|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
9-1400 |
0e+00 |
|
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: 2456.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 9 WANILDGPTLSVLPRDYNRPVAGKVIEANKTFDisdiLPFLNKANEPSVTQFTAPLAVFAVLVYRLTGDDDIVILTDSPK 88
Cdd:TIGR03443 2 WSERLDNPTLSVLPHDYLRPANNRLVEATYSLQ----LPSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTSSNK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 89 KQNlPFVVRLQVDPSKSFVDVSKQVGEQYLESLERA-TPLKDIVTHLKESKQLPNYPPIFRLSFQTAKKVQQlSTLVEGS 167
Cdd:TIGR03443 78 SGR-PFVLRLNITPELSFLQLYAKVSEEEKEGASDIgVPFDELSEHIQAAKKLERTPPLFRLAFQDAPDNQQ-TTYSTGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 168 TRDLAIFLENNTS---INIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAPETPIGKISLLTEQQSKLLPDPTANLDWSGYR 244
Cdd:TIGR03443 156 TTDLTVFLTPSSPeleLSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLPDPTKDLDWSGFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 245 GAIQDIFSDNAEKFPDRTCVVETKSFLNPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGV 324
Cdd:TIGR03443 236 GAIHDIFADNAEKHPDRTCVVETPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 325 LKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLEKAGVLDQLVEDYIKNELSLVSRISNLKIEADGNVLGGDVDG--KD 402
Cdd:TIGR03443 316 LKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDYIDKELELRTEIPALALQDDGSLVGGSLEGgeTD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 403 ALYDYQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMF 482
Cdd:TIGR03443 396 VLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 483 TPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQN 562
Cdd:TIGR03443 476 TPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAEN 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 563 VNIINMYGTTETQRAVSYFEIPSRAQDSTFLEVQKDIMPAGKGMHNVQLLVVNRHDRSKTCAIGEVGEIYVRAAGLAEQY 642
Cdd:TIGR03443 556 VCIVNMYGTTETQRAVSYFEIPSRSSDSTFLKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGEVGEIYVRAGGLAEGY 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 643 RGQPDLNKEKFVPNWFVSPSKWVEEDKKisKDEPWREFYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIEL 722
Cdd:TIGR03443 636 LGLPELNAEKFVNNWFVDPSHWIDLDKE--NNKPEREFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIEL 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 723 GEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPK-ETPELENFKSSSDDLDDLNdPIVKSLLLYRELIKDLKAHLKK 801
Cdd:TIGR03443 714 GEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdKSDELEEFKSEVDDEESSD-PVVKGLIKYRKLIKDIREYLKK 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 802 TLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQLAAVAQKSSAEVDDSEFTTTELQIKDLWLQVLPNPPASISLED 881
Cdd:TIGR03443 793 KLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDD 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 882 SFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAEVDRVKNGDEVQFA-DNKQESTSAGSDEqvvDYFQDA 960
Cdd:TIGR03443 873 SFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEELADEgDSEIEEEETVLEL---DYAKDA 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 961 KDLVSSqLLDSYKSRLALSNAELINIFLTGATGFLGSYILKDLLER--DLDVQVYAHVRAKDEESGLERLRNTGKVYGIW 1038
Cdd:TIGR03443 950 KTLVDS-LPKSYPSRKELDASTPITVFLTGATGFLGSFILRDLLTRrsNSNFKVFAHVRAKSEEAGLERLRKTGTTYGIW 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1039 NEEWTSRIKVVIADLSKDKLGLSGEKYAELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVS 1118
Cdd:TIGR03443 1029 DEEWASRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVS 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1119 STSTLDTEHYITLSDTLTEQGEDGIPESDDLLGSSKGLGTGYGQSKWAAEYIIRRAFERGLRGAIIRPGYVTGHSRTGAC 1198
Cdd:TIGR03443 1109 STSALDTEYYVNLSDELVQAGGAGIPESDDLMGSSKGLGTGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGAT 1188
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1199 NTDDFLLRMLKGCAELGKLPNISNTVNMVPVDHVALVVTASSLHPTAEEGHCVVQVTGHPRIRFNEFLNALNDYGYEVKL 1278
Cdd:TIGR03443 1189 NTDDFLLRMLKGCIQLGLIPNINNTVNMVPVDHVARVVVAAALNPPKESELAVAHVTGHPRIRFNDFLGTLKTYGYDVEI 1268
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1279 TDYVEWKRDLERFVVDQSKDSALYPLLHFVLDNLPQDTKAPELDDKNAKDILSGDTRWTGYDGSKGRGVDSAQTGIYIAY 1358
Cdd:TIGR03443 1269 VDYVHWRKSLERFVIERSEDNALFPLLHFVLDDLPQSTKAPELDDTNAATSLKADAAWTGVDVSSGAGVTEEQIGIYIAY 1348
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|..
gi 254566307 1359 LIKTGFLPPPSKEGKKPLPEIEISEESLKLIKeGAGARTSAA 1400
Cdd:TIGR03443 1349 LVKVGFLPAPTKTGALPLPKIEISEAQLKLIA-SAGGRGSAA 1389
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
258-834 |
0e+00 |
|
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: 1005.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 258 FPDRTCVVETKSFLNpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPA 337
Cdd:cd17647 1 FPERTCVVETPSLNS--SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 338 YPPARQNVYLQVAKPAGLIVLEKAGVLdqlvedyiknelslvsrisnlkieadgnvlggdvdgkdalydyqqfktrrtgv 417
Cdd:cd17647 79 YPPARQNIYLGVAKPRGLIVIRAAGVV----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 418 lVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSD 497
Cdd:cd17647 106 -VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 498 DIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRA 577
Cdd:cd17647 185 DIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 578 VSYFEIPSRAQDSTFLEVQKDIMPAGKGMHNVQLLVVNRHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNW 657
Cdd:cd17647 265 VSYFEVPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 658 FVSPSKWVEEDKkiSKDEPWREFYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQ 737
Cdd:cd17647 345 FVEPDHWNYLDK--DNNEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRE 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 738 NVTLVRRDKDEEPILISYVVPK-ETPELENFKSSSDDLDDLNDPIVKSLLLYRELIKDLKAHLKKTLASYAIPTIIVPMA 816
Cdd:cd17647 423 NITLVRRDKDEEPTLVSYIVPRfDKPDDESFAQEDVPKEVSTDPIVKGLIGYRKLIKDIREFLKKRLASYAIPSLIVVLD 502
|
570
....*....|....*...
gi 254566307 817 KLPLNPNGKVDKPKLPFP 834
Cdd:cd17647 503 KLPLNPNGKVDKPKLQFP 520
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
259-831 |
6.37e-138 |
|
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: 430.03 E-value: 6.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd05930 1 PDAVAVV---------DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARqnvylqvakpaglivlekagvLDQLVEDyiknelslvsriSNLKIeadgnvlggdvdgkdalydyqqfktrrtgVL 418
Cdd:cd05930 72 PAER---------------------LAYILED------------SGAKL-----------------------------VL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDD 498
Cdd:cd05930 90 TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 499 IGTPGKLAEWMQTYGATVTHLTPAM-GQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRA 577
Cdd:cd05930 170 RKDPEALADLLAEEGITVLHLTPSLlRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 578 VSYFEIPSRaqdstflEVQKDIMPAGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNW 657
Cdd:cd05930 250 ATYYRVPPD-------DEEDGRVPIGRPIPNTRVYVLDENLR--PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 658 FvspskwveedkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQ 737
Cdd:cd05930 321 F------------------------GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVRE 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 738 NVTLVRRDKDEEPILISYVVPKETPELENfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIPTIIVPMAK 817
Cdd:cd05930 377 AAVVAREDGDGEKRLVAYVVPDEGGELDE--------------------------EELRAHLAERLPDYMVPSAFVVLDA 430
|
570
....*....|....
gi 254566307 818 LPLNPNGKVDKPKL 831
Cdd:cd05930 431 LPLTPNGKVDRKAL 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-928 |
6.83e-138 |
|
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: 457.01 E-value: 6.83e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG-PTLSVLPRDYNRPVAGKVIEANKTFDISDIL--PFLNKANEPSVTQFTAPLAVFAVLVYRLTGDDD 79
Cdd:COG1020 205 ARQLAYWRQQLAGlPPLLELPTDRPRPAVQSYRGARVSFRLPAELtaALRALARRHGVTLFMVLLAAFALLLARYSGQDD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 80 IVILT-----DSPKKQNLP--FV----VRLQVDPSKSFVDVSKQVGEQYLESLE-RATPLKDIVTHLKESKQLpNYPPIF 147
Cdd:COG1020 285 VVVGTpvagrPRPELEGLVgfFVntlpLRVDLSGDPSFAELLARVRETLLAAYAhQDLPFERLVEELQPERDL-SRNPLF 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 148 R--LSFQ-TAKKVQQLS----TLVEGSTR----DLAIFLENNT---SINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAP 213
Cdd:COG1020 364 QvmFVLQnAPADELELPgltlEPLELDSGtakfDLTLTVVETGdglRLTLEYNTDLFDAATIERMAGHLVTLLEALAADP 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 214 ETPIGKISLLTE-QQSKLLPDPTAN-LDWSGYRGaIQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNI 291
Cdd:COG1020 444 DQPLGDLPLLTAaERQQLLAEWNATaAPYPADAT-LHELFEAQAARTPDAVAVV---------FGDQSLTYAELNARANR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 292 VGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAglIVLEKAGVLDQLVEDy 371
Cdd:COG1020 514 LAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGAR--LVLTQSALAARLPEL- 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 372 iknelslvsrisnlkieaDGNVLggDVDgKDALYDYqqfktrrtgvlvgPDSNPTLS----------FTSGSEGIPKGVL 441
Cdd:COG1020 591 ------------------GVPVL--ALD-ALALAAE-------------PATNPPVPvtpddlayviYTSGSTGRPKGVM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 442 GRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTP 521
Cdd:COG1020 637 VEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTP 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 522 AMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYFEIPSRAQDStflevqkDIMP 601
Cdd:COG1020 717 SLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADG-------GSVP 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 602 AGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPSkwveedkkiskdepwrefy 681
Cdd:COG1020 790 IGRPIANTRVYVLDAHLQ--PVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPG------------------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 682 lgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKET 761
Cdd:COG1020 849 ----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 762 PELENfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQLAA 841
Cdd:COG1020 925 AAAAA--------------------------ALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAA 978
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 842 VAQkssaevddSEFTTTELQIKDLWLQVLPNPPASISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKL 921
Cdd:COG1020 979 AAA--------PPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAA 1050
|
....*..
gi 254566307 922 FAAEVDR 928
Cdd:COG1020 1051 AAAAAAA 1057
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
985-1284 |
3.50e-124 |
|
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: 387.39 E-value: 3.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYAHVRAKDEESGLERLRNTGKVYG--IWNEEWTSRIKVVIADLSKDKLGLSG 1062
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRKNVSKIYCLVRAKDEEAALERLIDNLKEYGlnLWDELELSRIKVVVGDLSKPNLGLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1063 EKYAELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHYitlsdtlteqGEDG 1142
Cdd:cd05235 81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEY----------NALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1143 IPESDDLLGSSKGLGTGYGQSKWAAEYIIRRAFERGLRGAIIRPGYVTGHSRTGACNTDDFLLRMLKGCAELGKLPNISN 1222
Cdd:cd05235 151 DEESDDMLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIYPISGA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254566307 1223 TVNMVPVDHVALVVTASSLHPtaEEGHCVVQVTGHPRIRFNEFLNALNDYGYEVKLTDYVEW 1284
Cdd:cd05235 231 PLDLSPVDWVARAIVKLALNE--SNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEEW 290
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
985-1364 |
8.97e-119 |
|
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: 375.60 E-value: 8.97e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYAHVRAKDEESGLERLRNTGKVYGIWNEEWT-SRIKVVIADLSKDKLGLSGE 1063
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRSTRAKVICLVRADSEEHAMERLREALRSYRLWHENLAmERIEVVAGDLSKPRLGLSDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1064 KYAELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHYITlsdtlteqgedGI 1143
Cdd:TIGR01746 81 EWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLST-----------GV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1144 PESDDLLGSSKGLGTGYGQSKWAAEYIIRRAFERGLRGAIIRPGYVTGHSRTGACNTDDFLLRMLKGCAELGKLPNIS-N 1222
Cdd:TIGR01746 150 TEDDATVTPYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQSPeL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1223 TVNMVPVDHVALVVTASSLHPTAEEGHCVVQVTGHPRIRFNEFLNALNDYGYEVKLTDYVEWKRDLERfVVDQSKDSALY 1302
Cdd:TIGR01746 230 TEDLTPVDFVARAIVALSSRPAASAGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLED-SDTAKRDSRRY 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 1303 PLL---HFVLDNLPQDTK-APELDDKNAKDILSGdtrwtgyDGSKGRGVDSAQTGIYIAYLIKTGF 1364
Cdd:TIGR01746 309 PLLpllHFTGDAFESDETdTRNLDSRSTAEALEG-------DGIREPSITAPLLHLYLQYLKEIGF 367
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
281-739 |
3.40e-117 |
|
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: 373.14 E-value: 3.40e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 281 TYKQIDQASNIVGNYLVHT-GIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLE 359
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 360 K-AGVLDQLVedyiknelslvsrisnlkieadgnVLGGDVDGKDALYDYQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPK 438
Cdd:TIGR01733 81 AlASRLAGLV------------------------LPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 439 GVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKL-AEWMQTYGATVT 517
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 518 HLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYFEIPSRAQDSTFLevqk 597
Cdd:TIGR01733 217 NLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 598 diMPAGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepw 677
Cdd:TIGR01733 293 --VPIGRPLANTRLYVLDDDLR--PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPF------------------- 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254566307 678 refYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNV 739
Cdd:TIGR01733 350 ---AGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-927 |
2.03e-100 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 356.39 E-value: 2.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANIL-DGPTLSVLPRDYNRPVA----GKVIEANKTFDISDILPFLnkANEPSVTQFTAPLAVFAVLVYRLTGD 77
Cdd:PRK12467 237 ERQLAYWQEQLgGEHTVLELPTDRPRPAVpsyrGARLRVDLPQALSAGLKAL--AQREGVTLFMVLLASFQTLLHRYSGQ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 78 DDIVILTDSPKKQNLPF-----------VVRLQVDPSKSFVDVSKQVGEQYLES-LERATPLKDIVTHLKESKQLpNYPP 145
Cdd:PRK12467 315 SDIRIGVPNANRNRVETerligffvntqVLKAEVDPQASFLELLQQVKRTALGAqAHQDLPFEQLVEALQPERSL-SHSP 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 146 IFRLSFQ-----TAKKVQQLSTL----VEG------STR-DLAI-FLENNTSI--NIYYNSLLYTHNRIAYFSQQFSSFI 206
Cdd:PRK12467 394 LFQVMFNhqntaTGGRDREGAQLpgltVEElswarhTAQfDLALdTYESAQGLwaAFTYATDLFEATTIERLATHWRNLL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 207 DEVNKAPETPIGKISLL-TEQQSKLLPDptANLDWSGY-RGAIQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQ 284
Cdd:PRK12467 474 EAIVAEPRRRLGELPLLdAEERARELVR--WNAPATEYaPDCVHQLIEAQARQHPERPALV---------FGEQVLSYAE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 285 IDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARqnvyLQvakpaglIVLEKAGVL 364
Cdd:PRK12467 543 LNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR----LA-------YMLDDSGVR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 365 DQLVEDYIKNELSLVSRISNLKIEADGNVLggdvdgkdalydyQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRH 444
Cdd:PRK12467 612 LLLTQSHLLAQLPVPAGLRSLCLDEPADLL-------------CGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISH 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 445 FSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMG 524
Cdd:PRK12467 679 GALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHL 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 525 Q-LLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYFEIPSRAQDStflevqkDIMPAG 603
Cdd:PRK12467 759 QaLLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDF-------GNVPIG 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 604 KGMHNVQLLVVNRHdrSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPSKwveedkkiskdepwrefylg 683
Cdd:PRK12467 832 QPLANLGLYILDHY--LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGG-------------------- 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 684 prdRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVrRDKDEEPILISYVVPKETPE 763
Cdd:PRK12467 890 ---RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVPAAVAD 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 764 LENfksssddlddlndpivkslllYRELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQLAAVA 843
Cdd:PRK12467 966 GAE---------------------HQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATF 1024
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 844 QKSSAEVddseftttELQIKDLWLQVLPNPPasISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFA 923
Cdd:PRK12467 1025 VAPQTEL--------EKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFA 1094
|
....
gi 254566307 924 AEVD 927
Cdd:PRK12467 1095 QAVA 1098
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
988-1233 |
3.54e-98 |
|
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: 314.93 E-value: 3.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 988 LTGATGFLGSYILKDLLERDLDV-QVYAHVRAKDEESGLERLRNTGKVYGIWNEEW---TSRIKVVIADLSKDKLGLSGE 1063
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRSTPDVkKIYLLVRAKDGESALERLRQELEKYPLFDALLkeaLERIVPVAGDLSEPNLGLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1064 KYAELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQ-FGFVSsTSTLDTEHYITLSDTLTEQGEDG 1142
Cdd:pfam07993 81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKpFHHVS-TAYVNGERGGLVEEKPYPEGEDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1143 IPESDDLLGSSKGLGTGYGQSKWAAEYIIRRAFERGLRGAIIRPGYVTGHSRTGACNTDDFLLRMLKGCAELGKLPNISN 1222
Cdd:pfam07993 160 MLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSILG 239
|
250
....*....|....*
gi 254566307 1223 T----VNMVPVDHVA 1233
Cdd:pfam07993 240 DpdavLDLVPVDYVA 254
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
985-1263 |
5.69e-97 |
|
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: 311.76 E-value: 5.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDlDVQVYAHVRAKDEESGLERLRNTGKVYGIWNEEWTSRIKVVIADLSKDKLGLSGEK 1064
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRT-DARVYCLVRASDEAAARERLEALLERYGLWLELDASRVVVVAGDLTQPRLGLSEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 YAELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHYitlsdtlteqgeDGIP 1144
Cdd:COG3320 81 FQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADR------------SGVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1145 ESDDlLGSSKGLGTGYGQSKWAAEYIIRRAFERGLRGAIIRPGYVTGHSRTGACNTDDFLLRMLKGCAELGKLPNISN-T 1223
Cdd:COG3320 149 EEDD-LDEGQGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPGLGDaR 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 254566307 1224 VNMVPVDHVALVVTASSLHPtaEEGHCVVQVTGHPRIRFN 1263
Cdd:COG3320 228 LNLVPVDYVARAIVHLSRQP--EAAGRTFHLTNPQPLSLG 265
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
249-831 |
5.16e-94 |
|
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: 312.21 E-value: 5.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:cd12117 1 ELFEEQAARTPDAVAVV---------YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPARQNVYLQVAKPAGLIVLEK-AGVLDQLVEDYIKNELSLvsrisnlkiEADGNVLGGDVDGKDALYdy 407
Cdd:cd12117 72 AAYVPLDPELPAERLAFMLADAGAKVLLTDRSlAGRAGGLEVAVVIDEALD---------AGPAGNPAVPVSPDDLAY-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 408 qqfktrrtgvlvgpdsnptLSFTSGSEGIPKGVLGRHFS---LAYYFPWMSktfnLSENDKFTMLSGIAHDPIQRDMFTP 484
Cdd:cd12117 141 -------------------VMYTSGSTGRPKGVAVTHRGvvrLVKNTNYVT----LGPDDRVLQTSPLAFDASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 485 LFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVN 564
Cdd:cd12117 198 LLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 565 IINMYGTTETQRAVSYFEIPSRAQDStflevqkDIMPAGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQYRG 644
Cdd:cd12117 278 LVNGYGPTENTTFTTSHVVTELDEVA-------GSIPIGRPIANTRVYVLDEDGR--PVPPGVPGELYVGGDGLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 645 QPDLNKEKFVPNWFvspskwveedkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGE 724
Cdd:cd12117 349 RPALTAERFVADPF------------------------GPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 725 IDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLA 804
Cdd:cd12117 405 IEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAA----------------------------ELRAFLRERLP 456
|
570 580
....*....|....*....|....*..
gi 254566307 805 SYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd12117 457 AYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-939 |
5.40e-94 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 336.93 E-value: 5.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 13 LDGPTLSV--LPRDYNRPVAGkVIEANKTFDISDILPFLNKANEPSVTQFTAPLAVFAVLVYRLTGDDDIVI-LTDSPKK 89
Cdd:PRK12316 4292 LDEPTRLAqaIARADLRSANG-YGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFgATVAGRP 4370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 90 QNLP--------FVVRLQV----DPSKSFVDVSKQVGEQYLESLERA-TPLKDIVTHLKESKQ--------LPNYPPIFR 148
Cdd:PRK12316 4371 AELPgiegqiglFINTLPViatpRAQQSVVEWLQQVQRQNLALREHEhTPLYEIQRWAGQGGEalfdsllvFENYPVSEA 4450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 149 LSFQTAKKVQQLSTLVEGSTR---DLAIFLENNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAPETPIGKISLL-T 224
Cdd:PRK12316 4451 LQQGAPGGLRFGEVTNHEQTNyplTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLeK 4530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 225 EQQSKLLPDPTANLdwSGY--RGAIQDIFSDNAEKFPDRTCVVetksFlnpnsQTRTFTYKQIDQASNIVGNYLVHTGIK 302
Cdd:PRK12316 4531 AEQQRIVALWNRTD--AGYpaTRCVHQLVAERARMTPDAVAVV----F-----DEEKLTYAELNRRANRLAHALIARGVG 4599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 303 RGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQnvylqvakpagLIVLEKAGVLDQLVEDYIKNELSLVSRI 382
Cdd:PRK12316 4600 PEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERL-----------AYMMEDSGAALLLTQSHLLQRLPIPDGL 4668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 383 SNLKIEADGnvlggdvdgkdalyDYQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSE 462
Cdd:PRK12316 4669 ASLALDRDE--------------DWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTP 4734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 463 NDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPtSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLS--AQATKEIPSLHH 540
Cdd:PRK12316 4735 DDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAehAERDGEPPSLRV 4813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 541 AFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYFeipsRAQDSTflEVQKDIMPAGKGMHNVQLLVVNrhDRS 620
Cdd:PRK12316 4814 YCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLW----KARDGD--ACGAAYMPIGTPLGNRSGYVLD--GQL 4885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 621 KTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPSKwveedkkiskdepwrefylgprdRLYRTGDLGRYLPT 700
Cdd:PRK12316 4886 NPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGG-----------------------RLYRTGDLARYRAD 4942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 701 GDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVtLVRRDKDEEPILISYVVPKETPELENFKSSSddlddlndp 780
Cdd:PRK12316 4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV-VIAQEGAVGKQLVGYVVPQDPALADADEAQA--------- 5012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 781 ivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQL--AAVAQKSSAEVddsefttt 858
Cdd:PRK12316 5013 ---------ELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLqqAYVAPRSELEQ-------- 5075
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 859 elQIKDLWLQVLPNPpaSISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAEVDRVKNGDEVQFA 938
Cdd:PRK12316 5076 --QVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFD 5151
|
.
gi 254566307 939 D 939
Cdd:PRK12316 5152 D 5152
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
249-831 |
1.56e-91 |
|
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: 305.35 E-value: 1.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEG---------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPARQNVYLQVAKPAglIVLEKAGVLDQLVedyiknelslvsrisnlkieadgnVLGGDVDGKDALYDyq 408
Cdd:cd17646 73 AAYLPLDPGYPADRLAYMLADAGPA--VVLTTADLAARLP------------------------AGGDVALLGDEALA-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 409 QFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLG 488
Cdd:cd17646 125 APPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 489 AQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAM-GQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTiAQNVNIIN 567
Cdd:cd17646 205 ARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMlRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLA-LPGAELHN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 568 MYGTTETQRAVSYFEIPSRAQDSTflevqkdiMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPD 647
Cdd:cd17646 284 LYGPTEAAIDVTHWPVRGPAETPS--------VPIGRPVPNTRLYVLD--DALRPVPVGVPGELYLGGVQLARGYLGRPA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 648 LNKEKFVPNWFvspskwveedkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDT 727
Cdd:cd17646 354 LTAERFVPDPF------------------------GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 728 HISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELENfksssddlddlndpivkslllyrelIKDLKAHLKKTLASYA 807
Cdd:cd17646 410 ALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPD-------------------------TAALRAHLAERLPEYM 464
|
570 580
....*....|....*....|....
