSIDKNA-A 749
Cdd:PRK13388 237 -RYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEG---AVIVVREPGTpP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 750 GAIPIGYPidntDAYIVDLN-LNPVPPGV-------------PGEIM-LAGQNLARGYLGKPAQTAQRflpnpFGNGRvY 814
Cdd:PRK13388 313 GSIGRGAP----GVAIYNPEtLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAER-----MRHGM-Y 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 815 ATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTEqarLVAAIEQQPG--LHS 889
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAvpdERVGDQ---VMAALVLRDGatFDP 459
|
490 500 510
....*....|....*....|....*....|....*..
gi 37542635 890 EGIKQELL--RHLPAYLIPSQLLLLDELPRTATGKVD 924
Cdd:PRK13388 460 DAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVL 496
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
948-1017 |
9.73e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 45.32 E-value: 9.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37542635 948 RTDLEQSVMTDFAQVLGLTA---VTPDTDFFEQGGNSILLTRLAGTLSAKYQVQIPLHEFFLTPTPAAVAQAI 1017
Cdd:smart00823 10 RRLLLDLVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
26-166 |
1.09e-05 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 49.51 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 26 YPLSSEQKRLWLLAQLAGTATLPVT-VRYAFTGTVDLAVVQQNLSAWIAHSESLRSLFV-EVLERPVRLLMPTGLVKLEY 103
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGAYVEqMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37542635 104 FD-RPPSDADMAELIGA--------AFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQ 166
Cdd:cd19543 82 LDlSHLSEAEQEAELEAlaeedrerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFA 153
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
441-923 |
1.40e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 49.29 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 441 TPPQLTLTEWVAASTEKSPLAVAVIDhgQQLSYAELWARAALVAANISQHV--AKPRSIiAVALPRSAEFIAALLGVVRA 518
Cdd:PRK07867 1 TSSAPTVAELLLPLAEDDDRGLYFED--SFTSWREHIRGSAARAAALRARLdpTRPPHV-GVLLDNTPEFSLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 519 GHAFLPIDPrlpTDRIQFL---IENSGCELVITSDQQSV---EGWPQVARIRMEAL----------DPDIRWVAPTGlsh 582
Cdd:PRK07867 78 GIVPVGLNP---TRRGAALardIAHADCQLVLTESAHAElldGLDPGVRVINVDSPawadelaahrDAEPPFRVADP--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 583 SDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWPLTAQDNVLHN----HSfsfdPSVWALFWP-LLTGGTIVLAdv 657
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSmplfHS----NAVMAGWAVaLAAGASIALR-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 658 RTMEDSTALLDLMiRHDVSVLGGVPSLLGTLIDHPFANDCRAVKL-VLSGGEVLNPELAhKIQKVWQADVANLYGPTEAT 736
Cdd:PRK07867 226 RKFSASGFLPDVR-RYGATYANYVGKPLSYVLATPERPDDADNPLrIVYGNEGAPGDIA-RFARRFGCVVVDGFGSTEGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 737 IdALYFSIDkNAAGAipIGYPIDNTDAYIVDlNLNPVPPGVP------------GEIM-LAGQNLARGYLGKPAQTAQRF 803
Cdd:PRK07867 304 V-AITRTPD-TPPGA--LGPLPPGVAIVDPD-TGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 804 lpnpfgNGRVYATGDLGRRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQALELKEAIVFA---QHAGTeqaRLVAA 880
Cdd:PRK07867 379 ------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAvpdPVVGD---QVMAA 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 37542635 881 IEQQPG-----------LHSE---GIKQellrhlpaylIPSQLLLLDELPRTATGKV 923
Cdd:PRK07867 450 LVLAPGakfdpdafaefLAAQpdlGPKQ----------WPSYVRVCAELPRTATFKV 496
|
|
| AR_like_SDR_e |
cd05193 |
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ... |
1063-1299 |
3.10e-05 |
|
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187536 [Multi-domain] Cd Length: 295 Bit Score: 47.61 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLK-----RTTSR----VICLCRAKDAEHAKARilegLKTYRIDVGSEL*RVEYLTGdlalph 1133
Cdd:cd05193 1 VLVTGASGFVASHVVEQLLErgykvRATVRdpskVKKVNHLLDLDAKPGR----LELAVADLTDEQSFDEVIKG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1134 lglsehqwqtlaeeVDVIYHNGALVNFV--YPYSALKAtNVGGTQAILElACTA--RLKSVQYVSTVDTLLATHVPRPFI 1209
Cdd:cd05193 71 --------------CAGVFHVATPVSFSskDPNEVIKP-AIGGTLNALK-AAAAakSVKRFVLTSSAGSVLIPKPNVEGI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1210 EDDAP-------LRSAVGVPVGYTGSKWVAEGVA-NLGLRRGIPVSIFRPGLILGHTETGASQSIDYLLVAlrgfLPMGI 1281
Cdd:cd05193 135 VLDEKswnleefDSDPKKSAWVYAASKTLAEKAAwKFADENNIDLITVIPTLTIGTIFDSETPSSSGWAMS----LITGN 210
|
250
....*....|....*...