gi 254566307 808 IPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd17646 465 VPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
251-835 |
7.99e-90 |
|
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: 300.78 E-value: 7.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 251 FSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAT 330
Cdd:cd17655 3 FEEQAEKTPDHTAVV---------FEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 331 FSVIDPAYPPARQNvYLqvakpaglivLEKAGVldqlveDYIKNELSLVSRISNLkieadgnvlgGDVDgkdaLYDYQQF 410
Cdd:cd17655 74 YLPIDPDYPEERIQ-YI----------LEDSGA------DILLTQSHLQPPIAFI----------GLID----LLDEDTI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 411 KTRRTGVLvGPDSNPT----LSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLF 486
Cdd:cd17655 123 YHEESENL-EPVSKSDdlayVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 487 LGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRL-QTIAQNVNI 565
Cdd:cd17655 202 SGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIiELFGTNPTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 566 INMYGTTETQRAVSYFEIPSRAqdstfleVQKDIMPAGKGMHNVQLLVVNRHDRSKtcAIGEVGEIYVRAAGLAEQYRGQ 645
Cdd:cd17655 282 TNAYGPTETTVDASIYQYEPET-------DQQVSVPIGKPLGNTRIYILDQYGRPQ--PVGVAGELYIGGEGVARGYLNR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 646 PDLNKEKFVPNWFVspskwveedkkiskdepwrefylgPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEI 725
Cdd:cd17655 353 PELTAEKFVDDPFV------------------------PGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 726 DTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKetpelENFKsssddlddlndpivkslllyrelIKDLKAHLKKTLAS 805
Cdd:cd17655 409 EARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE-----KELP-----------------------VAQLREFLARELPD 460
|
570 580 590
....*....|....*....|....*....|
gi 254566307 806 YAIPTIIVPMAKLPLNPNGKVDKPKLPFPD 835
Cdd:cd17655 461 YMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
251-832 |
1.83e-86 |
|
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: 291.17 E-value: 1.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 251 FSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAT 330
Cdd:cd17651 1 FERQAARTPDAPALV---------AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 331 FSVIDPAYPPARQNVYLQVAKPAgLIVLEKAGVLDQLVEdyikneLSLVSRISNLKIEADGNV-LGGDVDGKDALYdyqq 409
Cdd:cd17651 72 YVPLDPAYPAERLAFMLADAGPV-LVLTHPALAGELAVE------LVAVTLLDQPGAAAGADAePDPALDADDLAY---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 410 fktrrtgvlvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGA 489
Cdd:cd17651 141 -----------------VIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 490 QLLIPTsDDIGT-PGKLAEWMQTYGATVTHLTPAMGQLLSAQAT---KEIPSLHHAFFVGDILTKRDCLRLQTIAQ-NVN 564
Cdd:cd17651 204 TLVLPP-EEVRTdPPALAAWLDEQRISRVFLPTVALRALAEHGRplgVRLAALRYLLTGGEQLVLTEDLREFCAGLpGLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 565 IINMYGTTETQrAVSYFEIPSRAQDSTflevqkDIMPAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRG 644
Cdd:cd17651 283 LHNHYGPTETH-VVTALSLPGDPAAWP------APPPIGRPIDNTRVYVLDAALRP--VPPGVPGELYIGGAGLARGYLN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 645 QPDLNKEKFVPNWFVspskwveedkkiskdepwrefylgPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGE 724
Cdd:cd17651 354 RPELTAERFVPDPFV------------------------PGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 725 IDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAHLKKTLA 804
Cdd:cd17651 410 IEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV--------------------------DAAELRAALATHLP 463
|
570 580
....*....|....*....|....*...
gi 254566307 805 SYAIPTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd17651 464 EYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
51-927 |
3.00e-85 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 305.82 E-value: 3.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 51 KANEPSVTQFTAPLAVFAVLVYRLTGDDDIVI------------LTDSPKKQN-LPfvVRLQVDPSKSFVDVSKQVG--- 114
Cdd:PRK10252 243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAgfifmrrlgsaaLTATGPVLNvLP--LRVHIAAQETLPELATRLAaql 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 115 -----------EQYLESLERA---TPLKDIVTHLKeskqLPNYPPIFRlsfqtakKVQ-QLSTLVEGSTRDLAIFL---- 175
Cdd:PRK10252 321 kkmrrhqrydaEQIVRDSGRAagdEPLFGPVLNIK----VFDYQLDFP-------GVQaQTHTLATGPVNDLELALfpde 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 176 ENNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAPETPIGKISLLTEQQSKLLPDptanldwsgyrgaiqdiFSDNA 255
Cdd:PRK10252 390 HGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQ-----------------VNATA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 256 EKFPDRT--CVVETKSFLNPNSQT-----RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:PRK10252 453 VEIPETTlsALVAQQAAKTPDAPAladarYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAG 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPARQNVYLQVAKPAglIVLEKAGVLDQLvedyiknelslvsrisnlkieADGnvlggdvdGKDALYDYQ 408
Cdd:PRK10252 533 AAWLPLDTGYPDDRLKMMLEDARPS--LLITTADQLPRF---------------------ADV--------PDLTSLCYN 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 409 QFKTR---RTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPL 485
Cdd:PRK10252 582 APLAPqgaAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPF 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 486 FLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAM-----GQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIA 560
Cdd:PRK10252 662 IAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMlaafvASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLT 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 561 qNVNIINMYGTTETQRAVSYFeiPSRAQDSTflEVQKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAE 640
Cdd:PRK10252 742 -GAPLHNLYGPTEAAVDVSWY--PAFGEELA--AVRGSSVPIGYPVWNTGLRILD--ARMRPVPPGVAGDLYLTGIQLAQ 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 641 QYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRI 720
Cdd:PRK10252 815 GYLGRPDLTASRFIADPF------------------------APGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRI 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 721 ELGEIDTHISRHPLIRQNVTL--VRRDKDEEP----ILISYVVPKETPELEnfksssddlddlndpivkslllyrelIKD 794
Cdd:PRK10252 871 ELGEIDRAMQALPDVEQAVTHacVINQAAATGgdarQLVGYLVSQSGLPLD--------------------------TSA 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 795 LKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPD-TVQLAAVAQKssaevddsefTTTELQIKDLWLQVLPNP 873
Cdd:PRK10252 925 LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPElKAQVPGRAPK----------TGTETIIAAAFSSLLGCD 994
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 254566307 874 PASIslEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAEVD 927
Cdd:PRK10252 995 VVDA--DADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-924 |
1.56e-84 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 307.09 E-value: 1.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG--PTLSvLPRDYNRPVAGKVIEANKTFDI----SDILPFLnkANEPSVTQFTAPLAVFAVLVYRLTG 76
Cdd:PRK12467 1302 ARQLAYWKAQLGGeqPVLE-LPTDRPRPAVQSHRGARLAFELppalAEGLRAL--ARREGVTLFMLLLASFQTLLHRYSG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 77 DDDIVI------LTDSPKKQNLPFVVRLQV-----DPSKSFVDVSKQVGEQYLES-LERATPLKDIVTHLKESKQLpNYP 144
Cdd:PRK12467 1379 QDDIRVgvpianRNRAETEGLIGFFVNTQVlraevDGQASFQQLLQQVKQAALEAqAHQDLPFEQLVEALQPERSL-SHS 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 145 PIFRLSF--QTAKKvQQLSTLVEGSTRDLAifLENNT-----SINIY-----------YNSLLYTHNRIAYFSQQFSSFI 206
Cdd:PRK12467 1458 PLFQVMFnhQRDDH-QAQAQLPGLSVESLS--WESQTaqfdlTLDTYesseglqasltYATDLFEASTIERLAGHWLNLL 1534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 207 DEVNKAPETPIGKISLLTE---QQSKLLPDPTANlDWSGYRGaIQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYK 283
Cdd:PRK12467 1535 QGLVADPERRLGELDLLDEaerRQILEGWNATHT-GYPLARL-VHQLIEDQAAATPEAVALV---------FGEQELTYG 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 284 QIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQnvylqvakpagLIVLEKAGV 363
Cdd:PRK12467 1604 ELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERL-----------AYMIEDSGI 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 364 LDQLVEDYIKNELSLVSRISNLKIEADGNVLGGDVDGKDAlydyqqfktrrtgVLVGPDSNPTLSFTSGSEGIPKGVLGR 443
Cdd:PRK12467 1673 ELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYSDSNPA-------------VNLAPQNLAYVIYTSGSTGRPKGAGNR 1739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 444 HFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAM 523
Cdd:PRK12467 1740 HGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSM 1819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 524 GQLL--SAQATKEIPSLHHAFFVGDILtKRDCLRlQTIAQ--NVNIINMYGTTETQRAVSYFeiPSRAQDSTflevQKDI 599
Cdd:PRK12467 1820 LQQLlqMDEQVEHPLSLRRVVCGGEAL-EVEALR-PWLERlpDTGLFNLYGPTETAVDVTHW--TCRRKDLE----GRDS 1891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 600 MPAGKGMHNVQLLVVnrhDRS-KTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPSKwveedkkiskdepwr 678
Cdd:PRK12467 1892 VPIGQPIANLSTYIL---DASlNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGS--------------- 1953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 679 efylgprdRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVrRDKDEEPILISYVVP 758
Cdd:PRK12467 1954 --------RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVP 2024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 759 KETPELENFKSSSDdlddlndpivkslllYRElikDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQ 838
Cdd:PRK12467 2025 TDPGLVDDDEAQVA---------------LRA---ILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASE 2086
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 839 L--AAVAQKSSAevddseftttELQIKDLWLQVLPNPpaSISLEDSFFDLGGHSILATRMIFELRRKlAVDLPLGTIFKH 916
Cdd:PRK12467 2087 LqqAYVAPQSEL----------EQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQH 2153
|
....*...
gi 254566307 917 PTVKLFAA 924
Cdd:PRK12467 2154 QTVQSLAA 2161
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
170-926 |
2.61e-83 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 303.24 E-value: 2.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 170 DLAIFLENNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAPETPIGKISLLT-EQQSKLLPDPTANLDWSGYRGAIQ 248
Cdd:PRK12467 3019 TLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAaHERRQVLHAWNATAAAYPSERLVH 3098
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:PRK12467 3099 QLIEAQVARTPEAPALV---------FGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPARQNVylqvakpagliVLEKAGVldqlvedyiKNELSLVSRISNLKIEADGNVLggDVDGkDALYDYq 408
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAY-----------MIEDSGV---------KLLLTQAHLLEQLPAPAGDTAL--TLDR-LDLNGY- 3225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 409 qfktrrtgvlvgPDSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQ 478
Cdd:PRK12467 3226 ------------SENNPSTRvmgenlayviYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQ 3293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 479 RDMFTPLFLGAQLLIpTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQA-TKEIPSLHHAFFVGDILTKRDCLRLQ 557
Cdd:PRK12467 3294 ERFLWTLICGGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAgGADCASLDIYVFGGEAVPPAAFEQVK 3372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 558 TIAQNVNIINMYGTTETQRAVSYFEIPSRAQdstfleVQKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAG 637
Cdd:PRK12467 3373 RKLKPRGLTNGYGPTEAVVTVTLWKCGGDAV------CEAPYAPIGRPVAGRSIYVLD--GQLNPVPVGVAGELYIGGVG 3444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 638 LAEQYRGQPDLNKEKFVPNWFVSpskwveedkkiskdepwrefyLGprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRG 717
Cdd:PRK12467 3445 LARGYHQRPSLTAERFVADPFSG---------------------SG--GRLYRTGDLARYRADGVIEYLGRIDHQVKIRG 3501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 718 FRIELGEIDTHISRHPLIRQNVTLVrRDKDEEPILISYVVPKETPElenfksssddlddlndpivkslllyrELIKDLKA 797
Cdd:PRK12467 3502 FRIELGEIEARLLQHPSVREAVVLA-RDGAGGKQLVAYVVPADPQG--------------------------DWRETLRD 3554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 798 HLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDT-VQLAAVAQKSSaevddsefttTELQIKDLWLQVLPNPpaS 876
Cdd:PRK12467 3555 HLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAkGSREYVAPRSE----------VEQQLAAIWADVLGVE--Q 3622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 254566307 877 ISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAEV 926
Cdd:PRK12467 3623 VGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS 3672
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
247-831 |
2.63e-83 |
|
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: 281.74 E-value: 2.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVvetksflnpNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:cd05918 1 VHDLIEERARSQPDAPAV---------CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARqnvylqvakpaglivlekagvLDQLVEDyIKNELSLVSRISnlkieadgnvlggdvdgkDALYd 406
Cdd:cd05918 72 AGGAFVPLDPSHPLQR---------------------LQEILQD-TGAKVVLTSSPS------------------DAAY- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 407 yqqfktrrtgVLvgpdsnptlsFTSGSEGIPKGVLGRHFSL---AYYFpwmSKTFNLSENDKFTMLSGIAHDPIQRDMFT 483
Cdd:cd05918 111 ----------VI----------FTSGSTGKPKGVVIEHRALstsALAH---GRALGLTSESRVLQFASYTFDVSILEIFT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 484 PLFLGAQLLIPTSDDIgtPGKLAEWMQTYGATVTHLTPAMGQLLSAQatkEIPSLHHAFFVGDILTKRDclrLQTIAQNV 563
Cdd:cd05918 168 TLAAGGCLCIPSEEDR--LNDLAGFINRLRVTWAFLTPSVARLLDPE---DVPSLRTLVLGGEALTQSD---VDTWADRV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 564 NIINMYGTTETQRAVSYFEIPSRAQDStflevqkDImpaGKGMhNVQLLVVNRHDRSKTCAIGEVGEIYVRAAGLAEQYR 643
Cdd:cd05918 240 RLINAYGPAECTIAATVSPVVPSTDPR-------NI---GRPL-GATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 644 GQPDLNKEKFVPNWfvspsKWveedkkiskdepWREFYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELG 723
Cdd:cd05918 309 NDPEKTAAAFIEDP-----AW------------LKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELG 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 724 EIDTHISRHPLIRQNVT---LVRRDKDEEPILISYVVPKETPElenfksssdDLDDLNDPIVKSLLLYRELIKDLKAHLK 800
Cdd:cd05918 372 EIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSS---------GSGDGDSLFLEPSDEFRALVAELRSKLR 442
|
570 580 590
....*....|....*....|....*....|.
gi 254566307 801 KTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05918 443 QRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-923 |
1.29e-82 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 301.11 E-value: 1.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG--PTLSvLPRDYNRPVAGKVIEANKTFDISDILP--FLNKANEPSVTQFTAPLAVFAVLVYRLTGDD 78
Cdd:PRK12316 237 ERQLEYWRAQLGEehPVLE-LPTDHPRPAVPSYRGSRYEFSIDPALAeaLRGTARRQGLTLFMLLLGAFNVLLHRYSGQT 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 79 DI---VILTDSPKKQN---LPF-----VVRLQVDPSKSFVDVSKQVGEQYLES-LERATPLKDIVTHLKESKQLpNYPPI 146
Cdd:PRK12316 316 DIrvgVPIANRNRAEVeglIGFfvntqVLRSVFDGRTRVATLLAGVKDTVLGAqAHQDLPFERLVEALKVERSL-SHSPL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 147 FRLSFQT------AKKVQQLSTL----VEGSTR----DLAI-FLENNTSIN---IYYNSLLYTHNrIAYFSQQFSSFIDE 208
Cdd:PRK12316 395 FQVMYNHqplvadIEALDTVAGLefgqLEWKSRttqfDLTLdTYEKGGRLHaalTYATDLFEART-VERMARHWQNLLRG 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 209 VNKAPETPIGKISLLT--EQQSKLLPDPTANLDWSGYRGaIQDIFSDNAEKFPDRTCVVETKSflnpnsqtrTFTYKQID 286
Cdd:PRK12316 474 MVENPQARVDELPMLDaeERGQLVEGWNATAAEYPLQRG-VHRLFEEQVERTPEAPALAFGEE---------TLDYAELN 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 287 QASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQnVYLqvakpaglivLEKAGVLDQ 366
Cdd:PRK12316 544 RRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL-AYM----------LEDSGVQLL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 367 LVEDYIKNELSLVSRISNLkieadgnvlggDVDGKDALYDYQQfkTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFS 446
Cdd:PRK12316 613 LSQSHLGRKLPLAAGVQVL-----------DLDRPAAWLEGYS--EENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 447 LAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQ- 525
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQa 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 526 LLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYFeipsraqdsTFLEVQKDIMPAGKG 605
Cdd:PRK12316 760 FLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW---------TCVEEGGDSVPIGRP 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 606 MHNVQLLVVNRHdrSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPskwveedkkiskdepwrefylgpr 685
Cdd:PRK12316 831 IANLACYILDAN--LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAG------------------------ 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 686 DRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDeepiLISYVVPKETPEle 765
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQ----LVGYVVLESEGG-- 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 766 nfksssddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQlaaVAQK 845
Cdd:PRK12316 959 ------------------------DWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV---AQQG 1011
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 846 SSAEVDDSEFTTTElqikdLWLQVLPNPPasISLEDSFFDLGGHSILATRMIFELRRKlAVDLPLGTIFKHPTVKLFA 923
Cdd:PRK12316 1012 YVAPRNALERTLAA-----IWQDVLGVER--VGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLA 1081
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
259-831 |
1.15e-81 |
|
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: 276.11 E-value: 1.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVEtksflnpnsQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd17643 1 PEAVAVVD---------EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARQNVYLQVAKPAGLIVlekagvldqlvedyiknelslvsrisnlkieadgnvlggdvDGKDALYdyqqfktrrtgVL 418
Cdd:cd17643 72 PVERIAFILADSGPSLLLT-----------------------------------------DPDDLAY-----------VI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 vgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDD 498
Cdd:cd17643 100 ----------YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 499 IGTPGKLAEWMQTYGATVTHLTP-AMGQLLSA--QATKEIPSLHHAFFVGDILTKRdclRLQTIAQNVN-----IINMYG 570
Cdd:cd17643 170 ARSPEDFARLLRDEGVTVLNQTPsAFYQLVEAadRDGRDPLALRYVIFGGEALEAA---MLRPWAGRFGldrpqLVNMYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 571 TTETQRAVSYFEIpsRAQDSTflevQKDIMPAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRGQPDLNK 650
Cdd:cd17643 247 ITETTVHVTFRPL--DAADLP----AAAASPIGRPLPGLRVYVLDADGRP--VPPGVVGELYVSGAGVARGYLGRPELTA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 651 EKFVPNWFVspskwveedkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHIS 730
Cdd:cd17643 319 ERFVANPFG-----------------------GPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 731 RHPLIRQNVTLVRRDKDEEPILISYVVPKETPElenfksssddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPT 810
Cdd:cd17643 376 THPSVRDAAVIVREDEPGDTRLVAYVVADDGAA--------------------------ADIAELRALLKELLPDYMVPA 429
|
570 580
....*....|....*....|.
gi 254566307 811 IIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd17643 430 RYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
171-926 |
1.25e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 294.94 E-value: 1.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 171 LAIFLENNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAPETPIGKISLL-TEQQSKLLPDPTANLDWSGYRGAIQD 249
Cdd:PRK12316 1928 LAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLdAGERQRILADWDRTPEAYPRGPGVHQ 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 250 IFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGA 329
Cdd:PRK12316 2008 RIAEQAARAPEAIAVV---------FGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 330 TFSVIDPAYPPARQnVYLQVAKPAGLiVLEKAGVLDQLvedyiknelSLVSRISNLKIEADGnvlggdvdgkdalyDYQQ 409
Cdd:PRK12316 2079 AYVPLDPNYPAERL-AYMLEDSGAAL-LLTQRHLLERL---------PLPAGVARLPLDRDA--------------EWAD 2133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 410 FKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGA 489
Cdd:PRK12316 2134 YPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGA 2213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 490 QLLIpTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKE--IPSLHHAFFVGDILTKRDCLRLQTIAQNVNIIN 567
Cdd:PRK12316 2214 RVLI-RDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFN 2292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 568 MYGTTETQRAVSYFEipSRAQDSTflevQKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPD 647
Cdd:PRK12316 2293 GYGPTEAVVTPLLWK--CRPQDPC----GAAYVPIGRALGNRRAYILD--ADLNLLAPGMAGELYLGGEGLARGYLNRPG 2364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 648 LNKEKFVPNWFVSPSkwveedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDT 727
Cdd:PRK12316 2365 LTAERFVPDPFSASG-----------------------ERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEA 2421
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 728 HISRHPLIRQNVtLVRRDKDEEPILISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAHLKKTLASYA 807
Cdd:PRK12316 2422 RLQAHPAVREAV-VVAQDGASGKQLVAYVVPDDAAED--------------------------LLAELRAWLAARLPAYM 2474
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 808 IPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQL--AAVAQKssaevddsefTTTELQIKDLWLQVLpnPPASISLEDSFFD 885
Cdd:PRK12316 2475 VPAHWVVLERLPLNPNGKLDRKALPKPDVSQLrqAYVAPQ----------EGLEQRLAAIWQAVL--KVEQVGLDDHFFE 2542
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 254566307 886 LGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAEV 926
Cdd:PRK12316 2543 LGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASL 2583
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-930 |
1.16e-79 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 291.69 E-value: 1.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 2 SEENLNYWANILdGPTLSVLPRDYNRPVAGKVIEANKTFDI------SDILPFLNKANEPSVtqFTAPLAVFAVLVYRLT 75
Cdd:PRK05691 862 AARQLAYWKAQL-GDEQPVLELATDHPRSARQAHSAARYSLrvdaslSEALRGLAQAHQATL--FMVLLAAFQALLHRYS 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 76 GDDDIVILTDSPKKQNL-----------PFVVRLQVDPSKSFVDVSKQVGEQYLES-LERATPLKDIVTHLKESKQLPNY 143
Cdd:PRK05691 939 GQGDIRIGVPNANRPRLetqglvgffinTQVLRAQLDGRLPFTALLAQVRQATLGAqAHQDLPFEQLVEALPQAREQGLF 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 144 PPIFRLSFQTAKKVQQLSTLV--------EGSTRDLAIFLEN----NTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNK 211
Cdd:PRK05691 1019 QVMFNHQQRDLSALRRLPGLLaeelpwhsREAKFDLQLHSEEdrngRLTLSFDYAAELFDAATIERLAEHFLALLEQVCE 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 212 APETPIGKISLLTEQQSKLLpdptanLDWSGYRGA-----IQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQID 286
Cdd:PRK05691 1099 DPQRALGDVQLLDAAERAQL------AQWGQAPCApaqawLPELLNEQARQTPERIALV---------WDGGSLDYAELH 1163
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 287 QASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKpAGLIvLEKAGVLDQ 366
Cdd:PRK05691 1164 AQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG-VELL-LTQSHLLER 1241
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 367 LvedyikNELSLVSRISNLKIEADGnvlggdvdgkdalydyqqFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFS 446
Cdd:PRK05691 1242 L------PQAEGVSAIALDSLHLDS------------------WPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA 1297
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 447 LAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQL 526
Cdd:PRK05691 1298 LAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQL 1377
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 527 -----LSAQATkeipSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYFEipSRAQDSTFlevqkdiMP 601
Cdd:PRK05691 1378 fidepLAAACT----SLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQ--CQAEDGER-------SP 1444
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 602 AGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPnwfvspskwveedkkiskdEPWREfy 681
Cdd:PRK05691 1445 IGRPLGNVLCRVLD--AELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP-------------------DPLGE-- 1501
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 682 lgPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKdEEPILISYVVPKET 761
Cdd:PRK05691 1502 --DGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGA-AGAQLVGYYTGEAG 1578
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 762 PELENfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQLAA 841
Cdd:PRK05691 1579 QEAEA--------------------------ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREH 1632
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 842 VAQKssaevddsefTTTELQIKDLWLQVLPNPpaSISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKL 921
Cdd:PRK05691 1633 VEPR----------TELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGA 1700
|
....*....
gi 254566307 922 FAAEVDRVK 930
Cdd:PRK05691 1701 FAEQVARIQ 1709
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
278-831 |
5.50e-79 |
|
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: 269.16 E-value: 5.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAgLIV 357
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPA-LVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 358 LEKAgvldqlvedyiknelslvsrisnlkiEADGNVLGGDVDGKDALYDYQQFKTRRTGVLvgPDSNPTLSFTSGSEGIP 437
Cdd:cd12116 90 TDDA--------------------------LPDRLPAGLPVLLLALAAAAAAPAAPRTPVS--PDDLAYVIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 438 KGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVT 517
Cdd:cd12116 142 KGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 518 HLTPAMGQLLSAQATKEIPSLHhAFFVGDILTKRdcLRLQTIAQNVNIINMYGTTETQravsyfeIPSRAQdstFLEVQK 597
Cdd:cd12116 222 QATPATWRMLLDAGWQGRAGLT-ALCGGEALPPD--LAARLLSRVGSLWNLYGPTETT-------IWSTAA---RVTAAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 598 DIMPAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNwfvspskwveedkkiskdePw 677
Cdd:cd12116 289 GPIPIGRPLANTQVYVLDAALRP--VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPD-------------------P- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 678 refYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDkDEEPILISYVV 757
Cdd:cd12116 347 ---FAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVV 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 758 PKETPELEnfksssddlddlndpivkslllyrelIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd12116 423 LKAGAAPD--------------------------AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
255-831 |
1.22e-78 |
|
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: 267.58 E-value: 1.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 255 AEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVI 334
Cdd:cd05945 1 AAANPDRPAVVEGG---------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 335 DPAYPPARQNVYLQVAKPAGLIVlekagvldqlvedyiknelslvsrisnlkieadgnvlggdvDGKDALYdyqqfktrr 414
Cdd:cd05945 72 DASSPAERIREILDAAKPALLIA-----------------------------------------DGDDNAY--------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 415 tgvlvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIP 494
Cdd:cd05945 102 ------------IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 495 TSDDIGTPGKLAEWMQTYGATVTHLTP---AMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGT 571
Cdd:cd05945 170 PRDATADPKQLFRFLAEHGITVWVSTPsfaAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGP 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 572 TETQRAVSYFEIPSRAQDstflevQKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKE 651
Cdd:cd05945 250 TEATVAVTYIEVTPEVLD------GYDRLPIGYAKPGAKLVILD--EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 652 KFVPnwfvspskwveedkkiskDEPWrefylgprdRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISR 731
Cdd:cd05945 322 AFFP------------------DEGQ---------RAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQ 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 732 HPLIRQNVTLVRRDKDEEPILISYVVPKETPElenfksssddlddlndpivkslllyRELIKDLKAHLKKTLASYAIPTI 811
Cdd:cd05945 375 VPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE-------------------------AGLTKAIKAELAERLPPYMIPRR 429
|
570 580
....*....|....*....|
gi 254566307 812 IVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05945 430 FVYLDELPLNANGKIDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-932 |
6.40e-77 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 283.00 E-value: 6.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 6 LNYWANILDGPTLSV-LPRDYNRPVAGKVIEANKTFDISDIL--PFLNKANEPSVTQFTAPLAVFAVLVYRLTGDDDIVI 82
Cdd:PRK12316 2789 LDYWRERLGGEQPVLeLPLDRPRPALQSHRGARLDVALDVALsrELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRV 2868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 83 ------LTDSPKKQNLPF-----VVRLQVDPSKSFVDVSKQVGEQYLESLE-RATPLKDIVTHLKESKQLpNYPPIFR-- 148
Cdd:PRK12316 2869 gvpianRNRAETERLIGFfvntqVLRAQVDAQLAFRDLLGQVKEQALGAQAhQDLPFEQLVEALQPERSL-SHSPLFQvm 2947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 149 LSFQTAKK---------VQQLSTLVEGSTRDLAIFLE---NNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAPETP 216
Cdd:PRK12316 2948 YNHQSGERaaaqlpglhIESFAWDGAATQFDLALDTWesaEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRS 3027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 217 IGKISLLT-EQQSKLLPDPTANLDWSGYRGAIQDIFSDNAEKFPDRTCVVETKSFLnpnsqtrtfTYKQIDQASNIVGNY 295
Cdd:PRK12316 3028 VDELAMLDaEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRL---------SYAELNRRANRLAHR 3098
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 296 LVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNvylqvakpaglIVLEKAGVLDQLVEDYIKne 375
Cdd:PRK12316 3099 LIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA-----------YMLEDSGAQLLLSQSHLR-- 3165
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 376 LSLVSRISNLKIEADGnvlggdvdgkdalydyQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMS 455
Cdd:PRK12316 3166 LPLAQGVQVLDLDRGD----------------ENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 456 KTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEI 535
Cdd:PRK12316 3230 QAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHR 3309
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 536 PSLHHAFFVGDILTKRDCLrlQTIAQNVNIINMYGTTETQRAVSYFeipsraqdsTFLEVQKDIMPAGKGMHNVQLLVVN 615
Cdd:PRK12316 3310 CTSLKRIVCGGEALPADLQ--QQVFAGLPLYNLYGPTEATITVTHW---------QCVEEGKDAVPIGRPIANRACYILD 3378
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 616 rhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVspskwveedkkiskdepwrefylgPRDRLYRTGDLG 695
Cdd:PRK12316 3379 --GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFV------------------------PGERLYRTGDLA 3432
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 696 RYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLvrrdKDEEPILISYVVPKETPElenfksssddld 775
Cdd:PRK12316 3433 RYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAG------------ 3496
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 776 dlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQLAAVAQKSSAEVddsef 855
Cdd:PRK12316 3497 --------------DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNEL----- 3557
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 856 tttELQIKDLWLQVLPNPpaSISLEDSFFDLGGHSILATRMIFELrRKLAVDLPLGTIFKHPTVKLFaAEVDRVKNG 932
Cdd:PRK12316 3558 ---ERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGL-ARVARVGGG 3627
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
278-832 |
1.46e-72 |
|
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: 249.98 E-value: 1.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARqnvylqvakpagliv 357
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 358 lekagvLDQLVEDyiknelslvSRISNLKIEadgnvlggdvDGKDALYdyqqfktrrtgvlvgpdsnptLSFTSGSEGIP 437
Cdd:cd17649 76 ------LRYMLED---------SGAGLLLTH----------HPRQLAY---------------------VIYTSGSTGTP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 438 KGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVT 517
Cdd:cd17649 110 KGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 518 HLTPAMGQLLSAQATKEI----PSLHHAFFVGDILTKRDCLRLQTIAqnVNIINMYGTTETQRAVSYFEIPSRAQDstfl 593
Cdd:cd17649 190 DLPPAYLQQLAEEADRTGdgrpPSLRLYIFGGEALSPELLRRWLKAP--VRLFNAYGPTEATVTPLVWKCEAGAAR---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 594 evQKDIMPAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkisk 673
Cdd:cd17649 264 --AGASMPIGRPLGGRSAYILDADLNP--VPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF--------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 674 depwrefyLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQnVTLVRRDKDEEPILI 753
Cdd:cd17649 325 --------GAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVRE-AAVVALDGAGGKQLV 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 754 SYVVPKETPELEnfksssddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd17649 396 AYVVLRAAAAQP------------------------ELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
247-832 |
1.05e-70 |
|
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: 245.04 E-value: 1.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVETKSFLnpnsqtrtfTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQL---------TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARQNVYLQvakPAGLIVLekagvldqlvedyiknelslVSRISNLkieadgnvlggdvdgkdaLYd 406
Cdd:cd17644 73 AGGAYVPLDPNYPQERLTYILE---DAQISVL--------------------LTQPENL------------------AY- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 407 yqqfktrrtgvlvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLF 486
Cdd:cd17644 111 --------------------VIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 487 LGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKE-IPSLHHAFFV---GD-ILTKRDCLRLQTIAQ 561
Cdd:cd17644 171 SGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStIDLPSSLRLVivgGEaVQPELVRQWQKNVGN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 562 NVNIINMYGTTETQRAVSYFEIpsraqdSTFLEVQKDIMPAGKGMHNVQLLVVNRHdrSKTCAIGEVGEIYVRAAGLAEQ 641
Cdd:cd17644 251 FIQLINVYGPTEATIAATVCRL------TQLTERNITSVPIGRPIANTQVYILDEN--LQPVPVGVPGELHIGGVGLARG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 642 YRGQPDLNKEKFVPNWFVSpskwveedkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIE 721
Cdd:cd17644 323 YLNRPELTAEKFISHPFNS----------------------SESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIE 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 722 LGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAHLKK 801
Cdd:cd17644 381 LGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESP--------------------------STVELRQFLKA 434
|
570 580 590
....*....|....*....|....*....|.
gi 254566307 802 TLASYAIPTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd17644 435 KLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
277-831 |
4.24e-70 |
|
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: 242.76 E-value: 4.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 277 TRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVylqvakpagli 356
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 357 VLEKAGVldqlvedyiknelslvsrisnlkieadgnvlggDVdgkdalydyqqfktrrtgVLVGPDSNPTLSFTSGSEGI 436
Cdd:cd17650 79 MLEDSGA---------------------------------KL------------------LLTQPEDLAYVIYTSGTTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 437 PKGVLGRHFSLAY-YFPWmSKTFNLsenDKFTM----LSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWMQT 511
Cdd:cd17650 108 PKGVMVEHRNVAHaAHAW-RREYEL---DSFPVrllqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 512 YGATVTHLTPA--MGQLLSAQATKEIPSLHHAFFVG-DILTKRDCLRL-QTIAQNVNIINMYGTTETQRAVSYFEIP-SR 586
Cdd:cd17650 184 SRITLMESTPAliRPVMAYVYRNGLDLSAMRLLIVGsDGCKAQDFKTLaARFGQGMRIINSYGVTEATIDSTYYEEGrDP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 587 AQDSTFLevqkdimPAGKGMHNVQLLVVNRHDRSKtcAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwve 666
Cdd:cd17650 264 LGDSANV-------PIGRPLPNTAMYVLDERLQPQ--PVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 667 edkkiskdepwrefylGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDK 746
Cdd:cd17650 327 ----------------APGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 747 DEEPILISYVVPKETPELenfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKV 826
Cdd:cd17650 391 GGEARLCAYVVAAATLNT----------------------------AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 254566307 827 DKPKL 831
Cdd:cd17650 443 DRRAL 447
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
259-828 |
2.59e-69 |
|
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: 241.41 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd12114 1 PDATAVICGD---------GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARQNvYLQVAKPAGLIVLEkaGVLDQLVEDyikneLSLVSRISNLKIEADGNVLGGDVDGKDALYdyqqfktrrtgVL 418
Cdd:cd12114 72 PAARRE-AILADAGARLVLTD--GPDAQLDVA-----VFDVLILDLDALAAPAPPPPVDVAPDDLAY-----------VI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 vgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDD 498
Cdd:cd12114 133 ----------FTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 499 IGTPGKLAEWMQTYGATVTHLTPAMGQLL---SAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETq 575
Cdd:cd12114 203 RRDPAHWAELIERHGVTLWNSVPALLEMLldvLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEA- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 576 ravsyfeipsrAQDSTFLEVQKDIM-----PAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRGQPDLNK 650
Cdd:cd12114 282 -----------SIWSIYHPIDEVPPdwrsiPYGRPLANQRYRVLDPRGRD--CPDWVPGELWIGGRGVALGYLGDPELTA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 651 EKFVPnwfvspskwveedkkiskdepwrefyLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHIS 730
Cdd:cd12114 349 ARFVT--------------------------HPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQ 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 731 RHPLIRQNVTLVRRDkDEEPILISYVVPKETPElenfksssddlddlndPIVKslllyreliKDLKAHLKKTLASYAIPT 810
Cdd:cd12114 403 AHPGVARAVVVVLGD-PGGKRLAAFVVPDNDGT----------------PIAP---------DALRAFLAQTLPAYMIPS 456
|
570
....*....|....*...
gi 254566307 811 IIVPMAKLPLNPNGKVDK 828
Cdd:cd12114 457 RVIALEALPLTANGKVDR 474
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
247-831 |
1.11e-68 |
|
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: 238.94 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVEtksflnpnsQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF---------GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARQNVYLQVAKPAGLIVLekagvldqlvedyiknelslvsrisnlkieadgnvlggdvdgkdalyd 406
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVTA------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 407 yqqfktrrtgvlvgpdsnpTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHD-PIQRDMFTPL 485
Cdd:COG0318 104 -------------------LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 486 FLGAQLLIPTSDDigtPGKLAEWMQTYGATVTHLTPAMGQLLSAQ---ATKEIPSLHHAFFVGDILTKRDCLRLQTIAqN 562
Cdd:COG0318 165 LAGATLVLLPRFD---PERVLELIERERVTVLFGVPTMLARLLRHpefARYDLSSLRLVVSGGAPLPPELLERFEERF-G 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 563 VNIINMYGTTETQRAVSYfeIPSRAQDSTFLEVqkdimpaGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQY 642
Cdd:COG0318 241 VRIVEGYGLTETSPVVTV--NPEDPGERRPGSV-------GRPLPGVEVRIVDEDGR--ELPPGEVGEIVVRGPNVMKGY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 643 RGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIEL 722
Cdd:COG0318 310 WNDPEATAEAFRDGWL-------------------------------RTGDLGRLDEDGYLYIVGRKKDMIISGGENVYP 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 723 GEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELEnfksssddlddlndpivkslllyrelIKDLKAHLKKT 802
Cdd:COG0318 359 AEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD--------------------------AEELRAFLRER 412
|
570 580
....*....|....*....|....*....
gi 254566307 803 LASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:COG0318 413 LARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
259-832 |
5.82e-68 |
|
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: 236.38 E-value: 5.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd17652 1 PDAPAVV---------FGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARQNVYLQVAKPAglIVLEKAGvldqlvedyiknelslvsrisnlkieadgnvlggdvdgkDALYdyqqfktrrtgVL 418
Cdd:cd17652 72 PAERIAYMLADARPA--LLLTTPD---------------------------------------NLAY-----------VI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 vgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDD 498
Cdd:cd17652 100 ----------YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 499 IGTPGKLAEWMQTYGATVTHLTPAmgqLLSAQATKEIPSLHHAFFVGDILTKRdclRLQTIAQNVNIINMYGTTETQRAV 578
Cdd:cd17652 170 LLPGEPLADLLREHRITHVTLPPA---ALAALPPDDLPDLRTLVVAGEACPAE---LVDRWAPGRRMINAYGPTETTVCA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 579 SYFEIPSRAqdstflevqkDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWF 658
Cdd:cd17652 244 TMAGPLPGG----------GVPPIGRPVPGTRVYVLD--ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 659 VSPSkwveedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQN 738
Cdd:cd17652 312 GAPG-----------------------SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 739 VTLVRRDKDEEPILISYVVPKETPelenfksssddlddlnDPIVkslllyreliKDLKAHLKKTLASYAIPTIIVPMAKL 818
Cdd:cd17652 369 VVVVRDDRPGDKRLVAYVVPAPGA----------------APTA----------AELRAHLAERLPGYMVPAAFVVLDAL 422
|
570
....*....|....
gi 254566307 819 PLNPNGKVDKPKLP 832
Cdd:cd17652 423 PLTPNGKLDRRALP 436
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
250-832 |
9.43e-68 |
|
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: 235.91 E-value: 9.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 250 IFSDNAEKFPDRTCVVEtksflnpnsQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGA 329
Cdd:cd17645 3 LFEEQVERTPDHVAVVD---------RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 330 TFSVIDPAYPPARQNVYLQvakpaglivlekagvlDQLVEDYIKNELSLVSRIsnlkieadgnvlggdvdgkdalydyqq 409
Cdd:cd17645 74 AYVPIDPDYPGERIAYMLA----------------DSSAKILLTNPDDLAYVI--------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 410 fktrrtgvlvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGA 489
Cdd:cd17645 111 -------------------YTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 490 QLLIPTSDDIGTPGKLAEWMQTYGATVTHL-TPAMGQLLSAQATkeipSLHHAFFVGDILTKrdclrlqTIAQNVNIINM 568
Cdd:cd17645 172 ALHVVPSERRLDLDALNDYFNQEGITISFLpTGAAEQFMQLDNQ----SLRVLLTGGDKLKK-------IERKGYKLVNN 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 569 YGTTETQRAVSYFEIPSRAQDstflevqkdiMPAGKGMHNVQLLVVNRHDrsKTCAIGEVGEIYVRAAGLAEQYRGQPDL 648
Cdd:cd17645 241 YGPTENTVVATSFEIDKPYAN----------IPIGKPIDNTRVYILDEAL--QLQPIGVAGELCIAGEGLARGYLNRPEL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 649 NKEKFVPNWFVspskwveedkkiskdepwrefylgPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTH 728
Cdd:cd17645 309 TAEKFIVHPFV------------------------PGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPF 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 729 ISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASYAI 808
Cdd:cd17645 365 LMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHE----------------------------ELREWLKNDLPDYMI 416
|
570 580
....*....|....*....|....
gi 254566307 809 PTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd17645 417 PTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
247-831 |
1.11e-67 |
|
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: 235.67 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:cd12115 1 LHDLVEAQAARTPDAIALV---------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARQNVylqvakpagliVLEKAGVLdqlvedyiknelslvsrisnlkieadgnvlggdvdgkdalyd 406
Cdd:cd12115 72 AGAAYVPLDPAYPPERLRF-----------ILEDAQAR------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 407 yqqfktrrtGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSEndkftmLSGI-AHDPIQRD----- 480
Cdd:cd12115 99 ---------LVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE------LAGVlASTSICFDlsvfe 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 481 MFTPLFLGAQLlIPTSDDIGTPGKLAEWMQTYGATVthltP-AMGQLLSAQAtkeIP-SLHHAFFVGDILTKRDCLRLQT 558
Cdd:cd12115 164 LFGPLATGGKV-VLADNVLALPDLPAAAEVTLINTV----PsAAAELLRHDA---LPaSVRVVNLAGEPLPRDLVQRLYA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 559 IAQNVNIINMYGTTETQRAVSYFEIPSRAQDSTflevqkdimPAGKGMHNVQLLVVNRHDRSKtcAIGEVGEIYVRAAGL 638
Cdd:cd12115 236 RLQVERVVNLYGPSEDTTYSTVAPVPPGASGEV---------SIGRPLANTQAYVLDRALQPV--PLGVPGELYIGGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 639 AEQYRGQPDLNKEKFVPNWFVSPSkwveedkkiskdepwrefylgprdRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGF 718
Cdd:cd12115 305 ARGYLGRPGLTAERFLPDPFGPGA------------------------RLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 719 RIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAH 798
Cdd:cd12115 361 RIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG--------------------------LVEDLRRH 414
|
570 580 590
....*....|....*....|....*....|...
gi 254566307 799 LKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd12115 415 LGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
251-716 |
1.29e-67 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 234.51 E-value: 1.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 251 FSDNAEKFPDRTCVVetksflnpNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAT 330
Cdd:pfam00501 1 LERQAARTPDKTALE--------VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 331 FSVIDPAYPPARQNVYLQVAKPAGLIVLEkagvlDQLVEDYIKNELSLVSRISNLKIEADGNVLGGDVDGKDALYDyqqf 410
Cdd:pfam00501 73 YVPLNPRLPAEELAYILEDSGAKVLITDD-----ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAD---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 411 KTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAY----YFPWMSKTFNLSENDKFTMLSGIAHD-PIQRDMFTPL 485
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDfGLSLGLLGPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 486 FLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEI---PSLHHAFFVGDILTKRDCLRLQTIAQN 562
Cdd:pfam00501 224 LAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRallSSLRLVLSGGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 563 VnIINMYGTTETQRAVSYFEIPSRAQDStflevqkdIMPAGKGMHNVQLLVVNRHDRsKTCAIGEVGEIYVRAAGLAEQY 642
Cdd:pfam00501 304 A-LVNGYGLTETTGVVTTPLPLDEDLRS--------LGSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCVRGPGVMKGY 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 643 RGQPDLNKEKFVPnwfvspskwveedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIR 716
Cdd:pfam00501 374 LNDPELTAEAFDE------------------------------DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
259-832 |
2.82e-61 |
|
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: 218.11 E-value: 2.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVEtksflnpnsQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd17656 2 PDAVAVVF---------ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARQNVYLqvAKPAGLIVLEKAGVLDQLVEDYIKN--ELSLVSRI--SNLKIEADGNvlggdvdgkDALYdyqqfktrr 414
Cdd:cd17656 73 PEERRIYIM--LDSGVRVVLTQRHLKSKLSFNKSTIllEDPSISQEdtSNIDYINNSD---------DLLY--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 415 tgvlvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIP 494
Cdd:cd17656 133 ------------IIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 495 TSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSA--QATKEIPS-LHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGT 571
Cdd:cd17656 201 REETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSerEFINRFPTcVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 572 TETQRAVSY-----FEIPsraqdstflevqkDIMPAGKGMHNVQLLVVNRHDRSKTCaiGEVGEIYVRAAGLAEQYRGQP 646
Cdd:cd17656 281 SETHVVTTYtinpeAEIP-------------ELPPIGKPISNTWIYILDQEQQLQPQ--GIVGELYISGASVARGYLNRQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 647 DLNKEKFVPNwfvspskwveedkkiskdePWRefylgPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEID 726
Cdd:cd17656 346 ELTAEKFFPD-------------------PFD-----PNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 727 THISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPElenfksssddlddlndpivkslllyrelIKDLKAHLKKTLASY 806
Cdd:cd17656 402 AQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN----------------------------ISQLREYLAKQLPEY 453
|
570 580
....*....|....*....|....*.
gi 254566307 807 AIPTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd17656 454 MIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
259-832 |
6.43e-58 |
|
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: 207.64 E-value: 6.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGD-VVMIYAYRGVDLMVAVMGVLKAGATFSVIDPA 337
Cdd:cd17648 1 PDRVAVV---------YGDKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 338 YPPARQNVYLQVAKPAGLIVlekagvldqlvedyiknelslvsrisnlkieadgnvlggdvDGKDALYdyqqfktrrtgv 417
Cdd:cd17648 72 YPDERIQFILEDTGARVVIT-----------------------------------------NSTDLAY------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 418 lvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTML--SGIAHDPIQRDMFTPLFLGAQLLIPT 495
Cdd:cd17648 99 ---------AIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQKLVVPP 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 496 SDDIGTPGKLAEWMQTYGATVTHLTPAmgqLLSAQATKEIPSLHHAFFVGDILTKR--DCLRLQTIAQnvnIINMYGTTE 573
Cdd:cd17648 170 DEMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDLARLPHLKRVDAAGEEFTAPvfEKLRSRFAGL---IINAYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 574 TQ--RAVSYFEIPSRAQDSTflevqkdimpaGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKE 651
Cdd:cd17648 244 TTvtNHKRFFPGDQRFDKSL-----------GRPVRNTKCYVLN--DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 652 KFVPNWFVSPSkwveedkkiskdepwrEFYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISR 731
Cdd:cd17648 311 RFLPNPFQTEQ----------------ERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALAS 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 732 HPLIRQNVTLVRRDKDEEPILI-SYVVPKETPELENFKSSsddlddlndpivkslllyrelikDLKAHLKKTLASYAIPT 810
Cdd:cd17648 375 YPGVRECAVVAKEDASQAQSRIqKYLVGYYLPEPGHVPES-----------------------DLLSFLRAKLPRYMVPA 431
|
570 580
....*....|....*....|..