gi 37542635 1282 VPDYPRIFDIVPVDYVAA 1299
Cdd:cd05193 211 EGVSPALALIPPGYYVHV 228
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
465-821 |
3.39e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 48.34 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 465 IDHGQqLSYAELWARAALVA-----ANISQHVAKPRSIIAVALP------RSAEFIAALLGVVRAGHAFLPIDPRLPtDR 533
Cdd:PRK08180 105 IEHAL-LALAAMYAGVPYAPvspaySLVSQDFGKLRHVLELLTPglvfadDGAAFARALAAVVPADVEVVAVRGAVP-GR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 534 IQFLIEnsgcELVITSDQQSVEGwpqvariRMEALDPDirwvaptglshsDAAYLIYTSGSTGVPKGVVVEHRQVVNNIL 613
Cdd:PRK08180 183 AATPFA----ALLATPPTAAVDA-------AHAAVGPD------------TIAKFLFTSGSTGLPKAVINTHRMLCANQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 614 WRQRTWP-LTAQDNVL-------H----NHSFSFdpsvwALFWplltGGTIVLADVRTMEdstALLDLMIR--HDVS--V 677
Cdd:PRK08180 240 MLAQTFPfLAEEPPVLvdwlpwnHtfggNHNLGI-----VLYN----GGTLYIDDGKPTP---GGFDETLRnlREISptV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 678 LGGVPSLLGTLID----------HPFANdcraVKLVLSGGEVLNPELAHKIQKVWQADVANL------YGPTEATIDALY 741
Cdd:PRK08180 308 YFNVPKGWEMLVPalerdaalrrRFFSR----LKLLFYAGAALSQDVWDRLDRVAEATCGERirmmtgLGMTETAPSATF 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 742 FSIDKNAAGaiPIGYPIDNTDAYIvdlnlnpVPPGVPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFgngrvYATGDLGR 821
Cdd:PRK08180 384 TTGPLSRAG--NIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-----YRSGDAVR 449
|
|
| SDR_e_a |
cd05226 |
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
1063-1256 |
4.01e-05 |
|
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187537 [Multi-domain] Cd Length: 176 Bit Score: 45.86 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRtTSRVICLCRAKDA--EHAKARILEGLktyrIDVGSEL*RVEYLTGdlalphlglsehq 1140
Cdd:cd05226 1 ILILGATGFIGRALARELLEQ-GHEVTLLVRNTKRlsKEDQEPVAVVE----GDLRDLDSLSDAVQG------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1141 wqtlaeeVDVIYHNGALVNFVypySALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPRPFIEDDAplrsavg 1220
Cdd:cd05226 63 -------VDVVIHLAGAPRDT---RDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDLHEETEPSPSSP------- 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 37542635 1221 vpvgYTGSKWVAEGVAnlgLRRGIPVSIFRPGLILG 1256
Cdd:cd05226 126 ----YLAVKAKTEAVL---REASLPYTIVRPGVIYG 154
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
56-265 |
5.75e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.24 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 56 TGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEYFDRPPSDADMAELIGAA---FELDKGPLLRAF 132
Cdd:PRK05691 2821 RQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELLWQVTVADFAECAALFADAqrsLDLQQGPLLRAL 2900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 133 ITRTAAQQHELHLVGHPIVVDEPS---LQRIAQTLFQTEPDHQYPAVGAIAEVFQ----REQTLAQDAQITEQWQQWGIG 205
Cdd:PRK05691 2901 LVDGPQGQQRLLLAIHHLVVDGVSwrvLLEDLQALYRQLSAGAEPALPAKTSAFRdwaaRLQAYAGSESLREELGWWQAQ 2980
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 206 LQAPAAtEIPTENPrpaiKGSDRQVH-EALTAWGD----------QPVAEAEIVSSWL-----TVLMRWQGSQSAL 265
Cdd:PRK05691 2981 LGGPRA-ELPCDRP----QGGNLNRHaQTVSVRLDaertrqllqqAPAAYRTQVNDLLltalaRVLCRWSGQPSVL 3051
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
58-265 |
1.21e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.08 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 58 TVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLE-YFDRPPSDADMAELIG----AAFELDKGPLLRAF 132
Cdd:PRK12467 2212 ALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQERRPlLWQVVVADKEELEALCeqaqRSLDLEEGPLLRAV 2291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 133 ITRTAAQQHELHLVGHPIVVDEPS-------LQRIAQTLFQTEPDHQYPAVGAIAEVFQREQTLAQDAQITEQWQQWGIG 205