gi 254566307 811 IIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd17648 432 RLVRLEGIPVTINGKLDVRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-929 |
1.15e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 221.20 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANIL--DGPTLSvLPRDYNRP-VAGKVIEANKtFDISDILPFLNKA--NEPSVTQFTAPLAVFAVLVYRLTGD 77
Cdd:PRK05691 1916 QRQLDYWKAQLgnEHPLLE-LPADRPRPpVQSHRGELYR-FDLSPELAARVRAfnAQRGLTLFMTMTATLAALLYRYSGQ 1993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 78 DDIVILTD-----SPKKQNL--PF----VVRLQVDPSKSFVDVSKQVGEQYLESLERatplKDI-VTHLKESKQLPN--- 142
Cdd:PRK05691 1994 RDLRIGAPvanriRPESEGLigAFlntqVLRCQLDGQMSVSELLEQVRQTVIEGQSH----QDLpFDHLVEALQPPRsaa 2069
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 143 YPPIF-------RLSFQTAKK-----VQQLSTLVEGSTRDLAIF---LENNTSINIYYNSLLYTHNRIAYFSQQFSSFID 207
Cdd:PRK05691 2070 YNPLFqvmcnvqRWEFQQSRQlagmtVEYLVNDARATKFDLNLEvtdLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLE 2149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 208 EVNKAPETPIGKISLLTEQQSKLLPDP------TANLDwsgyrGAIQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFT 281
Cdd:PRK05691 2150 ALLGDPQQRLAELPLLAAAEQQQLLDSlageagEARLD-----QTLHGLFAAQAARTPQAPALT---------FAGQTLS 2215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 282 YKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNvYLQVAKPAGLIvLEKA 361
Cdd:PRK05691 2216 YAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH-YMIEDSGIGLL-LSDR 2293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 362 GVLDQLVEdyiknelsLVSRISNLKIEADGNVLGGDVDGKDALydyqqfktrrtgvLVGPDSNPTLSFTSGSEGIPKGVL 441
Cdd:PRK05691 2294 ALFEALGE--------LPAGVARWCLEDDAAALAAYSDAPLPF-------------LSLPQHQAYLIYTSGSTGKPKGVV 2352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 442 GRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPgKLAEWMQTYGATVTHLTP 521
Cdd:PRK05691 2353 VSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAE-EICQLIREQQVSILGFTP 2431
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 522 AMG-QLLSAQATK-EIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETqravSYFEIPSRAQDStfLEVQKDI 599
Cdd:PRK05691 2432 SYGsQLAQWLAGQgEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTET----VVMPLACLAPEQ--LEEGAAS 2505
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 600 MPAGKgmhnvqllVVNrhdrSKTCAI----------GEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPSkwveedk 669
Cdd:PRK05691 2506 VPIGR--------VVG----ARVAYIldadlalvpqGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADG------- 2566
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 670 kiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVrRDKDEE 749
Cdd:PRK05691 2567 ----------------GRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA-LDTPSG 2629
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 750 PILISYVVPKETPELENFKSssddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKP 829
Cdd:PRK05691 2630 KQLAGYLVSAVAGQDDEAQA--------------------ALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 830 KLPFPDTVQLAAVAQKSSAEVddseftttELQIKDLWLQVLpnPPASISLEDSFFDLGGHSILATRMIfELRRKLAVDLP 909
Cdd:PRK05691 2690 ALPAPDPELNRQAYQAPRSEL--------EQQLAQIWREVL--NVERVGLGDNFFELGGDSILSIQVV-SRARQLGIHFS 2758
|
970 980
....*....|....*....|
gi 254566307 910 LGTIFKHPTVKLFAAEVDRV 929
Cdd:PRK05691 2759 PRDLFQHQTVQTLAAVATHS 2778
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
249-831 |
1.90e-57 |
|
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: 205.62 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVvetksflnpNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:cd17653 1 DAFERIAAAHPDAVAV---------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPARQNvylqvakpaglIVLEKAGvldqlvedyiknelslvsriSNLKIEADGnvlggdvdgkdalydyq 408
Cdd:cd17653 72 AAYVPLDAKLPSARIQ-----------AILRTSG--------------------ATLLLTTDS----------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 409 qfktrrtgvlvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLG 488
Cdd:cd17653 104 ------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 489 AQLLIPTSDDigtpgKLAEWMQTygATVTHLTPAMGQLLSAQatkEIPSLHHAFFVGDILTKRdclRLQTIAQNVNIINM 568
Cdd:cd17653 172 GTLVLADPSD-----PFAHVART--VDALMSTPSILSTLSPQ---DFPNLKTIFLGGEAVPPS---LLDRWSPGRRLYNA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 569 YGTTETQRAVSYFEIPSRAQdstflevqkdiMPAGKGMHNVQLLVVNRHDRSKTcaIGEVGEIYVRAAGLAEQYRGQPDL 648
Cdd:cd17653 239 YGPTECTISSTMTELLPGQP-----------VTIGKPIPNSTCYILDADLQPVP--EGVVGEICISGVQVARGYLGNPAL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 649 NKEKFVPNWFVSPSkwveedkkiskdepwrefylgprdRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTH 728
Cdd:cd17653 306 TASKFVPDPFWPGS------------------------RMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 729 ISR-HPLIRQNVTLVRRDKdeepiLISYVVPkETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASYA 807
Cdd:cd17653 362 VLQsQPEVTQAAAIVVNGR-----LVAFVTP-ETVDVD----------------------------GLRSELAKHLPSYA 407
|
570 580
....*....|....*....|....
gi 254566307 808 IPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd17653 408 VPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
278-927 |
2.06e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 220.04 E-value: 2.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKpAGLIV 357
Cdd:PRK05691 3744 QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSR-TPVLV 3822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 358 LEKAgVLDQLVEdyIKNELSLVSRISNLKIEadgNVLGGDVdgkdalydyqqfKTRRTGVLVGPDSNPTLSFTSGSEGIP 437
Cdd:PRK05691 3823 CSAA-CREQARA--LLDELGCANRPRLLVWE---EVQAGEV------------ASHNPGIYSGPDNLAYVIYTSGSTGLP 3884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 438 KGV-------LGRHFSLAYYFpwmsktfNLSENDKFTMLSGIAHD-PIQRDMFTPLFlGAQLLIPTSDDIGTPGKLAEWM 509
Cdd:PRK05691 3885 KGVmveqrgmLNNQLSKVPYL-------ALSEADVIAQTASQSFDiSVWQFLAAPLF-GARVEIVPNAIAHDPQGLLAHV 3956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 510 QTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDI----LTKRDCLRLQTIAqnvnIINMYGTTETQRAVSYFEIPS 585
Cdd:PRK05691 3957 QAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAmppeLARQWLQRYPQIG----LVNAYGPAECSDDVAFFRVDL 4032
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 586 RAQDSTFLevqkdimPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSPSkwv 665
Cdd:PRK05691 4033 ASTRGSYL-------PIGSPTDNNRLYLLD--EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPG--- 4100
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 666 eedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVrRD 745
Cdd:PRK05691 4101 --------------------ERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV-QE 4159
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 746 KDEEPILISYVVPKETPELENfksssddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGK 825
Cdd:PRK05691 4160 GVNGKHLVGYLVPHQTVLAQG-----------------------ALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGK 4216
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 826 VDKPKLPFPDTVQLAAVAQKSSAevddsefTTTELQIKDLWLQVLpnPPASISLEDSFFDLGGHSILATRMIFELRRKLA 905
Cdd:PRK05691 4217 LDRKALPALDIGQLQSQAYLAPR-------NELEQTLATIWADVL--KVERVGVHDNFFELGGHSLLATQIASRVQKALQ 4287
|
650 660
....*....|....*....|..
gi 254566307 906 VDLPLGTIFKHPTVKLFAAEVD 927
Cdd:PRK05691 4288 RNVPLRAMFECSTVEELAEYIE 4309
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
429-827 |
7.94e-49 |
|
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: 177.48 E-value: 7.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 429 FTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDigtPGKLAEW 508
Cdd:cd04433 7 YTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PEAALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 509 MQTYGATVTHLTPAMGQLLSAQATKE---IPSLHHAFFVGDILTKRDCLRLQTiAQNVNIINMYGTTETQRAVSYfeips 585
Cdd:cd04433 84 IEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVAT----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 586 raqdSTFLEVQKDIMPAGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWfvspskwv 665
Cdd:cd04433 158 ----GPPDDDARKPGSVGRPVPGVEVRIVDPDGG--ELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGW-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 666 eedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRD 745
Cdd:cd04433 224 -----------------------YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 746 KDEEPILISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGK 825
Cdd:cd04433 281 PEWGERVVAVVVLRPGADL--------------------------DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
..
gi 254566307 826 VD 827
Cdd:cd04433 335 ID 336
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
247-831 |
2.52e-46 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 175.08 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFsDNAEKFPDRTCVvetksflnpNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:PRK04813 5 IETIE-EFAQTQPDFPAY---------DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARQNVYLQVAKPAGLIVLEKAGVLDQLVEdyiknelslVSRISNLKieadgnvlggDVDGKDALYD 406
Cdd:PRK04813 75 AGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIP---------VITLDELK----------DIFATGNPYD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 407 YQQFktrrtgvlVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFtmlsgIAHDPIQRDM----- 481
Cdd:PRK04813 136 FDHA--------VKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQF-----LNQAPYSFDLsvmdl 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 482 FTPLFLGAQLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPA---MGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQT 558
Cdd:PRK04813 203 YPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSfadMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 559 IAQNVNIINMYGTTETQRAVSYFEIPsraqdstfLEV--QKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAA 636
Cdd:PRK04813 283 RFPSATIYNTYGPTEATVAVTSIEIT--------DEMldQYKRLPIGYAKPDSPLLIID--EEGTKLPDGEQGEIVISGP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 637 GLAEQYRGQPDLNKEKFVpnwfvspskwvEEDKKiskdepwrefylgprdRLYRTGDLGrYLPTGDCEVSGRADDQVKIR 716
Cdd:PRK04813 353 SVSKGYLNNPEKTAEAFF-----------TFDGQ----------------PAYHTGDAG-YLEDGLLFYQGRIDFQIKLN 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 717 GFRIELGEIDTHISRHPLIRQNVTlVRRDKDEEPI-LISYVVPKETPELENFksssddlddlndpivkslllyrELIKDL 795
Cdd:PRK04813 405 GYRIELEEIEQNLRQSSYVESAVV-VPYNKDHKVQyLIAYVVPKEEDFEREF----------------------ELTKAI 461
|
570 580 590
....*....|....*....|....*....|....*.
gi 254566307 796 KAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK04813 462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
986-1280 |
1.12e-40 |
|
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: 152.52 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERDldVQVYAHVRAKDEESGLERLRNTGKvygiwneeWTSRIKVVIADLSKDKLGLSGEKY 1065
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLENG--FKVLVLVRSESLGEAHERIEEAGL--------EADRVRVLEGDLTQPNLGLSAAAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1066 AELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTstldtehYITLsdtlteQGEDGIPE 1145
Cdd:cd05263 71 RELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTA-------YVAG------NREGNIRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1146 SDDLLGssKGLGTGYGQSKWAAEYIIRRAFERgLRGAIIRPGYVTGHSRTGACNTDDFLLRMLKGCAELGKLP----NIS 1221
Cdd:cd05263 138 TELNPG--QNFKNPYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRWLpmpgNKG 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254566307 1222 NTVNMVPVDHVALVVTASSLHPTAEEG--HCVVQVTGHPRIRFNEFLNALNDYGYEVKLTD 1280
Cdd:cd05263 215 ARLNLVPVDYVADAIVYLSKKPEANGQifHLTDPTPQTLREIADLFKSAFLSPGLLVLLMN 275
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
249-826 |
7.22e-33 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 135.62 E-value: 7.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVetksFLNPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:COG0365 13 NCLDRHAEGRGDKVALI----WEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPA----RqnvyLQVAKPAGLI----------VLEKAGVLDQLVEDYIKNELSLVSRISNLKIEADGNVL 394
Cdd:COG0365 89 AVHSPVFPGFGAEaladR----IEDAEAKVLItadgglrggkVIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 395 GGD-VDGKDALYDYQQfkTRRTGVLVgpdsnptLSFTSGSEGIPKGVLGRHfslAYYFPWMSKT----FNLSENDKF--- 466
Cdd:COG0365 165 WDElLAAASAEFEPEP--TDADDPLF-------ILYTSGTTGKPKGVVHTH---GGYLVHAATTakyvLDLKPGDVFwct 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 467 ------TMLSGIahdpiqrdMFTPLFLGA-QLLIPTSDDIGTPGKLAEWMQTYGATVTHLTPA-----MGQLLSAQATKE 534
Cdd:COG0365 233 adigwaTGHSYI--------VYGPLLNGAtVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTairalMKAGDEPLKKYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 535 IPSLHHAFFVGDILTKrdclrlQTIAQ-----NVNIINMYGTTETqraVSYFeipsraqdSTFLevqkDIMP-----AGK 604
Cdd:COG0365 305 LSSLRLLGSAGEPLNP------EVWEWwyeavGVPIVDGWGQTET---GGIF--------ISNL----PGLPvkpgsMGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 605 GM--HNVQllVVNrhDRSKTCAIGEVGEIYVRAA--GLAEQYRGQPdlnkEKFvpnwfvspskwveedkkiskdepwREF 680
Cdd:COG0365 364 PVpgYDVA--VVD--EDGNPVPPGEEGELVIKGPwpGMFRGYWNDP----ERY------------------------RET 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 681 YLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQN-VTLVR-RDKDEEPILisYVVP 758
Cdd:COG0365 412 YFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAaVVGVPdEIRGQVVKA--FVVL 489
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 759 KETPELENfksssddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKV 826
Cdd:COG0365 490 KPGVEPSD-----------------------ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
985-1272 |
9.21e-32 |
|
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: 127.41 E-value: 9.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQ-VYAHVRAKDEESGLERLRNTGKVYGIW-----NEEWTSRIKVVIADLSKDKL 1058
Cdd:cd05236 2 SVLITGATGFLGKVLLEKLLRSCPDIGkIYLLIRGKSGQSAEERLRELLKDKLFDrgrnlNPLFESKIVPIEGDLSEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1059 GLSGEKYAELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKP-KQFGFVSST-----STLDTEHYITLS 1132
Cdd:cd05236 82 GLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKlKAFVHVSTAyvngdRQLIEEKVYPPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1133 DTLTEQGEDGIPeSDDLLGSSKGLGTGYGQ------SKWAAEYIIRRAFErGLRGAIIRPGYVTGHSR------TGACNT 1200
Cdd:cd05236 162 ADPEKLIDILEL-MDDLELERATPKLLGGHpntytfTKALAERLVLKERG-NLPLVIVRPSIVGATLKepfpgwIDNFNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1201 DDfllRMLKGCAeLGKLPNISNTVNM----VPVDHVA--LVVTA--SSLHPTAEegHCVVQVTGHPR--IRFNEFLNALN 1270
Cdd:cd05236 240 PD---GLFLAYG-KGILRTMNADPNAvadiIPVDVVAnaLLAAAaySGVRKPRE--LEVYHCGSSDVnpFTWGEAEELIN 313
|
..
gi 254566307 1271 DY 1272
Cdd:cd05236 314 QY 315
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
277-826 |
1.42e-31 |
|
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: 130.41 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 277 TRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLI 356
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 357 VLEKagVLDQLVEdyIKNELSLVSRISNLKIEADGNVLGGDVDgkdALYDYQQFKTRRTGVLVGPDSNPTLSFTSGSEGI 436
Cdd:cd05911 88 TDPD--GLEKVKE--AAKELGPKDKIIVLDDKPDGVLSIEDLL---SPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 437 PKGVL--GRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAH---DPIqrdMFTPLFLGAQLLIPTSDDIgtpgklAEWMQT 511
Cdd:cd05911 161 PKGVClsHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHiygLFT---TLASLLNGATVIIMPKFDS------ELFLDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 512 ---YGATVTHLTPAMGQLL--SAQATKE-IPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYfeIPs 585
Cdd:cd05911 232 iekYKITFLYLVPPIAAALakSPLLDKYdLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV--NP- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 586 raqdstflEVQKDIMPAGKGMHNVQLLVVNrHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVP-NWFvspskw 664
Cdd:cd05911 309 --------DGDDKPGSVGRLLPNVEAKIVD-DDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEdGWL------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 665 veedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIrQNVTLV-- 742
Cdd:cd05911 374 -------------------------HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGV-ADAAVIgi 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 743 -RRDKDEEPilISYVVPKETPELENfksssddlddlndpivkslllyreliKDLKAHLKKTLASY-----AIptIIVPma 816
Cdd:cd05911 428 pDEVSGELP--RAYVVRKPGEKLTE--------------------------KEVKDYVAKKVASYkqlrgGV--VFVD-- 475
|
570
....*....|
gi 254566307 817 KLPLNPNGKV 826
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
254-828 |
1.00e-30 |
|
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: 126.96 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 254 NAEKFPDRTCVVEtksflnPNsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSV 333
Cdd:cd17631 4 RARRHPDRTALVF------GG---RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 334 IdpaypPARqnvylqvakpaglivLEKAGVLDQLvedyiknelslvsrisnlkieadgnvlggdvdgKDAlydyqqfktr 413
Cdd:cd17631 75 L-----NFR---------------LTPPEVAYIL---------------------------------ADS---------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 414 RTGVLVgpDSNPTLSFTSGSEGIPKGVLGRHFSLAYYfpwmsktfnlsendkfTMLSGIAHDPIQRDMF---TPLFLGAQ 490
Cdd:cd17631 92 GAKVLF--DDLALLMYTSGTTGRPKGAMLTHRNLLWN----------------AVNALAALDLGPDDVLlvvAPLFHIGG 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 491 LLIPTSDDI---GT--------PGKLAEWMQTYGATVTHLTPAMGQLLSAQ---ATKEIPSLHHAFFVGDILTKRdcLRL 556
Cdd:cd17631 154 LGVFTLPTLlrgGTvvilrkfdPETVLDLIERHRVTSFFLVPTMIQALLQHprfATTDLSSLRAVIYGGAPMPER--LLR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 557 QTIAQNVNIINMYGTTETQRAVsyfeipsraqdsTFL---EVQKDIMPAGKGMHNVQLLVVNRHDRskTCAIGEVGEIYV 633
Cdd:cd17631 232 ALQARGVKFVQGYGMTETSPGV------------TFLspeDHRRKLGSAGRPVFFVEVRIVDPDGR--EVPPGEVGEIVV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 634 RAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQV 713
Cdd:cd17631 298 RGPHVMAGYWNRPEATAAAFRDGWF-------------------------------HTGDLGRLDEDGYLYIVDRKKDMI 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 714 KIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELEnfksssddlddlndpivkslllyrelIK 793
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELD--------------------------ED 400
|
570 580 590
....*....|....*....|....*....|....*
gi 254566307 794 DLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDK 828
Cdd:cd17631 401 ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
985-1297 |
1.06e-29 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 120.47 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYAHVrakdeESGLERLRNtgkvygiwneewTSRIKVVIADLSkDKLGLsgek 1064
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRS-----PPGAANLAA------------LPGVEFVRGDLR-DPEAL---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yAELANTIDLIIHNGALVH-WVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTehyitlsdtlteqGEDGI 1143
Cdd:COG0451 59 -AAALAGVDAVVHLAAPAGvGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGD-------------GEGPI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1144 PESDDLlgsskGLGTGYGQSKWAAEYIIRRAFER-GLRGAIIRPGYVTGHSRTGAcnTDDFLLRMLKGcAELGKLPNISN 1222
Cdd:COG0451 125 DEDTPL-----RPVSPYGASKLAAELLARAYARRyGLPVTILRPGNVYGPGDRGV--LPRLIRRALAG-EPVPVFGDGDQ 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 1223 TVNMVPVDHVALVVTASSLHPTAEEGhcVVQVTGHPRIRFNEFLNALND-YGYEVKLTdYVEWKRDLERFVVDQSK 1297
Cdd:COG0451 197 RRDFIHVDDVARAIVLALEAPAAPGG--VYNVGGGEPVTLRELAEAIAEaLGRPPEIV-YPARPGDVRPRRADNSK 269
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
247-831 |
1.46e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 124.91 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVmiyAYRGVD---LMVAVMG 323
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDG---------RRTTYAELDERVNRLANALRALGVKKGDRV---AVFDWNsheYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 324 VLKAGATFSVIDPAYPPArQNVY-LQVAKPAGLIV---LEK--AGVLDQL--VEDYI-------KNELSLVSRISNLkie 388
Cdd:PRK06187 76 VPKIGAVLHPINIRLKPE-EIAYiLNDAEDRVVLVdseFVPllAAILPQLptVRTVIvegdgpaAPLAPEVGEYEEL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 389 adgnvlggdVDGKDALYDYQQFktrrtgvlvGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKF-- 466
Cdd:PRK06187 152 ---------LAAASDTFDFPDI---------DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYlv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 467 ------TMLSGIahdpiqrdMFTPLFLGAQLLIPTSDDigtPGKLAEWMQTYGATVTHLTPAMGQLLSAQ---ATKEIPS 537
Cdd:PRK06187 214 ivpmfhVHAWGL--------PYLALMAGAKQVIPRRFD---PENLLDLIETERVTFFFAVPTIWQMLLKApraYFVDFSS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 538 LHHAFFVGDILTK---RDCLRLQtiaqNVNIINMYGTTETQRAVSYfeipSRAQDSTFLEVQKDImPAGKGMHNVQLLVV 614
Cdd:PRK06187 283 LRLVIYGGAALPPallREFKEKF----GIDLVQGYGMTETSPVVSV----LPPEDQLPGQWTKRR-SAGRPLPGVEARIV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 615 NRHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWfvspskwveedkkiskdepwrefylgprdrlYRTGDL 694
Cdd:PRK06187 354 DDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGW-------------------------------LHTGDV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 695 GRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQN-VTLVRRDK-DEEPilISYVVPKETPELEnfksssd 772
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVaVIGVPDEKwGERP--VAVVVLKPGATLD------- 473
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 773 dlddlndpivkslllyrelIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK06187 474 -------------------AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
276-831 |
3.92e-27 |
|
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: 117.41 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 276 QTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKpAGL 355
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG-SKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 356 IVLEKAGVLDQLvedyiKNELSLVSRISNLKIEADGNVLGGDVDGKDALYDYQQFKTRRTGVLvgPDSNPTLSFTSGSEG 435
Cdd:cd05926 90 VLTPKGELGPAS-----RAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPL--PDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 436 IPKGVLGRHFSLAYYFPWMSKTFNLSENDKfTML-------SGIAhdpiqRDMFTPLFLGAQLLIPTSDDigtPGKLAEW 508
Cdd:cd05926 163 RPKGVPLTHRNLAASATNITNTYKLTPDDR-TLVvmplfhvHGLV-----ASLLSTLAAGGSVVLPPRFS---ASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 509 MQTYGATVTHLTPAMGQ-LLSAQATKEIPSLHHAFFVgdiltkRDC---------LRLQTiAQNVNIINMYGTTETQRAV 578
Cdd:cd05926 234 VRDYNATWYTAVPTIHQiLLNRPEPNPESPPPKLRFI------RSCsaslppavlEALEA-TFGAPVLEAYGMTEAAHQM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 579 SYFEIPsraqdstflEVQKDIMPAGKGmHNVQLLVVNRHDrsKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPN-W 657
Cdd:cd05926 307 TSNPLP---------PGPRKPGSVGKP-VGVEVRILDEDG--EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDgW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 658 FvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQ 737
Cdd:cd05926 375 F-------------------------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 738 NVTL-VRRDKDEEPIlISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAHLKKTLASYAIPTIIVPMA 816
Cdd:cd05926 424 AVAFgVPDEKYGEEV-AAAVVLREGASV--------------------------TEEELRAFCRKHLAAFKVPKKVYFVD 476
|
570
....*....|....*
gi 254566307 817 KLPLNPNGKVDKPKL 831
Cdd:cd05926 477 ELPKTATGKIQRRKV 491
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
241-831 |
5.81e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.54 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 241 SGYRG--AIQDIFSDNAEKFPDRTCVVEtksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLM 318
Cdd:PRK06087 17 QGYWGdaSLADYWQQTARAMPDKIAVVD--------NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 319 VAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIV--LEKAgvldqlvEDYIKNELSLVSRISNLKieadgNVLGG 396
Cdd:PRK06087 89 IIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptLFKQ-------TRPVDLILPLQNQLPQLQ-----QIVGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 397 DVDGK----DALYDY-QQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRH----FSLAYYfpwmSKTFNLSENDKFT 467
Cdd:PRK06087 157 DKLAPatssLSLSQIiADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHnnilASERAY----CARLNLTWQDVFM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 468 MLSGIAHDP-IQRDMFTPLFLGAQLLIptsDDIGTPGKLAEWMQTYGATVTH-LTPAMGQLLSA--QATKEIPSLHhaFF 543
Cdd:PRK06087 233 MPAPLGHATgFLHGVTAPFLIGARSVL---LDIFTPDACLALLEQQRCTCMLgATPFIYDLLNLleKQPADLSALR--FF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 544 V--GDILTK---RDCLRlqtiaQNVNIINMYGTTETqravsyfeIPS---RAQDSTFLEVQKDimpaGKGMHNVQLLVVN 615
Cdd:PRK06087 308 LcgGTTIPKkvaRECQQ-----RGIKLLSVYGSTES--------SPHavvNLDDPLSRFMHTD----GYAAAGVEIKVVD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 616 RHdrSKTCAIGEVGEiyvraaglaEQYRGqpdlnkekfvPNWFVSPSKWVEEDKKISKDEPWreFYlgprdrlyrTGDLG 695
Cdd:PRK06087 371 EA--RKTLPPGCEGE---------EASRG----------PNVFMGYLDEPELTARALDEEGW--YY---------SGDLC 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 696 RYLPTGDCEVSGRADDqVKIRGFR-IELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKE---TPELEnfksss 771
Cdd:PRK06087 419 RMDEAGYIKITGRKKD-IIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAphhSLTLE------ 491
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254566307 772 ddlddlndpivkslllyrelikDLKAHL-KKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK06087 492 ----------------------EVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
985-1269 |
1.76e-26 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 116.97 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYAHVRAkDEESGLERLRntgkvygiwnEEW-TSRIKVVIADLSKDKLGLSGE 1063
Cdd:PRK07201 2 RYFVTGGTGFIGRRLVSRLLDRRREATVHVLVRR-QSLSRLEALA----------AYWgADRVVPLVGDLTEPGLGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1064 KYAELANtIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDtEHYITLSDTLTEQGEdgi 1143
Cdd:PRK07201 71 DIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAVAG-DYEGVFREDDFDEGQ--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1144 pesddllgsskGLGTGYGQSKWAAEYIIRRafERGLRGAIIRPGYVTGHSRTGACNTDDFLLRMLKGCAELGKLPNISNT 1223
Cdd:PRK07201 146 -----------GLPTPYHRTKFEAEKLVRE--ECGLPWRVYRPAVVVGDSRTGEMDKIDGPYYFFKVLAKLAKLPSWLPM 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 254566307 1224 V-------NMVPVDHV--ALVVTAsslHPTAEEGHCVVQVTGHPRiRFNEFLNAL 1269
Cdd:PRK07201 213 VgpdggrtNIVPVDYVadALDHLM---HKDGRDGQTFHLTDPKPQ-RVGDIYNAF 263
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
280-831 |
2.10e-24 |
|
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: 107.81 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 280 FTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAtfsvidpaypparqnvylqVAKPAGLIVLE 359
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGA-------------------VYVPLTTLLGP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 360 KAgvldqlvedyiknelsLVSRISNLKIEAdgnvlggdvdgkdalydyqqfktrrtgVLVGPDSNPTLSFTSGSEGIPKG 439
Cdd:cd05972 62 KD----------------IEYRLEAAGAKA---------------------------IVTDAEDPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 440 VLGRHFSLAYYFPWMSKTFNLSENDKFTMLSgiahDP-----IQRDMFTPLFLGAQLLIPTSDDIgTPGKLAEWMQTYGA 514
Cdd:cd05972 99 VLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA----DPgwakgAWSSFFGPWLLGATVFVYEGPRF-DAERILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 515 TVTHLTPAMGQLLSAQATKE--IPSLHHAFFVGDILTkRDCLRLQTIAQNVNIINMYGTTETQRAVSyfeipsraqDSTF 592
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLSSykFSHLRLVVSAGEPLN-PEVIEWWRAATGLPIRDGYGQTETGLTVG---------NFPD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 593 LEVQKDIMpaGKGM--HNVQLLvvnrHDRSKTCAIGEVGEIYVRaaglaeqyrgqpdlnkekfvPNWfVSPSKWVEEDKK 670
Cdd:cd05972 244 MPVKPGSM--GRPTpgYDVAII----DDDGRELPPGEEGDIAIK--------------------LPP-PGLFLGYVGDPE 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 671 isKDEP-WREFYlgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEE 749
Cdd:cd05972 297 --KTEAsIRGDY-------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRG 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 750 PILISYVVPKETPELEnfksssddlddlndpivkslllyRELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKP 829
Cdd:cd05972 368 EVVKAFVVLTSGYEPS-----------------------EELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
..