Cdd:PRK12467 2292 LATLPDGSQRLLLVIHHLVVDGVSwrilledLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQ 2371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 206 LQApAATEIPTENPRPAIkgSDRQVHEALT----AWGDQPVAEA------EIVSSWLT----VLMRWQGSQSAL 265
Cdd:PRK12467 2372 LQG-ASTELPCDHPQGGL--QRRHAASVTThldsEWTRRLLQEApaayrtQVNDLLLTalarVIARWTGQASTL 2442
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
1066-1233 |
1.47e-04 |
|
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
Pssm-ID: 366449 [Multi-domain] Cd Length: 279 Bit Score: 45.44 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1066 TGATGYLGLYLIEQLLKRTTSRVIclcRAKDAEHAkarileglkTYRIDVGSEL*RVEYLTGDLalphlgLSEHQWQTLA 1145
Cdd:pfam01073 3 TGGGGFLGRHIIKLLVREGELKEV---RVFDLRES---------PELLEDFSKSNVIKYIQGDV------TDKDDLDNAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1146 EEVDVIYHNGALVNF--VYPYSALKATNVGGTQAILELACTARLKSVQYVSTVDTLLATHVPRPFIEDDAPLRSAVGVPV 1223
Cdd:pfam01073 65 EGVDVVIHTASAVDVfgKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQD 144
|
170
....*....|
gi 37542635 1224 GYTGSKWVAE 1233
Cdd:pfam01073 145 AYPRSKAIAE 154
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
581-850 |
1.52e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 46.26 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 581 SHSDAAYLIYTSGSTGVPKGVVVEHRQVVNNILWRQRTWP-LTAQDnvlhnhsfsfdpsVWALFWPL-----LTGGTIVL 654
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKND-------------VYLAYLPLahileLAAESVMA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 655 A--------DVRTMEDSTALLDLMIRHDVSVLG-----GVPSLLG------------------TLIDHPFANDCRAV--- 700
Cdd:PLN02387 315 AvgaaigygSPLTLTDTSNKIKKGTKGDASALKptlmtAVPAILDrvrdgvrkkvdakgglakKLFDIAYKRRLAAIegs 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 701 ----------------------------KLVLSGGEVLNPELAHKIQKVWQADVANLYGPTEATIDALYFSIDKNAAGAi 752
Cdd:PLN02387 395 wfgawglekllwdalvfkkiravlggriRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGR- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 753 pIGYPIDNTDAYIVD-------LNLNPVPpgvPGEIMLAGQNLARGYLGKPAQTAQRFLPNPFGNgRVYATGDLGRRWSS 825
Cdd:PLN02387 474 -VGPPLPCCYVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGM-RWFYTGDIGQFHPD 548
|
330 340
....*....|....*....|....*.
gi 37542635 826 GAISYLGRRDQQVKIR-GHRIELNEV 850
Cdd:PLN02387 549 GCLEIIDRKKDIVKLQhGEYVSLGKV 574
|
|
| UDP_invert_4-6DH_SDR_e |
cd05237 |
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ... |
1061-1195 |
3.13e-04 |
|
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187548 [Multi-domain] Cd Length: 287 Bit Score: 44.53 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1061 SVVFLTGATGYLGLYLIEQLLKRTTSRVICLCRAKDAEHAKARILEGLKTyridvgseL*RVEYLTGDLA-LPHLGLSEH 1139
Cdd:cd05237 3 KTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDENKLHELVRELRSRFP--------HDKLRFIIGDVRdKERLRRAFK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37542635 1140 QWQtlaeeVDVIYHNGALvNFV-----YPYSALKaTNVGGTQAILELACTARLKSVQYVST 1195
Cdd:cd05237 75 ERG-----PDIVFHAAAL-KHVpsmedNPEEAIK-TNVLGTKNVIDAAIENGVEKFVCIST 128
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
25-167 |
5.72e-04 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 44.23 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 25 AYPLSSEQKRLWLLAQLAGTAT---LPVTVRyaFTGTVDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKL 101
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSaynVPLCFR--FSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSF 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37542635 102 EYFDrpPSDADMAELIG-------AAFELDKGPLLRAFITRTAAQQHELHLVGHPIVVDEPSLQRIAQTLFQT 167
Cdd:cd20484 79 QEED--ISSLKESEIIAylrekakEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDA 149
|
|
| PLN02996 |
PLN02996 |
fatty acyl-CoA reductase |
1063-1195 |
9.61e-04 |
|
fatty acyl-CoA reductase