gi 254566307 830 KL 831
Cdd:cd05972 425 EL 426
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
274-831 |
7.68e-24 |
|
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: 106.40 E-value: 7.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 274 NSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQnvylqvakpa 353
Cdd:cd17654 11 TTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 354 gLIVLEKAGVLDQLVEDYIKNE-LSLVSRISNLKIEADGNVLggdvdgkdalydYqqfktrrtgVLvgpdsnptlsFTSG 432
Cdd:cd17654 81 -LTVMKKCHVSYLLQNKELDNApLSFTPEHRHFNIRTDECLA------------Y---------VI----------HTSG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 433 SEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDIGTPGKLAEWM-QT 511
Cdd:cd17654 129 TTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 512 YGATVTHLTPAM----------GQLLSAQATKEIPSLHHAFFVGDILtkrdclrLQTIAQNVN---IINMYGTTETQRAV 578
Cdd:cd17654 209 HRITVLQATPTLfrrfgsqsikSTVLSATSSLRVLALGGEPFPSLVI-------LSSWRGKGNrtrIFNIYGITEVSCWA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 579 SYFEIPSraQDSTflevqkdimpagkgmhnVQLlvvnrhdrsKTCAIGEVgeIYVRAAGLAEQyRGQpdlnkekfvpnwf 658
Cdd:cd17654 282 LAYKVPE--EDSP-----------------VQL---------GSPLLGTV--IEVRDQNGSEG-TGQ------------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 659 vspskwvEEDKKISKDEPWREFYLGPRDRLYRTGDLGRyLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRH-PLIRQ 737
Cdd:cd17654 318 -------VFLGGLNRVCILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESClGVESC 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 738 NVTLVRRDKdeepiLISYVVPKEtpelenfksssddlddlndpivKSLLLYRELIKDLkahlkktLASYAIPTIIVPMAK 817
Cdd:cd17654 390 AVTLSDQQR-----LIAFIVGES----------------------SSSRIHKELQLTL-------LSSHAIPDTFVQIDK 435
|
570
....*....|....
gi 254566307 818 LPLNPNGKVDKPKL 831
Cdd:cd17654 436 LPLTSHGKVDKSEL 449
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
245-831 |
4.75e-21 |
|
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: 98.60 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 245 GAIQDIFSDNAEKFPDRTCVVETksflnpnsqTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGV 324
Cdd:cd05959 4 NAATLVDLNLNEGRGDKTAFIDD---------AGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 325 LKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVleKAGVLDQLVEDYIKNELSLVSRI-SNLKIEADGNVLGGDVDGKDA 403
Cdd:cd05959 75 IRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV--SGELAPVLAAALTKSEHTLVVLIvSGGAGPEAGALLLAELVAAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 404 lydyQQFKTRRTGvlvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAyyfpWMSKTF-----NLSENDKFTMLSGIAHD-PI 477
Cdd:cd05959 153 ----EQLKPAATH----ADDPAFWLYSSGSTGRPKGVVHLHADIY----WTAELYarnvlGIREDDVCFSAAKLFFAyGL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 478 QRDMFTPLFLGAQ-LLIPTSDdigTPGKLAEWMQTYGATVTHLTPAM--GQLLSAQATKEIP-SLHHAFFVGDILTKRDC 553
Cdd:cd05959 221 GNSLTFPLSVGATtVLMPERP---TPAAVFKRIRRYRPTVFFGVPTLyaAMLAAPNLPSRDLsSLRLCVSAGEALPAEVG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 554 LRLQTIAqNVNIINMYGTTEtqraVSYFEIPSRAQDSTFlevqkdiMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYV 633
Cdd:cd05959 298 ERWKARF-GLDILDGIGSTE----MLHIFLSNRPGRVRY-------GTTGKPVPGYEVELRD--EDGGDVADGEPGELYV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 634 RAAGLAEQYRGQPDLNKEKFVPNWfvspskwveedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQV 713
Cdd:cd05959 364 RGPSSATMYWNNRDKTRDTFQGEW-------------------------------TRTGDKYVRDDDGFYTYAGRADDML 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 714 KIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPK---ETPElenfksssddlddlndpivkslllyrE 790
Cdd:cd05959 413 KVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpgyEDSE--------------------------A 466
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 254566307 791 LIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05959 467 LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
277-831 |
9.06e-21 |
|
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: 97.15 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 277 TRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLI 356
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 357 VlekagvldqlvedyiknelslvsrisnlkieadgnvlggdvDGKDALYdyqqfktrrtgvlvgpdsnptLSFTSGSEGI 436
Cdd:cd05919 88 T-----------------------------------------SADDIAY---------------------LLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 437 PKGVLGRH-FSLAYYFPWMSKTFNLSENDKFTMLS------GIAHDpiqrdMFTPLFLGAQLLIptSDDIGTPGKLAEWM 509
Cdd:cd05919 106 PKGVMHAHrDPLLFADAMAREALGLTPGDRVFSSAkmffgyGLGNS-----LWFPLAVGASAVL--NPGWPTAERVLATL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 510 QTYGATVTHLTPAMGQLLSAQATKE---IPSLHHAFFVGDILTKRDCLRLqTIAQNVNIINMYGTTETQRavsyfeipsr 586
Cdd:cd05919 179 ARFRPTVLYGVPTFYANLLDSCAGSpdaLRSLRLCVSAGEALPRGLGERW-MEHFGGPILDGIGATEVGH---------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 587 aqdsTFLEVQKD---IMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWfvspsk 663
Cdd:cd05919 248 ----IFLSNRPGawrLGSTGRPVPGYEIRLVD--EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGW------ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 664 wveedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVR 743
Cdd:cd05919 316 -------------------------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAV 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 744 RDKDEEPILISYVVPKetPELENFKSssddlddlndpivkslllyreLIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPN 823
Cdd:cd05919 371 PESTGLSRLTAFVVLK--SPAAPQES---------------------LARDIHRHLLERLSAHKVPRRIAFVDELPRTAT 427
|
....*...
gi 254566307 824 GKVDKPKL 831
Cdd:cd05919 428 GKLQRFKL 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
429-832 |
1.28e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 96.21 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 429 FTSGSEGIPKGVLGRH---FSLAYYFPWMsktFNLSENDkfTMLSgiahdpiqrdmFTPLF-LGAQL--LIPTsddIGTP 502
Cdd:cd05934 88 YTSGTTGPPKGVVITHanlTFAGYYSARR---FGLGEDD--VYLT-----------VLPLFhINAQAvsVLAA---LSVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 503 GKLAE---------W--MQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGT 571
Cdd:cd05934 149 ATLVLlprfsasrfWsdVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGM 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 572 TETQRAVSyfeipsraqdSTFLEVQKDiMPAGKGMHNVQLLVVNRHDRskTCAIGEVGEIYVRAA---GLAEQYRGQPDL 648
Cdd:cd05934 229 TETIVGVI----------GPRDEPRRP-GSIGRPAPGYEVRIVDDDGQ--ELPAGEPGELVIRGLrgwGFFKGYYNMPEA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 649 NKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTH 728
Cdd:cd05934 296 TAEAMRNGWF-------------------------------HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 729 ISRHPLIRQ-NVTLVRRDKDEEPILISYVVPK-ETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASY 806
Cdd:cd05934 345 ILRHPAVREaAVVAVPDEVGEDEVKAVVVLRPgETLDPE----------------------------ELFAFCEGQLAYF 396
|
410 420
....*....|....*....|....*.
gi 254566307 807 AIPTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:cd05934 397 KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
279-831 |
4.11e-20 |
|
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: 95.14 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 279 TFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAtfsVIDPAYPPARQNvylqvakpaglivl 358
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGA---VTNPILPFFREH-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 359 ekagvldqlvedyiknELSLVSRISNLKIEADGNVLGGdvdgkdalYDYQQFktrrtgvlvgPDSNPTLSFTSGSEGIPK 438
Cdd:cd05903 64 ----------------ELAFILRRAKAKVFVVPERFRQ--------FDPAAM----------PDAVALLLFTSGTTGEPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 439 GVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDP-IQRDMFTPLFLGAQLLIptsDDIGTPGKLAEWMQTYGATVT 517
Cdd:cd05903 110 GVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 518 H-LTPAMGQLLSAQATKEIPSLHHAFFV--GDILTKRDCLRLQTIAQNVnIINMYGTTETQRAVSYFEIPsraqdstflE 594
Cdd:cd05903 187 MgATPFLTDLLNAVEEAGEPLSRLRTFVcgGATVPRSLARRAAELLGAK-VCSAYGSTECPGAVTSITPA---------P 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 595 VQKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskd 674
Cdd:cd05903 257 EDRRLYTDGRPLPGVEIKVVD--DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWF---------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 675 epwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDqVKIR-GFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILI 753
Cdd:cd05903 319 ---------------RTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERAC 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 754 SYVVPKETPELEnfksssddlddlndpivkslllyrelIKDLKAHL-KKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05903 383 AVVVTKSGALLT--------------------------FDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
247-831 |
2.05e-19 |
|
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: 93.01 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMG---------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARqnvylqvakpaglivlekagvLDQLVEDyiknelslvsrisnlkieADGNVLGGDVDGKDALyd 406
Cdd:cd05936 72 AGAVVVPLNPLYTPRE---------------------LEHILND------------------SGAKALIVAVSFTDLL-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 407 yQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYyfpwmsktfNLSENDkftMLSGIAHDPIQR------- 479
Cdd:cd05936 111 -AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVA---------NALQIK---AWLEDLLEGDDVvlaalpl 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 480 --------DMFTPLFLGA-QLLIPTSDDIGTpgkLAEwMQTYGATVTHLTPAM-GQLLSAQATKEI--PSLHHAFFVGDI 547
Cdd:cd05936 178 fhvfgltvALLLPLALGAtIVLIPRFRPIGV---LKE-IRKHRVTIFPGVPTMyIALLNAPEFKKRdfSSLRLCISGGAP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 548 LTKRDCLRLQTIAQnVNIINMYGTTETQRAVSY--FEIPSRAQDstflevqkdimpAGKGMHNVQLLVVNrhDRSKTCAI 625
Cdd:cd05936 254 LPVEVAERFEELTG-VPIVEGYGLTETSPVVAVnpLDGPRKPGS------------IGIPLPGTEVKIVD--DDGEELPP 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 626 GEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEV 705
Cdd:cd05936 319 GEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------------------------------RTGDIGYMDEDGYFFI 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 706 SGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVT--LVRRDKDEEPilISYVVPKETPELENfksssddlddlndpivk 783
Cdd:cd05936 368 VDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVvgVPDPYSGEAV--KAFVVLKEGASLTE----------------- 428
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 254566307 784 slllyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05936 429 ---------EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
258-831 |
2.55e-19 |
|
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: 93.46 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 258 FPDRTCVvetkSFLNPNSQTRTfTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAY---RGVDLMVAVMGvlkAGATFSVI 334
Cdd:cd12119 9 HGDREIV----SRTHEGEVHRY-TYAEVAERARRLANALRRLGVKPGDRVATLAWnthRHLELYYAVPG---MGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 335 DPAYPPaRQNVYlqVAKPAGLIVLEKAGVLDQLVEDyIKNELSLVSRISNLKIEADGNVLGGDvdgkdALYDYQQFKTRR 414
Cdd:cd12119 81 NPRLFP-EQIAY--IINHAEDRVVFVDRDFLPLLEA-IAPRLPTVEHVVVMTDDAAMPEPAGV-----GVLAYEELLAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 415 TGVLVGPD----SNPTLSFTSGSEGIPKGVLGRH-------FSLAyyfpwMSKTFNLSENDkfTMLsgiahdPIqrdmfT 483
Cdd:cd12119 152 SPEYDWPDfdenTAAAICYTSGTTGNPKGVVYSHrslvlhaMAAL-----LTDGLGLSESD--VVL------PV-----V 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 484 PLF-------------LGAQLLIPTSDDigTPGKLAEWMQTYGATVTHLTPAMGQ-LLSAQATK--EIPSLHHAFFVGDI 547
Cdd:cd12119 214 PMFhvnawglpyaaamVGAKLVLPGPYL--DPASLAELIEREGVTFAAGVPTVWQgLLDHLEANgrDLSSLRRVVIGGSA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 548 LTKRDCLRLqtIAQNVNIINMYGTTETQRAVSYFEIPSRAQDSTFLEVQKDIMPAGKGMHNVQLLVVNRHDRSKTCAIGE 627
Cdd:cd12119 292 VPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 628 VGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSG 707
Cdd:cd12119 370 VGELQVRGPWVTKSYYKNDEESEALTEDGWL-------------------------------RTGDVATIDEDGYLTITD 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 708 RADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDK--DEEPILIsyVVPKETPELENfksssddlddlndpivksl 785
Cdd:cd12119 419 RSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPkwGERPLAV--VVLKEGATVTA------------------- 477
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 254566307 786 llyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd12119 478 -------EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
280-826 |
6.58e-19 |
|
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: 91.34 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 280 FTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAtfsvidpaypparqnvylqVAKPagLIVLe 359
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGA-------------------IAVP--LFAL- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 360 kagvldqLVEDyiknelSLVSRISNlkieADGNVLGGDvdgkdalydyqqfktrrtgvlvGPDSNPTLSFTSGSEGIPKG 439
Cdd:cd05971 65 -------FGPE------ALEYRLSN----SGASALVTD----------------------GSDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 440 VLGRHFSLAYYFPWMSKTFNLSENDKFTMLS--------GIAhdpiqrDMFTP-LFLGAQLLI--PTSDDigtPGKLAEW 508
Cdd:cd05971 106 ALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTpadwawigGLL------DVLLPsLYFGVPVLAhrMTKFD---PKAALDL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 509 MQTYGATVTHLTPAMGQLLSAQatkeipslhhaffvGDILtKRDCLRLQTIAQ-----------------NVNIINMYGT 571
Cdd:cd05971 177 MSRYGVTTAFLPPTALKMMRQQ--------------GEQL-KHAQVKLRAIATggeslgeellgwareqfGVEVNEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 572 TETQRAVSyfeipsraQDSTFLEVQKDIMPAGKGMHNVQLLvvnrHDRSKTCAIGEVGEIYVR---AAGLAEQYRgQPDL 648
Cdd:cd05971 242 TECNLVIG--------NCSALFPIKPGSMGKPIPGHRVAIV----DDNGTPLPPGEVGEIAVElpdPVAFLGYWN-NPSA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 649 NKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTH 728
Cdd:cd05971 309 TEKKMAGDWL-------------------------------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEEC 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 729 ISRHPLIRQNVTLVRRDKDEEPILISYVV--PKETPElenfksssddlddlndpivkslllyRELIKDLKAHLKKTLASY 806
Cdd:cd05971 358 LLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnPGETPS-------------------------DALAREIQELVKTRLAAH 412
|
570 580
....*....|....*....|
gi 254566307 807 AIPTIIVPMAKLPLNPNGKV 826
Cdd:cd05971 413 EYPREIEFVNELPRTATGKI 432
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
255-831 |
8.61e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 88.42 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 255 AEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVI 334
Cdd:PRK07656 15 ARRFGDKEAYVFGD---------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 335 DPAYPPARQNVYLQVAKPAGLIvlekagVLDQLV-EDY-IKNELSLVSRISNLKIEAdgnvlggDVDGKDALYDYQQF-- 410
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALF------VLGLFLgVDYsATTRLPALEHVVICETEE-------DDPHTEKMKTFTDFla 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 411 --KTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFtmlsgIAHDPiqrdMF------ 482
Cdd:PRK07656 153 agDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY-----LAANP----FFhvfgyk 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 483 ----TPLFLGAQLLI-PTSDdigtPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFF---------VGDIL 548
Cdd:PRK07656 224 agvnAPLMRGATILPlPVFD----PDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLavtgaasmpVALLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 549 TKRDCLRLQTIAQNvniinmYGTTETQRAVSYfeipSRAQDStflevQKDIM-PAGKGMHNVQLLVVNRHDRskTCAIGE 627
Cdd:PRK07656 300 RFESELGVDIVLTG------YGLSEASGVTTF----NRLDDD-----RKTVAgTIGTAIAGVENKIVNELGE--EVPVGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 628 VGEIYVRAAGLAEQYRGQPdlnkekfvpnwfvspskwvEEDKKISKDEPWrefylgprdrLYrTGDLGRYLPTGDCEVSG 707
Cdd:PRK07656 363 VGELLVRGPNVMKGYYDDP-------------------EATAAAIDADGW----------LH-TGDLGRLDEEGYLYIVD 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 708 RADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELENfksssddlddlndpivkslll 787
Cdd:PRK07656 413 RKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE--------------------- 471
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 254566307 788 yreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK07656 472 -----EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
300-831 |
1.25e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 87.50 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 300 GIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVID-PAYPPARQNVYLQVAKPAGL-IVLEKAGVLDQLVEDYIknels 377
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvPLNPTLKESVLRYLVADAGGrIVLADAGAADRLRDALP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 378 lVSRISNLKIEADGnvlgGDVDGKDAlydyqqfktrrTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKT 457
Cdd:cd05922 89 -ASPDPGTVLDADG----IRAARASA-----------PAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 458 FNLSENDK-FTMLsgiahdPIQRD-----MFTPLFLGAQLLIptSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLS--A 529
Cdd:cd05922 153 LGITADDRaLTVL------PLSYDyglsvLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTrlG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 530 QATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETQRAVSYF--EIPSRAQDStflevqkdimpAGKGMH 607
Cdd:cd05922 225 FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLppERILEKPGS-----------IGLAIP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 608 NVQLLVvnRHDRSKTCAIGEVGEIYVRAAglaeqyrgqpdlnkekfvpnwFVSPSKWveedkkisKDEPWREFYLGPRDR 687
Cdd:cd05922 294 GGEFEI--LDDDGTPTPPGEPGEIVHRGP---------------------NVMKGYW--------NDPPYRRKEGRGGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 688 LYrTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRqnVTLVRRDKD---EEPILISYVVPKETPel 764
Cdd:cd05922 343 LH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLII--EAAAVGLPDplgEKLALFVTAPDKIDP-- 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 765 enfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05922 418 ----------------------------KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
255-831 |
3.03e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.12 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 255 AEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVI 334
Cdd:PRK06155 31 AERYPDRPLLV---------FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 335 DPAYPPArQNVYLQVAKPAGLIVLEKAGV--LDQLvedyiknELSLVSRISNLKIEADGnvlGGDVDGKDALYDYQQFKT 412
Cdd:PRK06155 102 NTALRGP-QLEHILRNSGARLLVVEAALLaaLEAA-------DPGDLPLPAVWLLDAPA---SVSVPAGWSTAPLPPLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 413 RRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHfslAYYFPW---MSKTFNLSENDK-FTMLSgIAHDPIQRDMFTPLFLG 488
Cdd:PRK06155 171 PAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWWgrnSAEDLEIGADDVlYTTLP-LFHTNALNAFFQALLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 489 AQLLIptsddigTPGKLAE--W--MQTYGATVTHLTPAMGQLLSAQATKEIPSLHhaffvgdilTKRDCLRLQTIAQ--- 561
Cdd:PRK06155 247 ATYVL-------EPRFSASgfWpaVRRHGATVTYLLGAMVSILLSQPARESDRAH---------RVRVALGPGVPAAlha 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 562 ------NVNIINMYGTTETQrAVSYFEIPSRAQDStflevqkdimpAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRA 635
Cdd:PRK06155 311 afrerfGVDLLDGYGSTETN-FVIAVTHGSQRPGS-----------MGRLAPGFEARVVDEHDQE--LPDGEPGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 636 AglaeqyrgQPdlnkEKFVPNWFVSPSKWVeedkkiskdEPWREFYLGPRDRLYRTGDlgrylptGDCEVSGRADDQVKI 715
Cdd:PRK06155 377 D--------EP----FAFATGYFGMPEKTV---------EAWRNLWFHTGDRVVRDAD-------GWFRFVDRIKDAIRR 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 716 RGFRIELGEIDTHISRHPLIRQ-NVTLVRRDKDEEPILISyVVPKETPELEnfksssddlddlndPIvkslllyrelikD 794
Cdd:PRK06155 429 RGENISSFEVEQVLLSHPAVAAaAVFPVPSELGEDEVMAA-VVLRDGTALE--------------PV------------A 481
|
570 580 590
....*....|....*....|....*....|....*..