Pssm-ID: 215538 [Multi-domain] Cd Length: 491 Bit Score: 43.54 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1063 VFLTGATGYLGLYLIEQLLK--RTTSRVICLCRAKDAEHAKAR----ILEG--LKTYRIDVGSEL-----*RVEYLTGDL 1129
Cdd:PLN02996 14 ILVTGATGFLAKIFVEKILRvqPNVKKLYLLLRASDAKSATQRlhdeVIGKdlFKVLREKLGENLnslisEKVTPVPGDI 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37542635 1130 ALPHLG-----LSEHQWQtlaeEVDVIYHNGALVNFVYPYSALKATNVGGTQAILELA--CtARLKSVQYVST 1195
Cdd:PLN02996 94 SYDDLGvkdsnLREEMWK----EIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAkkC-VKVKMLLHVST 161
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
59-160 |
1.07e-03 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 43.39 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 59 VDLAVVQQNLSAWIAHSESLRSLFVE-------VLERPVrllmpTGLVKLEYFDR--PPSDADMAELIG---AAFELDKG 126
Cdd:cd19534 34 LDPDALRQALRALVEHHDALRMRFRRedggwqqRIRGDV-----EELFRLEVVDLssLAQAAAIEALAAeaqSSLDLEEG 108
|
90 100 110
....*....|....*....|....*....|....*
gi 37542635 127 PLLRA-FITRTAAQQHeLHLVGHPIVVDEPSlQRI 160
Cdd:cd19534 109 PLLAAaLFDGTDGGDR-LLLVIHHLVVDGVS-WRI 141
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
583-612 |
1.44e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.16 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|
gi 37542635 583 SDAAYLIYTSGSTGVPKGVVVEHRQVVNNI 612
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANV 250
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
505-656 |
1.61e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 42.73 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 505 SAE-FIAALlGVVRAGHAFLPIDPRLPTDRIQFLIENSGCELVITSDQQsvegwpQVARIR------------------M 565
Cdd:cd05933 43 SPEwFIAAV-GAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQK------QLQKILqiqdklphlkaiiqykepL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 566 EALDPD-IRW--VAPTGLSHSDAAY--------------LIYTSGSTGVPKGVVVEHrqvvNNILWRQRTWPLTAQDN-- 626
Cdd:cd05933 116 KEKEPNlYSWdeFMELGRSIPDEQLdaiissqkpnqcctLIYTSGTTGMPKGVMLSH----DNITWTAKAASQHMDLRpa 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 37542635 627 -VLHNHSFSFDP---------SVWAlfwPLLTGGTIVLAD 656
Cdd:cd05933 192 tVGQESVVSYLPlshiaaqilDIWL---PIKVGGQVYFAQ 228
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
779-941 |
1.75e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.83 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 779 GEIMLAGQNLARGYLGKPaqtaqrflpnPFGNGRVYATGDLGrRWSSGAISYLGRRDQQVKIRGHRIELNEVAHLLCQAL 858
Cdd:PRK05851 373 GEIEIRGASMMSGYLGQA----------PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 859 ELKEAIVFAQHAGTEQAR--LVAAIEQQpGLHSEGIKQELLRHLPAY--LIPSQLLLLD--ELPRTATGKVDMLKLDQla 932
Cdd:PRK05851 442 GVREGAVVAVGTGEGSARpgLVIAAEFR-GPDEAGARSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLRRLAVKR-- 518
|
....*....
gi 37542635 933 apQLNDAGG 941
Cdd:PRK05851 519 --SLEAADG 525
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
190-411 |
2.31e-03 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 41.90 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 190 AQDAQITEQWQQWGIGLQAPAATEIPTENPRPAIKGS-DRQVHEALTAWGDQPVAeAEIVSSWLTVLMRWQGSQSALCAI 268
Cdd:cd19545 162 LDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATlEHSISLPSSASSGVTLA-TVLRAAWALVLSRYTGSDDVVFGV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 269 KV--RDkAH----ANLIGPLQTYLPVRVDMPDGSTLAQLRLQVEEQLngndhpsfstllevcppkrdLSRTPYFQTGLQF 342
Cdd:cd19545 241 TLsgRN-APvpgiEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDL--------------------LDMIPFEHTGLQN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 343 IA-------------------HDVEQRDFHAGNLTRLPTKQPSSDLD---LFISCWVSDGTLGLTLDYDCAVLNSSQVEV 400
Cdd:cd19545 300 IRrlgpdaraacnfqtllvvqPALPSSTSESLELGIEEESEDLEDFSsygLTLECQLSGSGLRVRARYDSSVISEEQVER 379
|
250
....*....|.
gi 37542635 401 LAQALISVLSA 411
Cdd:cd19545 380 LLDQFEHVLQQ 390
|
|
| SDR_a5 |
cd05243 |
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ... |
1063-1115 |
2.90e-03 |
|
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187554 [Multi-domain] Cd Length: 203 Bit Score: 40.68 E-value: 2.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 37542635 1063 VFLTGATGYLGLYLIEQLLKRtTSRVICLCRakDAEHAKARILEGLKTYRIDV 1115
Cdd:cd05243 2 VLVVGATGKVGRHVVRELLDR-GYQVRALVR--DPSQAEKLEAAGAEVVVGDL 51
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-265 |
3.07e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 42.25 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 59 VDLAVVQQNLSAWIAHSESLRSLFVEVLERPVRLLMPTGLVKLEYFDRPPSDADMAELIGAA---FELDKGPLLRAFITR 135
Cdd:PRK12316 1133 LDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEAqrsLDLEQGPLLRALLVD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 136 TAAQQHELHLVGHPIVVDEPSLQRIAQTLFQTEPDHQyPAVGAIAEVFQR--EQTLAQDAQITEQWQQWGIGLqAPAATE 213
Cdd:PRK12316 1213 MADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLD-ADLPARTSSYQAwaRRLHEHAGARAEELDYWQAQL-EDAPHE 1290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 214 IPTENPRPAIKGS-DRQVHEALTA------WGDQPVAEAEIVSSWL-----TVLMRWQGSQSAL 265
Cdd:PRK12316 1291 LPCENPDGALENRhERKLELRLDAertrqlLQEAPAAYRTQVNDLLltalaRVTCRWSGQASVL 1354
|
|
| 4_coum_CoA_lig |
TIGR02372 |
4-coumarate--CoA ligase, photoactive yellow protein activation family; This model represents ... |
822-923 |
4.11e-03 |
|
4-coumarate--CoA ligase, photoactive yellow protein activation family; This model represents the 4-coumarate--CoA ligase associated with biosynthesis of the 4-hydroxy cinnamyl (also called 4-coumaroyl) chromophore covalently linked to a Cys residue in photoactive yellow protein of Rhodobacter spp. and
Pssm-ID: 131425 [Multi-domain] Cd Length: 386 Bit Score: 41.44 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 822 RWSS-GAISYLGRRDQQVKIRGHRIELNEVAHLLcQALELKEAIVFAQHAGTEQARLVAAIEQQPGLHSEGIKQELLRHL 900
Cdd:TIGR02372 284 AWDKdGGFTILGRKDEILQVGGVNVSPGHVRDIL-ERNPRVRAAAVRLDGRRLKAFIVVAEDADEAELEIELRATAARHL 362
|
90 100
....*....|....*....|...
gi 37542635 901 PAYLIPSQLLLLDELPRTATGKV 923
Cdd:TIGR02372 363 PAPARPDRFRFGTELPRTGAGKL 385
|
|
| GDP_MD_SDR_e |
cd05260 |
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ... |
1062-1193 |
8.06e-03 |
|
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187570 [Multi-domain] Cd Length: 316 Bit Score: 40.27 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37542635 1062 VVFLTGATGYLGLYLIEQLLKRtTSRVICLCRakdaeHAKARILEGLKTYRIDVGsel*RVEYLTGDLALPHlglSEHQW 1141
Cdd:cd05260 1 RALITGITGQDGSYLAEFLLEK-GYEVHGIVR-----RSSSFNTDRIDHLYINKD----RITLHYGDLTDSS---SLRRA 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 37542635 1142 QTLAEEvDVIYHNGAL----VNFVYPYSALkATNVGGTQAILELACTARLKSVQYV 1193
Cdd:cd05260 68 IEKVRP-DEIYHLAAQshvkVSFDDPEYTA-EVNAVGTLNLLEAIRILGLDARFYQ 121
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
861-922 |
9.80e-03 |
|
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: 36.37 E-value: 9.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37542635 861 KEAIVFAQHAGTEQARLVAAI--EQQPGLHSEGIKQELLRHLPAYLIPSQLLLLDELPRTATGK 922
Cdd:pfam13193 13 AEAAVVGVPDELKGEAPVAFVvlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| |