gi 254566307 795 LKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK06155 482 LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
249-826 |
5.40e-17 |
|
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: 86.01 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVETksflNPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:cd05970 21 DVVDAMAKEYPDKLALVWC----DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATfSVIDPAYPPARQNVY-LQVAKPAGLIVLEKAGVLDQlVEDYIKnELSLVSRisnlKIEADGNVLGGDVDGKDALYDY 407
Cdd:cd05970 97 AI-AIPATHQLTAKDIVYrIESADIKMIVAIAEDNIPEE-IEKAAP-ECPSKPK----LVWVGDPVPEGWIDFRKLIKNA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 408 QQFKTRRTGVLVGPDSNPTL-SFTSGSEGIPKGV-------LGrHFSLAYYfpWMsktfNLSENDKFTMlsgIAHDPIQR 479
Cdd:cd05970 170 SPDFERPTANSYPCGEDILLvYFSSGTTGMPKMVehdftypLG-HIVTAKY--WQ----NVREGGLHLT---VADTGWGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 480 DMFTPLF----LGAQLLIPTSDDIgTPGKLAEWMQTYGATVTHLTPAMGQ-LLSAQATK-EIPSLHHAFFVGDILTKRDC 553
Cdd:cd05970 240 AVWGKIYgqwiAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRfLIREDLSRyDLSSLRYCTTAGEALNPEVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 554 LRLQTiAQNVNIINMYGTTETQRAVSYFeipsraqdsTFLEVQKDIMpaGKGMHNVQLLVVNRHDRSktCAIGEVGEIYV 633
Cdd:cd05970 319 NTFKE-KTGIKLMEGFGQTETTLTIATF---------PWMEPKPGSM--GKPAPGYEIDLIDREGRS--CEAGEEGEIVI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 634 RAA-----GLAEQYRGQPdlnkEKFVPNWFvspskwveedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGR 708
Cdd:cd05970 385 RTSkgkpvGLFGGYYKDA----EKTAEVWH---------------------------DGYYHTGDAAWMDEDGYLWFVGR 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 709 ADDQVKIRGFRIELGEIDTHISRHP-LIRQNVTLVRRDKDEEPILISYVVPKETPELEnfksssddlddlndpivkslll 787
Cdd:cd05970 434 TDDLIKSSGYRIGPFEVESALIQHPaVLECAVTGVPDPIRGQVVKATIVLAKGYEPSE---------------------- 491
|
570 580 590
....*....|....*....|....*....|....*....
gi 254566307 788 yrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKV 826
Cdd:cd05970 492 --ELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
240-763 |
6.74e-17 |
|
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: 85.80 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 240 WSGYRGAIQDIFSDNAEKFPDRTCvvetkSFLNPNSQTRTFTYKQ-IDQASNIVGnYLVHTGIKRGDVVMIYAYRGVDLM 318
Cdd:cd05906 5 PEGAPRTLLELLLRAAERGPTKGI-----TYIDADGSEEFQSYQDlLEDARRLAA-GLRQLGLRPGDSVILQFDDNEDFI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 319 VAVMGVLKAGAtFSVIDPAyPPARQNVYLQVAKPAGLI-VLEKAGVL--DQLVEDYIK-NELSLVSRISNLKIEadgnvl 394
Cdd:cd05906 79 PAFWACVLAGF-VPAPLTV-PPTYDEPNARLRKLRHIWqLLGSPVVLtdAELVAEFAGlETLSGLPGIRVLSIE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 395 ggdvDGKDALYDYQqfktrrtGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFtmLS---- 470
Cdd:cd05906 151 ----ELLDTAADHD-------LPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVF--LNwvpl 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 471 ----GIAHDPIQrdmftPLFLGA-QLLIPTSDDIGTPGKLAEWMQTYGATVThLTPAMGQLLSAQATKEIP-------SL 538
Cdd:cd05906 218 dhvgGLVELHLR-----AVYLGCqQVHVPTEEILADPLRWLDLIDRYRVTIT-WAPNFAFALLNDLLEEIEdgtwdlsSL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 539 HHAFFVGDILTKRDCLRLQTI-----AQNVNIINMYGTTETQRAVSY---FEIPSRAQDSTFLEVqkdimpaGKGMHNVQ 610
Cdd:cd05906 292 RYLVNAGEAVVAKTIRRLLRLlepygLPPDAIRPAFGMTETCSGVIYsrsFPTYDHSQALEFVSL-------GRPIPGVS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 611 LLVVNRHDRSKtcAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVP-NWFvspskwveedkkiskdepwrefylgprdrly 689
Cdd:cd05906 365 MRIVDDEGQLL--PEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEdGWF------------------------------- 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 690 RTGDLGrYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTL---VRRDKDEEPILISYVVPKETPE 763
Cdd:cd05906 412 RTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAafaVRDPGAETEELAIFFVPEYDLQ 487
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
255-768 |
1.44e-16 |
|
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: 84.48 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 255 AEKFPDRTCVVEtksflnPNSQTRtFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVI 334
Cdd:cd05923 11 ASRAPDACAIAD------PARGLR-LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 335 DPAYPPARQNVYLQVAKPAGLIVLEKAGVLDQlvedyiknelslvSRISNLKIEAdgnvLGGDVDGKDALYDYQQFKTRR 414
Cdd:cd05923 84 NPRLKAAELAELIERGEMTAAVIAVDAQVMDA-------------IFQSGVRVLA----LSDLVGLGEPESAGPLIEDPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 415 TGVlvgpdSNPTLSF-TSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLsGIAhdPIQRDM-FTPLFLGAQLL 492
Cdd:cd05923 147 REP-----EQPAFVFyTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVL-GLM--PLYHVIgFFAVLVAALAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 493 -----IPTSDDigtPGKLAEWMQTYGATVTHLTPAMGQLL---SAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNvN 564
Cdd:cd05923 219 dgtyvVVEEFD---PADALKLIEQERVTSLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-E 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 565 IINMYGTTETQRAVsYFEIP---SRAQDSTFLEVQkdIMPAGKGMhnvqllvvnrhdrSKTCAIGEVGEIYVRAAGLA-- 639
Cdd:cd05923 295 KVNIYGTTEAMNSL-YMRDArtgTEMRPGFFSEVR--IVRIGGSP-------------DEALANGEEGELIVAAAADAaf 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 640 EQYRGQPDLNKEKFVPNWfvspskwveedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFR 719
Cdd:cd05923 359 TGYLNQPEATAKKLQDGW-------------------------------YRTGDVGYVDPSGDVRILGRVDDMIISGGEN 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254566307 720 IELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETP-------------ELENFK 768
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTlsadeldqfcrasELADFK 469
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
253-717 |
1.87e-16 |
|
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: 84.60 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 253 DNAEKFPDRTCVVetksFLN-PNSQTRTFTYKQIDQASNIVGNYLVHTGiKRGDVVMIYAYRGVDLMVAVMGVLKAGATf 331
Cdd:cd05931 1 RRAAARPDRPAYT----FLDdEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 332 SVidPAYPPAR-------QNVyLQVAKPAglIVLEKAGVLDQLVEDYIKNELSLVSRIsnlkieadgnvLGGDVDGKDAL 404
Cdd:cd05931 75 AV--PLPPPTPgrhaerlAAI-LADAGPR--VVLTTAAALAAVRAFAASRPAAGTPRL-----------LVVDLLPDTSA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 405 YDYQQFKTRRTGVLVgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDkfTMLSGIahdPIQRDM--- 481
Cdd:cd05931 139 ADWPPPSPDPDDIAY-------LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD--VVVSWL---PLYHDMgli 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 482 ---FTPLFLGAQL-LIPTSDDIGTPGKLAEWMQTYGATVT------------HLTPA-MGQL-LSaqatkeipSLHHAFF 543
Cdd:cd05931 207 gglLTPLYSGGPSvLMSPAAFLRRPLRWLRLISRYRATISaapnfaydlcvrRVRDEdLEGLdLS--------SWRVALN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 544 VG-----DILTK-----RDC-LRLQTI------AQNVNIINMyGTTETQRAVSYFEIPSRAQDSTFLEVQKD----IMPA 602
Cdd:cd05931 279 GAepvrpATLRRfaeafAPFgFRPEAFrpsyglAEATLFVSG-GPPGTGPVVLRVDRDALAGRAVAVAADDPaareLVSC 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 603 GKGMHNVQLLVVNRhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPnwfvspskwveedKKISKDEPWrefyl 682
Cdd:cd05931 358 GRPLPDQEVRIVDP-ETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGA-------------LAATDEGGW----- 418
|
490 500 510
....*....|....*....|....*....|....*
gi 254566307 683 gprdrlYRTGDLGrYLPTGDCEVSGRADDQVKIRG 717
Cdd:cd05931 419 ------LRTGDLG-FLHDGELYITGRLKDLIIVRG 446
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
225-826 |
2.07e-16 |
|
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: 84.55 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 225 EQQSKLLPDPTANLDWSGYRGAIQDIFSDNAEKF----PDRTCVVETKSflnPNSQTRTFTYKQIDQASNIVGNYLVHTG 300
Cdd:cd17634 29 YQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHlrenGDRTAIIYEGD---DTSQSRTISYRELHREVCRFAGTLLDLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 301 IKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAgLIVLEKAGVLDQLVEDYIKNelslVS 380
Cdd:cd17634 106 VKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR-LLITADGGVRAGRSVPLKKN----VD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 381 RISNLKIEADGNVL-----GGDVD---GKDALYDYQQFKT--RRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYY 450
Cdd:cd17634 181 DALNPNVTSVEHVIvlkrtGSDIDwqeGRDLWWRDLIAKAspEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 451 FPW-MSKTFNLSENDKFTMLSGI----AHDPIqrdMFTPLFLGAQ-LLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMG 524
Cdd:cd17634 261 AATtMKYVFDYGPGDIYWCTADVgwvtGHSYL---LYGPLACGATtLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 525 QLLSAQATK-----EIPSLHHAFFVGDILTKrDCLRLQT---IAQNVNIINMYGTTETqravSYFEIPSRAqdstflevQ 596
Cdd:cd17634 338 RALMAAGDDaiegtDRSSLRILGSVGEPINP-EAYEWYWkkiGKEKCPVVDTWWQTET----GGFMITPLP--------G 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 597 KDIMPAGKGMHNV---QLLVVNrhDRSKTCAIGEVGEIYVRAA--GLAEQYRGQPDLNKEKFvpnwfvspskwveedkki 671
Cdd:cd17634 405 AIELKAGSATRPVfgvQPAVVD--NEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTY------------------ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 672 skdepWREFylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPI 751
Cdd:cd17634 465 -----FSTF-----KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 752 LISYVV--PKETPElenfksssddlddlndpivkslllyRELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKV 826
Cdd:cd17634 535 PYAYVVlnHGVEPS-------------------------PELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
260-831 |
1.71e-15 |
|
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: 80.80 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 260 DRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVH-TGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd05941 1 DRIAIV---------DDGDSITYADLVARAARLANRLLAlGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARQNVYLQVAKPAglIVLEKAGVLdqlvedyiknelslvsrisnlkieadgnvlggdvdgkdalydyqqfktrrtgvl 418
Cdd:cd05941 72 PLAELEYVITDSEPS--LVLDPALIL------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 vgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAH-DPIQRDMFTPLFLGAQLLIPTSD 497
Cdd:cd05941 96 ----------YTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHvHGLVNALLCPLFAGASVEFLPKF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 498 DIgTPGKLAEWMQtyGATVTHLTPAMgqllsaqATKEIPSLHHAFFVGDILTKRDC--LRL----------QTIAQNVNI 565
Cdd:cd05941 166 DP-KEVAISRLMP--SITVFMGVPTI-------YTRLLQYYEAHFTDPQFARAAAAerLRLmvsgsaalpvPTLEEWEAI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 566 -----INMYGTTETQRAVSyfeipsraqdsTFLEVQKDIMPAGKGMHNVQLLVVNRhDRSKTCAIGEVGEIYVRAAGLAE 640
Cdd:cd05941 236 tghtlLERYGMTEIGMALS-----------NPLDGERRPGTVGMPLPGVQARIVDE-ETGEPLPRGEVGEIQVRGPSVFK 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 641 QYRGQPDLNKEKFVPnwfvspskwveedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGR-ADDQVKIRGFR 719
Cdd:cd05941 304 EYWNKPEATKEEFTD------------------------------DGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYK 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 720 IELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKE---TPELEnfksssddlddlndpivkslllyrelikDLK 796
Cdd:cd05941 354 VSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAgaaALSLE----------------------------ELK 405
|
570 580 590
....*....|....*....|....*....|....*
gi 254566307 797 AHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05941 406 EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
429-828 |
1.76e-15 |
|
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: 79.37 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 429 FTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDigtPGKLAEW 508
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFN---PKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 509 MQTYGATVTHLTPAMGQLLsAQATKEIPSLHHAFFVGDILTKRDCLRLQTIAQNVNIINMYGTTETqravSYFeipsraq 588
Cdd:cd17633 84 INQYNATVIYLVPTMLQAL-ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL----SFI------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 589 dsTFLEVQKDIMP--AGKGMHNVQLLVVNRHDrsktcaiGEVGEIYVRAAGLAEQYrgqpdlnkekfVPNWFVSPSKWve 666
Cdd:cd17633 152 --TYNFNQESRPPnsVGRPFPNVEIEIRNADG-------GEIGKIFVKSEMVFSGY-----------VRGGFSNPDGW-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 667 edkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIrqnvtlvrrdk 746
Cdd:cd17633 210 ----------------------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGI----------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 747 dEEPILISYvvPKEtpelenfksssddlddLNDPIVKSLLLYRELI-KDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGK 825
Cdd:cd17633 257 -EEAIVVGI--PDA----------------RFGEIAVALYSGDKLTyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
...
gi 254566307 826 VDK 828
Cdd:cd17633 318 IAR 320
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
232-766 |
2.37e-15 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 81.00 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 232 PDPTANLDWSG-------YRGAIQDIFSDNAEKFPDRTCVVETKSFLNPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRG 304
Cdd:cd05968 37 EPPYQTLDLSGgkpwaawFVGGRMNIVEQLLDKWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 305 DVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLEKAGVLDQLVEdyIKNELSLVSR--- 381
Cdd:cd05968 117 DRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVN--LKEEADKACAqcp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 382 -ISNLKIEADGNVLGGDVDGKDALYDYQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRH--FSLAYYFPwMSKTF 458
Cdd:cd05968 195 tVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHagFPLKAAQD-MYFQF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 459 NLSENDKFTMLS--GIAHDPIQrdMFTPLFLGAQL-LIPTSDDIGTPGKLAEWMQTYGatVTHLTpamgqlLSaqatkei 535
Cdd:cd05968 274 DLKPGDLLTWFTdlGWMMGPWL--IFGGLILGATMvLYDGAPDHPKADRLWRMVEDHE--ITHLG------LS------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 536 PSLHHAF--FVGDILTKRDCLRLQTIA--------------------QNVNIINMYGTTetqravsyfEIPSRAQDSTFL 593
Cdd:cd05968 337 PTLIRALkpRGDAPVNAHDLSSLRVLGstgepwnpepwnwlfetvgkGRNPIINYSGGT---------EISGGILGNVLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 594 evqKDIMPAG-----KGMHNVQLlvvnrhDRSKTCAIGEVGEIYVRAA--GLAEQYRGQPDLNKEKFVPNWfvsPSKWVE 666
Cdd:cd05968 408 ---KPIKPSSfngpvPGMKADVL------DESGKPARPEVGELVLLAPwpGMTRGFWRDEDRYLETYWSRF---DNVWVH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 667 edkkiskdepwrefylgprdrlyrtGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTL-VRRD 745
Cdd:cd05968 476 -------------------------GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIgVPHP 530
|
570 580
....*....|....*....|....*.
gi 254566307 746 -KDEEPILisYVVPKE----TPELEN 766
Cdd:cd05968 531 vKGEAIVC--FVVLKPgvtpTEALAE 554
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
3-231 |
2.58e-15 |
|
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: 80.45 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG--PTLSvLPRDYNRPVAGKVIEANKTFDIS-DILPFLNK-ANEPSVTQFTAPLAVFAVLVYRLTGDD 78
Cdd:pfam00668 192 QKDAAYWLEQLEGelPVLQ-LPKDYARPADRSFKGDRLSFTLDeDTEELLRKlAKAHGTTLNDVLLAAYGLLLSRYTGQD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 79 DIVILT-----DSPKKQNLP--FV----VRLQVDPSKSFVDVSKQVGEQYLESLE-RATPLKDIVTHLKESKQLPNYP-- 144
Cdd:pfam00668 271 DIVVGTpgsgrPSPDIERMVgmFVntlpLRIDPKGGKTFSELIKRVQEDLLSAEPhQGYPFGDLVNDLRLPRDLSRHPlf 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 145 -PIFRL-SFQTAKKVQQLSTLVEGSTR-------------DLAIFLENNT-SINIYYNSLLYTHNRIAYFSQQFSSFIDE 208
Cdd:pfam00668 351 dPMFSFqNYLGQDSQEEEFQLSELDLSvssvieeeakydlSLTASERGGGlTIKIDYNTSLFDEETIERFAEHFKELLEQ 430
|
250 260
....*....|....*....|...
gi 254566307 209 VNKAPETPIGKISLLTEQQSKLL 231
Cdd:pfam00668 431 AIAHPSQPLSELDLLSDAEKQKL 453
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
280-828 |
3.59e-15 |
|
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: 79.87 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 280 FTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPParqnvylqvakpaglivle 359
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGP------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 360 KAgvldqlvedyIKNELSLvsrisnlkieADGNVLGGDVDGKDALydyqqfktrrtgvlvgpDSNPTLS-FTSGSEGIPK 438
Cdd:cd05973 62 KA----------IEHRLRT----------SGARLVVTDAANRHKL-----------------DSDPFVMmFTSGTTGLPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 439 GVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSgiahDP-----IQRDMFTPLFLGaqllIPTSDDIG--TPGKLAEWMQT 511
Cdd:cd05973 105 GVPVPLRALAAFGAYLRDAVDLRPEDSFWNAA----DPgwaygLYYAITGPLALG----HPTILLEGgfSVESTWRVIER 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 512 YGATVTHLTPAMGQLLSAqATKEIP-----SLHHAFFVGDILTKrDCLRLQTIAQNVNIINMYGTTETQRAVSYFEIPSR 586
Cdd:cd05973 177 LGVTNLAGSPTAYRLLMA-AGAEVParpkgRLRRVSSAGEPLTP-EVIRWFDAALGVPIHDHYGQTELGMVLANHHALEH 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 587 aqdstflEVQKDIMPAGKGMHNVQLLvvnrHDRSKTCAIGEVGEiyvraagLAEQYRGQPDLnkekfvpnWFvsPSKWVE 666
Cdd:cd05973 255 -------PVHAGSAGRAMPGWRVAVL----DDDGDELGPGEPGR-------LAIDIANSPLM--------WF--RGYQLP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 667 EDKKISKDepWrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDK 746
Cdd:cd05973 307 DTPAIDGG--Y-----------YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDP 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 747 DEEPILISYVVPKE----TPELEnfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNP 822
Cdd:cd05973 374 ERTEVVKAFVVLRGghegTPALA---------------------------DELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
....*.
gi 254566307 823 NGKVDK 828
Cdd:cd05973 427 SGKIQR 432
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
278-831 |
7.31e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 79.31 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIV 357
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 358 LEKagvLDQLVEDyIKNELSL----VSRISNLKIEADGNVLGGDVDGK--------DALYDYQQFKTRRTGVLVGPDSNP 425
Cdd:PRK06178 137 LDQ---LAPVVEQ-VRAETSLrhviVTSLADVLPAEPTLPLPDSLRAPrlaaagaiDLLPALRACTAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 426 TLSFTSGSEGIPKGVLGRHFSLAYyfpwMSKTF---NLSENDKFTMLS-----GIAHDPIqrDMFTPLFLGAQLLIPTSD 497
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMVY----TAAAAyavAVVGGEDSVFLSflpefWIAGENF--GLLFPLFSGATLVLLARW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 498 DigtPGKLAEWMQTYGATVTHLT----------PAMGQllsaqatKEIPSLHHAFFVGDI--LTKRDCLRLQTIAQNVNI 565
Cdd:PRK06178 287 D---AVAFMAAVERYRVTRTVMLvdnavelmdhPRFAE-------YDLSSLRQVRVVSFVkkLNPDYRQRWRALTGSVLA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 566 INMYGTTETQRAvsyfeipsraqDSTFLEVQKDIM-----PAGKGMH--NVQLLVVNrHDRSKTCAIGEVGEIYVRAAGL 638
Cdd:PRK06178 357 EAAWGMTETHTC-----------DTFTAGFQDDDFdllsqPVFVGLPvpGTEFKICD-FETGELLPLGAEGEIVVRTPSL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 639 AEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGF 718
Cdd:PRK06178 425 LKGYWNKPEATAEALRDGWL-------------------------------HTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 719 RIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELENfksssddlddlndpivkslllyreliKDLKAH 798
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA--------------------------AALQAW 527
|
570 580 590
....*....|....*....|....*....|...
gi 254566307 799 LKKTLASYAIPTIIVpMAKLPLNPNGKVDKPKL 831
Cdd:PRK06178 528 CRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
254-832 |
9.93e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 78.82 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 254 NAEKFPDRTCVVEtksflnpnsQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSV 333
Cdd:PRK07788 58 AARRAPDRAALID---------ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 334 IDPAYPPaRQNVylQVAKPAGLIVL----EKAGVLDQLVEDYIKnELSLVSRISNLKIEADGnvlggdVDGKDALYDyqq 409
Cdd:PRK07788 129 LNTGFSG-PQLA--EVAAREGVKALvyddEFTDLLSALPPDLGR-LRAWGGNPDDDEPSGST------DETLDDLIA--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 410 fkTRRTGVLVGPDSNPTLS-FTSGSEGIPKGVLGRHFSLayyfpwmsktfnlsendkFTMLSGI-AHDPIQRDMFT---- 483
Cdd:PRK07788 196 --GSSTAPLPKPPKPGGIViLTSGTTGTPKGAPRPEPSP------------------LAPLAGLlSRVPFRAGETTllpa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 484 PLF-------------LGAQLLIPTSDDigtPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIP-----SLHHAFFVG 545
Cdd:PRK07788 256 PMFhatgwahltlamaLGSTVVLRRRFD---PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAkydtsSLKIIFVSG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 546 DILTKRDCLRLQTIAQNVnIINMYGTTEtqraVSYFEIPSRAqdstflEVQKDIMPAGKGMHNVQLLVVNRHDRSKTcaI 625
Cdd:PRK07788 333 SALSPELATRALEAFGPV-LYNLYGSTE----VAFATIATPE------DLAEAPGTVGRPPKGVTVKILDENGNEVP--R 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 626 GEVGEIYVRAAGLAEQYRGQPdlnkekfvpnwfvspskwveeDKKISkdepwrefylgprDRLYRTGDLGRYLPTGDCEV 705
Cdd:PRK07788 400 GVVGRIFVGNGFPFEGYTDGR---------------------DKQII-------------DGLLSSGDVGYFDEDGLLFV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 706 SGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELENfksssddlddlndpivksl 785
Cdd:PRK07788 446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE------------------- 506
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 254566307 786 llyreliKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLP 832
Cdd:PRK07788 507 -------DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
249-831 |
1.19e-14 |
|
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: 78.52 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGD---------RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATFSVIDPAYPPARQNVYLQVAKPAGLIVLEKAGVLDQLvedyiknelslvsrisnlkieadgnvlggdvdgkdALYDYQ 408
Cdd:cd05920 90 AVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHR-----------------------------------ALAREL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 409 QFKTRRTGVLVgpdsnptLSftSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHD-----PiqrDMFT 483
Cdd:cd05920 135 AESIPEVALFL-------LS--GGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNfplacP---GVLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 484 PLFLGAQLLIPTSddiGTPGKLAEWMQTYGATVTHLTPAMGQL-LSAQA--TKEIPSLH------------HAFFVGDIL 548
Cdd:cd05920 203 TLLAGGRVVLAPD---PSPDAAFPLIEREGVTVTALVPALVSLwLDAAAsrRADLSSLRllqvggarlspaLARRVPPVL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 549 tkrDClRLQTIaqnvniinmYGTTETqrAVSYfeipSRAQDS--TFLEVQKDIMPAGKgmhnvQLLVVNRHDRskTCAIG 626
Cdd:cd05920 280 ---GC-TLQQV---------FGMAEG--LLNY----TRLDDPdeVIIHTQGRPMSPDD-----EIRVVDEEGN--PVPPG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 627 EVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVS 706
Cdd:cd05920 334 EEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------------------------------YRTGDLVRRTPDGYLVVE 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 707 GRADDQVKIRGFRIELGEIDTHISRHPLIRQnVTLVRRDkdeEPIL----ISYVVPKETPelenfksssddlddlndpiV 782
Cdd:cd05920 384 GRIKDQINRGGEKIAAEEVENLLLRHPAVHD-AAVVAMP---DELLgersCAFVVLRDPP-------------------P 440
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 254566307 783 KSLllyrelikDLKAHLKKT-LASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05920 441 SAA--------QLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
280-826 |
1.26e-14 |
|
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: 77.93 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 280 FTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLE 359
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 360 KagvldqlvedyiknelslvsrisnlkieadgnvlggdvdgkdaLYDyqqfktRRTgvlvgPDSNPTLSFTSGSEGIPKG 439
Cdd:cd05969 81 E-------------------------------------------LYE------RTD-----PEDPTLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 440 VLGRHFSLAYYFPWMSKTFNLSENDKF------TMLSGIAHdpiqrDMFTPLFLGAQLLIptSDDIGTPGKLAEWMQTYG 513
Cdd:cd05969 107 VLHVHDAMIFYYFTGKYVLDLHPDDIYwctadpGWVTGTVY-----GIWAPWLNGVTNVV--YEGRFDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 514 ATVTHLTPA-----MGQLLSAQATKEIPSLHHAFFVGDILTKrDCLRLQTIAQNVNIINMYGTTET--QRAVSYFEIPSR 586
Cdd:cd05969 180 VTVWYTAPTairmlMKEGDELARKYDLSSLRFIHSVGEPLNP-EAIRWGMEVFGVPIHDTWWQTETgsIMIANYPCMPIK 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 587 AQDstflevqkdimpAGKGMHNVQLLVVNRhDRSKTCAiGEVGEIYVRAA--GLAEQYRGQPDLNKEKFVPNWfvspskw 664
Cdd:cd05969 259 PGS------------MGKPLPGVKAAVVDE-NGNELPP-GTKGILALKPGwpSMFRGIWNDEERYKNSFIDGW------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 665 veedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRR 744
Cdd:cd05969 318 ------------------------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 745 DKDEEPILISYVVPKetpelENFKSSSddlddlndpivkslllyrELIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNG 824
Cdd:cd05969 374 DPLRGEIIKAFISLK-----EGFEPSD------------------ELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSG 430
|
..
gi 254566307 825 KV 826
Cdd:cd05969 431 KI 432
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
255-933 |
1.77e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.44 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 255 AEKFPDRTCVvetkSFLN-PNSQTRTFTYKQIDQASNIVGNYLvHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGatfsV 333
Cdd:PRK05691 19 AAQTPDRLAL----RFLAdDPGEGVVLSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYVAAFFGCLYAG----V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 334 ID-PAYPP--AR---QNVYLQV---AKPAglIVLEKAGVLDQLVEdyiknelslvsrISNLKIEADGNVLGgdVDGKD-A 403
Cdd:PRK05691 90 IAvPAYPPesARrhhQERLLSIiadAEPR--LLLTVADLRDSLLQ------------MEELAAANAPELLC--VDTLDpA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 404 LYDYQQfktrrtGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIahdPIQRDM-- 481
Cdd:PRK05691 154 LAEAWQ------EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWL---PLYHDMgl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 482 ----FTPLFLGAQ-LLIPTSDDIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQ-ATKEIPSLH----HAFFVGDILTKR 551
Cdd:PRK05691 225 igglLQPIFSGVPcVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERvSESALERLDlsrwRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 552 DCLRlqTIAQNV--------NIINMYGTTEtqrAVSYFEIPSRAQDSTFLEVQKD--------------IMPAGKGMHNV 609
Cdd:PRK05691 305 DSLE--RFAEKFaacgfdpdSFFASYGLAE---ATLFVSGGRRGQGIPALELDAEalarnraepgtgsvLMSCGRSQPGH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 610 QLLVVNRHdRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVpnwfvspskwvEEDKKIskdepWrefylgprdrlY 689
Cdd:PRK05691 380 AVLIVDPQ-SLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFV-----------EHDGRT-----W-----------L 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 690 RTGDLGrYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHplirqnVTLVRR---------DKDEEPILISYVVPKE 760
Cdd:PRK05691 432 RTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVERE------VEVVRKgrvaafavnHQGEEGIGIAAEISRS 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 761 tpelenfksssddlddlndpiVKSLLLYRELIKDLKAHLKKtlASYAIPTIIV---PMAkLPLNPNGKVDKP----KLPF 833
Cdd:PRK05691 505 ---------------------VQKILPPQALIKSIRQAVAE--ACQEAPSVVLllnPGA-LPKTSSGKLQRSacrlRLAD 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 834 PDTVQLAAVAQKSSAEVDDSEFTTTELQ--IKDLWLQVLPnpPASISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLG 911
Cdd:PRK05691 561 GSLDSYALFPALQAVEAAQTAASGDELQarIAAIWCEQLK--VEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLR 638
|
730 740
....*....|....*....|..
gi 254566307 912 TIFKHPTVKLFAAEVDRVKNGD 933
Cdd:PRK05691 639 QLFEAPTLAAFSAAVARQLAGG 660
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
986-1247 |
2.00e-14 |
|
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: 75.78 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERdlDVQVYAHVRAKDEESGLERLrntgkvygiwneewtsRIKVVIADLskdklglsgEKY 1065
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQ--GYRVRALVRSGSDAVLLDGL----------------PVEVVEGDL---------TDA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1066 AELA---NTIDLIIHNGALVHWVYPYSK-LRDANVISTINVLNLAASGKPKQFGFVSSTSTLDtEHYITLSDtlteqgED 1141
Cdd:cd05228 54 ASLAaamKGCDRVFHLAAFTSLWAKDRKeLYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALG-GPPDGRID------ET 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1142 GIPESDDllgsskgLGTGYGQSKWAAEYIIRRAFERGLRGAIIRPGYVTG---HSRTgacNTDDFLLRMLKgcaelGKLP 1218
Cdd:cd05228 127 TPWNERP-------FPNDYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFGpgdEGPT---STGLDVLDYLN-----GKLP 191
|
250 260 270
....*....|....*....|....*....|
gi 254566307 1219 NISNT-VNMVPVDHVALVVTASSLHPTAEE 1247
Cdd:cd05228 192 AYPPGgTSFVDVRDVAEGHIAAMEKGRRGE 221
|
|
| UDP_G4E_4_SDR_e |
cd05232 |
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
985-1253 |
2.46e-14 |
|
UDP-glucose 4 epimerase, subgroup 4, extended (e) 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. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187543 [Multi-domain] Cd Length: 303 Bit Score: 75.46 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQvyAHVRAkdeesgLERLRNTGKVYGIWNEEWTSRikvviadlskdklglsgek 1064
Cdd:cd05232 1 KVLVTGANGFIGRALVDKLLSRGEEVR--IAVRN------AENAEPSVVLAELPDIDSFTD------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yaeLANTIDLIIHNGALVH-----WVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEhyiTLSDTLTEQG 1139
Cdd:cd05232 54 ---LFLGVDAVVHLAARVHvmndqGADPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEG---TVGAPFDETD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1140 EDGiPESDdllgsskglgtgYGQSKWAAEYIIRRAFER-GLRGAIIRPGYVTGHSRTGacNtddfLLRMLKGCAELGKLP 1218
Cdd:cd05232 128 PPA-PQDA------------YGRSKLEAERALLELGASdGMEVVILRPPMVYGPGVRG--N----FARLMRLIDRGLPLP 188
|
250 260 270
....*....|....*....|....*....|....*..
gi 254566307 1219 --NISNTVNMVPVDHVALVVTASSLHPTAEEGHCVVQ 1253
Cdd:cd05232 189 pgAVKNRRSLVSLDNLVDAIYLCISLPKAANGTFLVS 225
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
861-920 |
4.03e-14 |
|
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: 67.97 E-value: 4.03e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 861 QIKDLWLQVLPNPPASISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVK 920
Cdd:pfam00550 2 RLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
856-928 |
5.41e-14 |
|
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: 68.34 E-value: 5.41e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 856 TTTELQIKDLWLQVLPNPPASISLEDSFF-DLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAEVDR 928
Cdd:COG0236 4 EELEERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
244-831 |
8.75e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 75.74 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 244 RGAIQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMG 323
Cdd:PRK08316 10 RQTIGDILRRSARRYPDKTALV---------FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 324 VLKAGATFSVIDpaypparqnvYLQVAKPAGLIvLEKAGVLDQLVEDYIKNELSLVSRISNLKIEADGNVLGGdVDGKDA 403
Cdd:PRK08316 81 CARAGAVHVPVN----------FMLTGEELAYI-LDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGG-REAPGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 404 LYDYQQFKTRRTGVLVGPDSNPT----LSFTSGSEGIPKGVLGRHFSL-AYYfpwMSKTF--NLSENDKFtmlsgIAHDP 476
Cdd:PRK08316 149 WLDFADWAEAGSVAEPDVELADDdlaqILYTSGTESLPKGAMLTHRALiAEY---VSCIVagDMSADDIP-----LHALP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 477 I----QRDMF--TPLFLGAQLLIPTSDDigtPGKLAEWMQTYGATVTHLTPA--MGQLLSAQ-ATKEIPSLHHAFFVGDI 547
Cdd:PRK08316 221 LyhcaQLDVFlgPYLYVGATNVILDAPD---PELILRTIEAERITSFFAPPTvwISLLRHPDfDTRDLSSLRKGYYGASI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 548 LTKRDCLRLQTIAQNVNIINMYGTTETqravsyfeipsrAQDSTFL--EVQKDIM-PAGKGMHNVQLLVVNrhDRSKTCA 624
Cdd:PRK08316 298 MPVEVLKELRERLPGLRFYNCYGQTEI------------APLATVLgpEEHLRRPgSAGRPVLNVETRVVD--DDGNDVA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 625 IGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFVSpskwveedkkiskdepwrefylgprdrlyrtGDLGRYLPTGDCE 704
Cdd:PRK08316 364 PGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHS-------------------------------GDLGVMDEEGYIT 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 705 VSGRADDQVKIRGFRIELGEIDTHISRHPLIR-------------QNVTLVrrdkdeepilisyVVPKE----TPElenf 767
Cdd:PRK08316 413 VVDRKKDMIKTGGENVASREVEEALYTHPAVAevaviglpdpkwiEAVTAV-------------VVPKAgatvTED---- 475
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 768 ksssddlddlndpivkslllyrELIkdlkAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK08316 476 ----------------------ELI----AHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
426-829 |
2.51e-13 |
|
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: 72.75 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 426 TLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLIPTSDDigtpgKL 505
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ-----AL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 506 AEWMQTYGATVTHLTPAM-GQLLSAQATKEIPSLHHAFFVGDILTKRDcLRLQTIAQNVNIINMYGTTETQRAVSYFEIP 584
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQlQRLLDSGQGPAALKSLRAVLLGGAPIPPE-LLERAADRGIPLYTTYGMTETASQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 585 SRAQDStflevqkdimpAGKGMHNVQLLVVNRhdrsktcaigevGEIYVRAAGLAEQYRgQPDLNKEKFVPNWFvspskw 664
Cdd:cd17630 158 GFGRGG-----------VGVLLPGRELRIVED------------GEIWVGGASLAMGYL-RGQLVPEFNEDGWF------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 665 veedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRR 744
Cdd:cd17630 208 -------------------------TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 745 DKD--EEPILIsyVVPKETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASYAIPTIIVPMAKLPLNP 822
Cdd:cd17630 263 DEElgQRPVAV--IVGRGPADPA----------------------------ELRAWLKDKLARFKLPKRIYPVPELPRTG 312
|
....*..
gi 254566307 823 NGKVDKP 829
Cdd:cd17630 313 GGKVDRR 319
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
247-828 |
3.37e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 73.66 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVEtksflnpnsQTRTFTYKQIDQASNIVGNYLvHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKE---------NDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPARQNVYLQVAKPAGLIVlekagvldqlvEDYIKNELSlvsrisnlkiEADGNVLGGD---VDGKDA 403
Cdd:PRK07638 73 AGWTCVPLDIKWKQDELKERLAISNADMIVT-----------ERYKLNDLP----------DEEGRVIEIDewkRMIEKY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 404 LYDYQQFKTrrtgvlvgPDSNP-TLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMF 482
Cdd:PRK07638 132 LPTYAPIEN--------VQNAPfYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 483 TPLFLGAQL-LIPTSddigTPGKLAEWMQTYGATVTHLTPAMGQ-LLSAQATKE-----IPSlhhaffvGDILTKRDCLR 555
Cdd:PRK07638 204 STLYVGQTVhLMRKF----IPNQVLDKLETENISVMYTVPTMLEsLYKENRVIEnkmkiISS-------GAKWEAEAKEK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 556 LQTIAQNVNIINMYGTTETQrAVSYF--EIPSRAQDStflevqkdimpAGKGMHNVQLLVvnRHDRSKTCAIGEVGEIYV 633
Cdd:PRK07638 273 IKNIFPYAKLYEFYGASELS-FVTALvdEESERRPNS-----------VGRPFHNVQVRI--CNEAGEEVQKGEIGTVYV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 634 RAAGLAEQYRGQPDLNKEKFVPNWFVspskwveedkkiskdepwrefylgprdrlyrTGDLGRYLPTGDCEVSGRADDQV 713
Cdd:PRK07638 339 KSPQFFMGYIIGGVLARELNADGWMT-------------------------------VRDVGYEDEEGFIYIVGREKNMI 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 714 KIRGFRIELGEIDTHISRHPLIRQNVTLVRRDkdeepiliSYVvpKETPELenfksssddlddlndpIVKSlllyRELIK 793
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPD--------SYW--GEKPVA----------------IIKG----SATKQ 437
|
570 580 590
....*....|....*....|....*....|....*
gi 254566307 794 DLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDK 828
Cdd:PRK07638 438 QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
684-919 |
2.91e-12 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 69.01 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 684 PRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHI----SRHPLIRQNVTLVRRDKDEEPILISYVVPK 759
Cdd:COG3433 74 YPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLlvlrAAAVVRVAVLAALRGAGVGLLLIVGAVAAL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 760 ETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFPDTVQL 839
Cdd:COG3433 154 DGLAAA----------------------------AALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 840 AAVAQKSSAevddSEFTTTELQIKDLWLQVLPNPPASISLEDSFFDLGGHSILATRMIFELRRKlAVDLPLGTIFKHPTV 919
Cdd:COG3433 206 LAAASPAPA----LETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTL 280
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
425-828 |
3.63e-12 |
|
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: 69.60 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 425 PTLSFTSGSEGIPKGVLGRHFSL-AYYFPWMSKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAqlLIPTSDDIGTPG 503
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG--LCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 504 KLAEWMQTYGATVTHLTP-AMGQLLS--AQATKEIPSLHHAFFVGDILTKRDcLRLQTIAQNVNIINMYGTTETQRAvsy 580
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPtLLSKLVSelKSANATVPSLRLIGYGGSRAIAAD-VRFIEATGLTNTAQVYGLSETGTA--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 581 feipsraqdsTFLEV---QKDIMPAGKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNW 657
Cdd:cd17635 158 ----------LCLPTdddSIEINAVGRPYPGVDVYLAA--TDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 658 FvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQ 737
Cdd:cd17635 226 V-------------------------------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 738 NVTLVRRDKDEEPILISYVvpketpelenfksssddlddlndpiVKSLLLYRELIKDLKAHLKKTLASYAIPTIIVPMAK 817
Cdd:cd17635 275 CACYEISDEEFGELVGLAV-------------------------VASAELDENAIRALKHTIRRELEPYARPSTIVIVTD 329
|
410
....*....|.
gi 254566307 818 LPLNPNGKVDK 828
Cdd:cd17635 330 IPRTQSGKVKR 340
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
249-831 |
3.99e-12 |
|
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: 70.56 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVETKsflnpnsqtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGE---------RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATfsvidP--AYPPARQ---NVYLQVAKPAGLIVLEKAGVLD--QLVEDyiknelsLVSRISNLKieadgNVL----GGD 397
Cdd:COG1021 100 AI-----PvfALPAHRRaeiSHFAEQSEAVAYIIPDRHRGFDyrALARE-------LQAEVPSLR-----HVLvvgdAGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 398 VDGKDALYDyqqfkTRRTGVLVGPDSNP----TLSftSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIA 473
Cdd:COG1021 163 FTSLDALLA-----APADLSEPRPDPDDvaffQLS--GGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 474 HDpiqrdmFT---PLFLGAQL------LIPTSDdigtPGKLAEWMQTYGATVTHLTPAMGQLL---SAQATKEIPSLH-- 539
Cdd:COG1021 236 HN------FPlssPGVLGVLYaggtvvLAPDPS----PDTAFPLIERERVTVTALVPPLALLWldaAERSRYDLSSLRvl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 540 ----------HAFFVGDILTkrdClRLQtiaqnvniiNMYGTTETqrAVSYfeipSRAQDStfLEVQ-----KDIMPAGk 604
Cdd:COG1021 306 qvggaklspeLARRVRPALG---C-TLQ---------QVFGMAEG--LVNY----TRLDDP--EEVIlttqgRPISPDD- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 605 gmhnvQLLVVNRHDRskTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPNWFvspskwveedkkiskdepwrefylgp 684
Cdd:COG1021 364 -----EVRIVDEDGN--PVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------------------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 685 rdrlYRTGDLGRYLPTGDCEVSGRADDQVkIRGfrielGE------IDTHISRHPLIRqNVTLVRRDkDE---EPIlISY 755
Cdd:COG1021 411 ----YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVH-DAAVVAMP-DEylgERS-CAF 477
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 756 VVPK-ETPELenfksssddlddlndpivkslllyreliKDLKAHLK-KTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:COG1021 478 VVPRgEPLTL----------------------------AELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| SDR_e |
cd08946 |
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ... |
986-1236 |
8.37e-12 |
|
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: 65.78 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERDLDVQVYAHVrakdeesglerlrntgkvygiwneewtsrikvviadlskdklglsgeky 1065
Cdd:cd08946 1 ILVTGGAGFIGSHLVRRLLERGHEVVVIDRL------------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1066 aelantiDLIIHNGALVH----WVYPySKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTehyitlsdtlteqGED 1141
Cdd:cd08946 32 -------DVVVHLAALVGvpasWDNP-DEDFETNVVGTLNLLEAARKAGVKRFVYASSASVYGS-------------PEG 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1142 GIPESDDLLGSSkglgTGYGQSKWAAEYIIRRAFER-GLRGAIIRPGYVTGHSRTGacNTDDFLLRMLKGCAELGKLP-- 1218
Cdd:cd08946 91 LPEEEETPPRPL----SPYGVSKLAAEHLLRSYGESyGLPVVILRLANVYGPGQRP--RLDGVVNDFIRRALEGKPLTvf 164
|
250
....*....|....*....
gi 254566307 1219 -NISNTVNMVPVDHVALVV 1236
Cdd:cd08946 165 gGGNQTRDFIHVDDVVRAI 183
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
276-761 |
1.54e-11 |
|
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: 68.88 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 276 QTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAyrgvdLMV--AVMGVL---KAGATFSVIDPAYPPARQNVYLQVA 350
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYM-----PMIpeAAIAMLacaRIGAIHSVVFGGFAAKELASRIDDA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 351 KPAgLIVLEKAGV-------LDQLVEDYIknELSLVSRISNL-----KIEADGNVLGGDVDGKDALYDYQqfktRRTGVL 418
Cdd:cd05967 154 KPK-LIVTASCGIepgkvvpYKPLLDKAL--ELSGHKPHHVLvlnrpQVPADLTKPGRDLDWSELLAKAE----PVDCVP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 VgpDSNPTLS--FTSGSEGIPKGVL----GRHFSLAYYfpwMSKTFNLSENDKFTMLSGI----AHDPIqrdMFTPLFLG 488
Cdd:cd05967 227 V--AATDPLYilYTSGTTGKPKGVVrdngGHAVALNWS---MRNIYGIKPGDVWWAASDVgwvvGHSYI---VYGPLLHG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 489 AQLLIPTSDDIGTPGKLAEW--MQTYGatVTHLTpamgqllsaQATKEIPSLHHAFFVGDILTKRDCLRLQTI------- 559
Cdd:cd05967 299 ATTVLYEGKPVGTPDPGAFWrvIEKYQ--VNALF---------TAPTAIRAIRKEDPDGKYIKKYDLSSLRTLflagerl 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 560 -------AQN---VNIINMYGTTETQRAVSyfeIPSRAQDstflevQKDIMP--AGKGM--HNVQLLvvnrHDRSKTCAI 625
Cdd:cd05967 368 dpptlewAENtlgVPVIDHWWQTETGWPIT---ANPVGLE------PLPIKAgsPGKPVpgYQVQVL----DEDGEPVGP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 626 GEVGEIYVRAAglaeqyrgqpdlnkekfVPNWFVsPSKWveedkkiSKDEPWREFYLGPRDRLYRTGDLGRYLPTGDCEV 705
Cdd:cd05967 435 NELGNIVIKLP-----------------LPPGCL-LTLW-------KNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFI 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 706 SGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKET 761
Cdd:cd05967 490 MGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG 545
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
276-737 |
1.86e-11 |
|
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: 68.01 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 276 QTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGAtfsVIDPAYP--PARQNVYlqvakpa 353
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA---VPVPIYPtsSAEQIAY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 354 gliVLEKAGVLDQLVEDyiknelslvsrisnlkieadgnvlggdvdgkdalydyqqfktrrtgvlvgPDSNPTLSFTSGS 433
Cdd:cd05907 72 ---ILNDSEAKALFVED--------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 434 EGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKF-TMLSgIAHDPIQR-DMFTPLFLGAQLLIPTSDDIGTPGkLAEWMQT 511
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLPATEGDRHlSFLP-LAHVFERRaGLYVPLLAGARIYFASSAETLLDD-LSEVRPT 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 512 YGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDC------LRLQTIAQ--NVNIINMYGTTETQRAVSYfei 583
Cdd:cd05907 177 VFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAVGGRLRFAASggaplpAELLHFFRalGIPVYEGYGLTETSAVVTL--- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 584 pSRAQDSTFLEVQKdimpAGKGMHnvqllvvnrhdrsktCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPN-WFvsps 662
Cdd:cd05907 254 -NPPGDNRIGTVGK----PLPGVE---------------VRIADDGEILVRGPNVMLGYYKNPEATAEALDADgWL---- 309
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 663 kwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADD-QVKIRGFRIELGEIDTHISRHPLIRQ 737
Cdd:cd05907 310 ---------------------------HTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQ 358
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
270-444 |
3.21e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 67.61 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 270 FLNPNSQtRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQV 349
Cdd:PRK04319 65 YLDASRK-EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 350 AKPAGLIVLEKagvldqLVEDYIKNELSLVSRIsnLKIEADGNVLGGDVDGKDALydyQQFKTRRTGVLVGPDSNPTLSF 429
Cdd:PRK04319 144 SEAKVLITTPA------LLERKPADDLPSLKHV--LLVGEDVEEGPGTLDFNALM---EQASDEFDIEWTDREDGAILHY 212
|
170
....*....|....*
gi 254566307 430 TSGSEGIPKGVLGRH 444
Cdd:PRK04319 213 TSGSTGKPKGVLHVH 227
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
986-1186 |
4.13e-11 |
|
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: 64.63 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERDLDVqvyahvrakdeeSGLERLRNTGkvygiwNEEWTSRIKVVIADLS-KDKLglsgEK 1064
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEKGYEV------------IGLDRLTSAS------NTARLADLRFVEGDLTdRDAL----EK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 YAELANtIDLIIHNGALVHW----VYPySKLRDANVISTINVLNLAASGKPKQFGFVSSTSTldtehYitlsdtlteqGE 1140
Cdd:pfam01370 59 LLADVR-PDAVIHLAAVGGVgasiEDP-EDFIEANVLGTLNLLEAARKAGVKRFLFASSSEV-----Y----------GD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254566307 1141 -DGIPESDDLLGSSKGLGTGYGQSKWAAEYIIRRAFER-GLRGAIIRP 1186
Cdd:pfam01370 122 gAEIPQEETTLTGPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRL 169
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
278-828 |
5.21e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.93 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQ-IDQASNIVGnyLVHT-GIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQnvylqvakpagL 355
Cdd:PRK06188 36 TRLTYGQlADRISRYIQ--AFEAlGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH-----------A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 356 IVLEKAGVlDQLVED---YIKNELSLVSRISNLKieadgNVLG-GDV-DGKDALYDYQQFKTRRTGVLVGPDSNPTLSFT 430
Cdd:PRK06188 103 YVLEDAGI-STLIVDpapFVERALALLARVPSLK-----HVLTlGPVpDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 431 SGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHdpIQRDMFTP-LFLGAQLLIPTSDDigtPGKLAEWM 509
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVLAKFD---PAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 510 QTYGATVTHLTPAMgqllsaqatkeIPSL--HHAffvgdiLTKRDCLRLQTI------------AQNVNII-----NMYG 570
Cdd:PRK06188 252 EEQRITATFLVPTM-----------IYALldHPD------LRTRDLSSLETVyygaspmspvrlAEAIERFgpifaQYYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 571 TTETQRAVSYfeIPSRAQDstfLEVQKDIMPAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRGQPDLNK 650
Cdd:PRK06188 315 QTEAPMVITY--LRKRDHD---PDDPKRLTSCGRPTPGLRVALLDEDGRE--VAQGEVGEICVRGPLVMDGYWNRPEETA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 651 EKFVPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHIS 730
Cdd:PRK06188 388 EAFRDGWL-------------------------------HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 731 RHPLIRQ-NVTLVRRDKDEEPIlISYVVPK--ETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASYA 807
Cdd:PRK06188 437 EHPAVAQvAVIGVPDEKWGEAV-TAVVVLRpgAAVDAA----------------------------ELQAHVKERKGSVH 487
|
570 580
....*....|....*....|.
gi 254566307 808 IPTIIVPMAKLPLNPNGKVDK 828
Cdd:PRK06188 488 APKQVDFVDSLPLTALGKPDK 508
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
254-764 |
6.85e-11 |
|
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: 66.49 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 254 NAEKFPDRTCVVetksflnpNSQT-RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFS 332
Cdd:cd05904 14 FASAHPSRPALI--------DAATgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 333 VIDPAYPP---ARQnvyLQVAKPAGLIV-------LEKAGVLDQLVEDYIKNELSlvsrISNLKIEADGnvlggdvdgkd 402
Cdd:cd05904 86 TANPLSTPaeiAKQ---VKDSGAKLAFTtaelaekLASLALPVVLLDSAEFDSLS----FSDLLFEADE----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 403 alYDYQQfktrrtgVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYyfpwMSKTFNLSENdkftmlSGIAHDpiQRDMF 482
Cdd:cd05904 148 --AEPPV-------VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIA----MVAQFVAGEG------SNSDSE--DVFLC 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 483 T-PLF--------------LGAQLLIPTSDDIgtpGKLAEWMQTYGatVTHLtPAMGQLLSAQATKEIPSlhhaffvgdi 547
Cdd:cd05904 207 VlPMFhiyglssfalgllrLGATVVVMPRFDL---EELLAAIERYK--VTHL-PVVPPIVLALVKSPIVD---------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 548 ltKRDCLRLQTI---------------AQ---NVNIINMYGTTETQRAVSyfeipsraqdSTFLEVQKDIMP--AGKGMH 607
Cdd:cd05904 271 --KYDLSSLRQImsgaaplgkelieafRAkfpNVDLGQGYGMTESTGVVA----------MCFAPEKDRAKYgsVGRLVP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 608 NVQLLVVNrHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFvpnwfvspskwveeDKkiskdEPWrefylgprdr 687
Cdd:cd05904 339 NVEAKIVD-PETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI--------------DK-----EGW---------- 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 688 lYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPEL 764
Cdd:cd05904 389 -LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSL 464
|
|
| CDP_TE_SDR_e |
cd05258 |
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ... |
986-1197 |
1.52e-10 |
|
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. 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: 187568 [Multi-domain] Cd Length: 337 Bit Score: 64.23 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERDLDVQVYAHVRAKDEESGLERLRNTGKvygiwneewTSRIKVVIADL-SKDKLglsgek 1064
Cdd:cd05258 3 VLITGGAGFIGSNLARFFLKQGWEVIGFDNLMRRGSFGNLAWLKANRE---------DGGVRFVHGDIrNRNDL------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yAELANTIDLIIHNGA--LVHWVY--PYSKLrDANVISTINVLNLAASGKPKQFGFVSSTSTL--DTEHYITLSDTLT-- 1136
Cdd:cd05258 68 -EDLFEDIDLIIHTAAqpSVTTSAssPRLDF-ETNALGTLNVLEAARQHAPNAPFIFTSTNKVygDLPNYLPLEELETry 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 1137 -----EQGEDGIPESDDLLGSSkglgTGYGQSKWAAEYIIR---RAFerGLRGAIIRPGYVTGHSRTGA 1197
Cdd:cd05258 146 elapeGWSPAGISESFPLDFSH----SLYGASKGAADQYVQeygRIF--GLKTVVFRCGCLTGPRQFGT 208
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
254-447 |
1.61e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.39 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 254 NAEKFPDRTCVVetksflnpNSQT-RTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFS 332
Cdd:PLN02246 32 RLSEFSDRPCLI--------DGATgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 333 VIDPAYPPARqnVYLQV-AKPAGLIVLEKAGVlDQLVEDYIKNELSLVS---------RISNLkIEADGNVLgGDVDgkd 402
Cdd:PLN02246 104 TANPFYTPAE--IAKQAkASGAKLIITQSCYV-DKLKGLAEDDGVTVVTiddppegclHFSEL-TQADENEL-PEVE--- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254566307 403 alydyqqfktrrtgvlVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 447
Cdd:PLN02246 176 ----------------ISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
986-1235 |
1.89e-10 |
|
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. 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. 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: 187538 [Multi-domain] Cd Length: 301 Bit Score: 63.83 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERdlDVQVYAHVRAKDEESGL-ERLRNTGKvygiwneewTSRIKVVIADLSKDKlglsgEK 1064
Cdd:cd05227 2 VLVTGATGFIASHIVEQLLKA--GYKVRGTVRSLSKSAKLkALLKAAGY---------NDRLEFVIVDDLTAP-----NA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 YAELANTIDLIIHNGALVHWVYPYSK--LRDANVISTINVLNLA-ASGKPKQFGFVSSTSTLDTEHYITLSDTLTEQged 1141
Cdd:cd05227 66 WDEALKGVDYVIHVASPFPFTGPDAEddVIDPAVEGTLNVLEAAkAAGSVKRVVLTSSVAAVGDPTAEDPGKVFTEE--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1142 giPESDDLLGSSKGLgTGYGQSKWAAEYIIRRAFERGLRG---AIIRPGYVTGHSRTGA--CNTDDFLLRMLkgcaeLGK 1216
Cdd:cd05227 143 --DWNDLTISKSNGL-DAYIASKTLAEKAAWEFVKENKPKfelITINPGYVLGPSLLADelNSSNELINKLL-----DGK 214
|
250 260
....*....|....*....|.
gi 254566307 1217 LPNISNTVN--MVPVDHVALV 1235
Cdd:cd05227 215 LPAIPPNLPfgYVDVRDVADA 235
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
249-440 |
4.52e-10 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 63.97 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 249 DIFSDNAEKFPDRTCVVETKsflnpNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAG 328
Cdd:COG1022 15 DLLRRRAARFPDRVALREKE-----DGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 329 ATfSVidPAYP--PARQNVY-LQVAKPAGLIVlEKAGVLDQLVEdyIKNELSLVSRIsnlkIEADGNVLGGDVD------ 399
Cdd:COG1022 90 AV-TV--PIYPtsSAEEVAYiLNDSGAKVLFV-EDQEQLDKLLE--VRDELPSLRHI----VVLDPRGLRDDPRllslde 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254566307 400 ----GKDALYDyQQFKTRRTGvlVGPDSNPTLSFTSGSEGIPKGV 440
Cdd:COG1022 160 llalGREVADP-AELEARRAA--VKPDDLATIIYTSGTTGRPKGV 201
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
419-831 |
4.78e-10 |
|
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: 63.52 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 419 VGPDSNPTLSFTSGSEGIPKGVL---GRHFSLAyyfpwMSKTFNL--SENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLI 493
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQqtfGNHWWSA-----IGSALNLglTEDDNWLCALPLFHISGLSILMRSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 494 PTSDDigtPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEIPSLHHAFFVGDILTKRDCLRlQTIAQNVNIINMYGTTE 573
Cdd:cd05912 149 VDKFD---AEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLE-QCKEKGIPVYQSYGMTE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 574 TQravsyfeipSRAQDSTFLEVQKDIMPAGKGMHNVQLLVVNRHDRSKtcaigEVGEIYVRAAGLAEQYRGQPDLNKEKF 653
Cdd:cd05912 225 TC---------SQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPY-----EVGEILLKGPNVTKGYLNRPDATEESF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 654 VPNWFvspskwveedkkiskdepwrefylgprdrlyRTGDLGrYLPT-GDCEVSGRADDQVKIRGFRIELGEIDTHISRH 732
Cdd:cd05912 291 ENGWF-------------------------------KTGDIG-YLDEeGFLYVLDRRSDLIISGGENIYPAEIEEVLLSH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 733 PLIRQNVTLVRRDKDEEPILISYVVPKETPELEnfksssddlddlndpivkslllyrelikDLKAHLKKTLASYAIPTII 812
Cdd:cd05912 339 PAIKEAGVVGIPDDKWGQVPVAFVVSERPISEE----------------------------ELIAYCSEKLAKYKVPKKI 390
|
410
....*....|....*....
gi 254566307 813 VPMAKLPLNPNGKVDKPKL 831
Cdd:cd05912 391 YFVDELPRTASGKLLRHEL 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
278-831 |
1.10e-09 |
|
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: 62.50 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQIDQASNIVGNYLVHTGIKR-GDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAgli 356
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARIT--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 357 vlekagvldqlvedyiknelslvsrisnlkieadgnvlggdvdgkDALYDYQqfktrrtgvLVGPDSNPTLSFTSGSEGI 436
Cdd:cd05958 86 ---------------------------------------------VALCAHA---------LTASDDICILAFTSGTTGA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 437 PKGVLGRHFS-LAYYFPWMSKTFNLSENDKFTMLSGIAhdpiqrdmFT---------PLFLGAQ-LLIPTSddigTPGKL 505
Cdd:cd05958 112 PKATMHFHRDpLASADRYAVNVLRLREDDRFVGSPPLA--------FTfglggvllfPFGVGASgVLLEEA----TPDLL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 506 AEWMQTYGATVTHLTP----AMGQLLSAQAtKEIPSLHHAFFVGDILTKrDCLRLQTIAQNVNIINMYGTTETqravsyF 581
Cdd:cd05958 180 LSAIARYKPTVLFTAPtayrAMLAHPDAAG-PDLSSLRKCVSAGEALPA-ALHRAWKEATGIPIIDGIGSTEM------F 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 582 EI-PSRAQDstflevqkDIMPA--GKGMHNVQLLVVNrhDRSKTCAIGEVGEIYVRAAglaEQYRGQPDLNKEKFVPN-W 657
Cdd:cd05958 252 HIfISARPG--------DARPGatGKPVPGYEAKVVD--DEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGgW 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 658 FVspskwveedkkiskdepwrefylgprdrlyrTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQ 737
Cdd:cd05958 319 NI-------------------------------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAE 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 738 NVTLVRRDKDEEPILISYVVPKetPElenfksssddldDLNDPIvkslllyreLIKDLKAHLKKTLASYAIPTIIVPMAK 817
Cdd:cd05958 368 CAVVGHPDESRGVVVKAFVVLR--PG------------VIPGPV---------LARELQDHAKAHIAPYKYPRAIEFVTE 424
|
570
....*....|....
gi 254566307 818 LPLNPNGKVDKPKL 831
Cdd:cd05958 425 LPRTATGKLQRFAL 438
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
281-735 |
2.18e-09 |
|
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: 61.34 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 281 TYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLEK 360
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 361 agvLDQLvedyiknelslvsrisnlkieadgnvlggdvdgkdALYDYqqfktrrtgvlvgpdsnptlsfTSGSEGIPKGV 440
Cdd:cd05935 83 ---LDDL-----------------------------------ALIPY----------------------TSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 441 LGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHDP-IQRDMFTPLFLGAQLLIPTSDDIGTpgkLAEWMQTYGATV-TH 518
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTgFVGSLNTAVYVGGTYVLMARWDRET---ALELIEKYKVTFwTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 519 LTPAMGQLLSAQ--ATKEIPSLH--------HAFFVGDILTKRDCLRLQTIaqnvniinmYGTTETQRAVSYFeiPSRAQ 588
Cdd:cd05935 180 IPTMLVDLLATPefKTRDLSSLKvltgggapMPPAVAEKLLKLTGLRFVEG---------YGLTETMSQTHTN--PPLRP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 589 DSTFLevqkdimpaGKGMHNVQLLVVNRHDrSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVpnwfvspskwveed 668
Cdd:cd05935 249 KLQCL---------GIP*FGVDARVIDIET-GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI-------------- 304
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 669 kkiskdepwrefYLGPRdRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLI 735
Cdd:cd05935 305 ------------EIKGR-RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI 358
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
255-698 |
2.55e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.45 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 255 AEKFPDRTCVVETKSFLNPNSQT-RTFTYKQIDQASNIVGNYLVHTGIKRGD--VVMIYAyrGVDLMVAVMGVLKAGATF 331
Cdd:PRK09274 16 AQERPDQLAVAVPGGRGADGKLAyDELSFAELDARSDAIAHGLNAAGIGRGMraVLMVTP--SLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 332 SVIDPAYppARQNVY--LQVAKPAGLIVLEKAGVLDQLvedYIKNELSLVSRISnlkieADGNVLGG-----DVDGKDAL 404
Cdd:PRK09274 94 VLVDPGM--GIKNLKqcLAEAQPDAFIGIPKAHLARRL---FGWGKPSVRRLVT-----VGGRLLWGgttlaTLLRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 405 YDYQqfktrrtGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFnlsendkftmlsGIAHDpiQRDMFT- 483
Cdd:PRK09274 164 APFP-------MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDY------------GIEPG--EIDLPTf 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 484 PLF------LGAQLLIPTSD-------DigtPGKLAEWMQTYGATVTHLTPA-MGQLLSAQATKEI--PSLHHAFFVGDI 547
Cdd:PRK09274 223 PLFalfgpaLGMTSVIPDMDptrpatvD---PAKLFAAIERYGVTNLFGSPAlLERLGRYGEANGIklPSLRRVISAGAP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 548 LTKRDCLRLQTI-AQNVNIINMYGTTEtqrAVSYFEIPSRAQdstfLEVQKDIMPAGKG------MHNVQLLVVNRHDR- 619
Cdd:PRK09274 300 VPIAVIERFRAMlPPDAEILTPYGATE---ALPISSIESREI----LFATRAATDNGAGicvgrpVDGVEVRIIAISDAp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 620 ------SKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEkfvpnwfvspskwveedKKISKDEpwrefylgpRDRLYRTGD 693
Cdd:PRK09274 373 ipewddALRLATGEIGEIVVAGPMVTRSYYNRPEATRL-----------------AKIPDGQ---------GDVWHRMGD 426
|
....*
gi 254566307 694 LGrYL 698
Cdd:PRK09274 427 LG-YL 430
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
279-746 |
2.63e-09 |
|
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: 61.22 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 279 TFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATfsvidpaypparqNVylqvakpaglivl 358
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-------------DV------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 359 ekagvldqlvedyiknelslvsrisnlkieadgnVLGGDVDGKDALYDYQQfkTRRTGVLV--GPDSNPTLSFTSGSEGI 436
Cdd:cd17640 59 ----------------------------------VRGSDSSVEELLYILNH--SESVALVVenDSDDLATIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 437 PKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHdPIQRDMFTPLFL--GAQLL--IPT-SDDigtpgkLAEWMQT 511
Cdd:cd17640 103 PKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWH-SYERSAEYFIFAcgCSQAYtsIRTlKDD------LKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 512 YGATVTHLTPAMGQLLSAQATKEIPS---LHHAFFVGDILTKRDC------LRLQTI--AQNVNIINMYGTTETQRAVSY 580
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIkqfLFLFFLSGGIFKFGISgggalpPHVDTFfeAIGIEVLNGYGLTETSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 581 FEIPSRAQDStflevqkdimpAGKGMHNVQLLVVNrHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPdlnkekfvpnwfvs 660
Cdd:cd17640 256 RRLKCNVRGS-----------VGRPLPGTEIKIVD-PEGNVVLPPGEKGIVWVRGPQVMKGYYKNP-------------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 661 pskwvEEDKKISKDEPWrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIR-GFRIELGEIDTHISRHPLIrQNV 739
Cdd:cd17640 310 -----EATSKVLDSDGW-----------FNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFI-EQI 372
|
....*..
gi 254566307 740 TLVRRDK 746
Cdd:cd17640 373 MVVGQDQ 379
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
247-466 |
3.21e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 61.43 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALL---------FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAyppARQNVY---LQVAKPAGLIVLEKagvLDQLVEDyIKNELSLVSRISnLKIEADGNVLGGDVDGKDA 403
Cdd:PRK08279 110 LGAVVALLNTQ---QRGAVLahsLNLVDAKHLIVGEE---LVEAFEE-ARADLARPPRLW-VAGGDTLDDPEGYEDLAAA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 404 LYDYQQFKTRRTGVLVGPDsnPTLS-FTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKF 466
Cdd:PRK08279 182 AAGAPTTNPASRSGVTAKD--TAFYiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVL 243
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
6-209 |
3.92e-09 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 60.74 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 6 LNYWANILDG--PTLSVLP---------RDYNRPVAGKVIEANKTFDISDIlpflnkANEPSVTQFTAPLAVFAVLVYRL 74
Cdd:cd20483 191 LDFWKEKLEGipDASKLLPfakaerppvKDYERSTVEATLDKELLARMKRI------CAQHAVTPFMFLLAAFRAFLYRY 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 75 TGDDDIVIL-TDSpkkqNLP----------FV----VRLQVDPSKSFVDVSKQVGEQYLESLE-RATPLKDIVTHLKESK 138
Cdd:cd20483 265 TEDEDLTIGmVDG----DRPhpdfddlvgfFVnmlpIRCRMDCDMSFDDLLESTKTTCLEAYEhSAVPFDYIVDALDVPR 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 139 QlPNYPPIFRLSF--QTAKKVQQLST----------------------LVEGSTRDLAIFLEnntsiniyYNSLLYTHNR 194
Cdd:cd20483 341 S-TSHFPIGQIAVnyQVHGKFPEYDTgdfkftdydhydiptacdialeAEEDPDGGLDLRLE--------FSTTLYDSAD 411
|
250
....*....|....*
gi 254566307 195 IAYFSQQFSSFIDEV 209
Cdd:cd20483 412 MERFLDNFVTFLTSV 426
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
985-1243 |
4.16e-09 |
|
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: 59.75 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLdvqvyAHVRAKDEESGLERLRNtgkvygiWNEEWTSRIKVVIADLSKDKLGLSGek 1064
Cdd:cd05241 1 SVLVTGGSGFFGERLVKQLLERGG-----TYVRSFDIAPPGEALSA-------WQHPNIEFLKGDITDRNDVEQALSG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yaelantIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEhyitlSDTLTEQGEDGIP 1144
Cdd:cd05241 67 -------ADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFGG-----QNIHNGDETLPYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1145 ESDDLLgsskglgtgYGQSKWAAEYIIRRAFER-GLRGAIIRPGYVTGhsrtgacNTDDFLLRMLKGCAELG-KLPNIS- 1221
Cdd:cd05241 135 PLDSDM---------YAETKAIAEIIVLEANGRdDLLTCALRPAGIFG-------PGDQGLVPILFEWAEKGlVKFVFGr 198
|
250 260
....*....|....*....|....*.
gi 254566307 1222 --NTVNMVPVDHV--ALVVTASSLHP 1243
Cdd:cd05241 199 gnNLVDFTYVHNLahAHILAAAALVK 224
|
|
| SDR_e_a |
cd05226 |
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
986-1202 |
4.61e-09 |
|
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: 57.41 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERdlDVQVYAHVRakdeesglerlrntgKVYGIWNEEWTsRIKVVIADLSKDKLglsgekY 1065
Cdd:cd05226 1 ILILGATGFIGRALARELLEQ--GHEVTLLVR---------------NTKRLSKEDQE-PVAVVEGDLRDLDS------L 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1066 AELANTIDLIIHngaLVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHyitlsdtlteqgEDGIPE 1145
Cdd:cd05226 57 SDAVQGVDVVIH---LAGAPRDTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDLH------------EETEPS 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 1146 SDDLlgsskglgtgYGQSKWAAEYIIRrafERGLRGAIIRPGYVTG-HSRTGACNTDD 1202
Cdd:cd05226 122 PSSP----------YLAVKAKTEAVLR---EASLPYTIVRPGVIYGdLARAIANAVVT 166
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
247-444 |
7.71e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 59.90 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:PRK07798 5 IADLFEAVADAVPDRVALV---------CGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 327 AGATFSVIDPAYPPaRQNVYL-QVAKPAGLI--------VlekAGVLDQLvedyikNELSLVSRISNlkiEADGNVLGGD 397
Cdd:PRK07798 76 ARAVPVNVNYRYVE-DELRYLlDDSDAVALVyerefaprV---AEVLPRL------PKLRTLVVVED---GSGNDLLPGA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254566307 398 VDGKDALydyqqfKTRRTGVLVGPDSNPTLSF--TSGSEGIPKGVLGRH 444
Cdd:PRK07798 143 VDYEDAL------AAGSPERDFGERSPDDLYLlyTGGTTGMPKGVMWRQ 185
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
988-1191 |
7.88e-09 |
|
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: 59.06 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 988 LTGATGFLGSYILKDLLERdldvqvyahvrakDEEsgLERLRNTGKVYGIWNEE--WTSRIKVVIADLSKDKLGLSGEKY 1065
Cdd:cd09811 4 VTGGGGFLGQHIIRLLLER-------------KEE--LKEIRVLDKAFGPELIEhfEKSQGKTYVTDIEGDIKDLSFLFR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1066 AelANTIDLIIHNGALVHWVYP--YSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHYitlsDTLTEQGEDGI 1143
Cdd:cd09811 69 A--CQGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFK----GRPIFNGVEDT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254566307 1144 PesddLLGSSKglgTGYGQSKWAAEYIIRRAFERGLRG------AIIRPGYVTG 1191
Cdd:cd09811 143 P----YEDTST---PPYASSKLLAENIVLNANGAPLKQggylvtCALRPMYIYG 189
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
236-831 |
1.07e-08 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 59.51 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 236 ANLDWSGYRgAIQDIFSDNAEKFPDRTCVvetksflnpNSQTRTFTYKQIDQASNIVGNYLV-HTGIKRGDVVMIYAYRG 314
Cdd:PRK08751 17 AEIDLEQFR-TVAEVFATSVAKFADRPAY---------HSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 315 VDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLEKAG------VLDQLVEDYIKNEL---------SLV 379
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGttvqqvIADTPVKQVITTGLgdmlgfpkaALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 380 SRISN-LKIEADGNVLGGDVDGKDALydYQQFKTRRTGVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYF----PWM 454
Cdd:PRK08751 167 NFVVKyVKKLVPEYRINGAIRFREAL--ALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqahQWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 455 SKTFNLSENDKFTMLSGIAHDPIQRDMFTPLFL---GAQLLIPTSDDIgtPGKLAEWMQTYGATVTHLTPAMGQLLSAQA 531
Cdd:PRK08751 245 AGTGKLEEGCEVVITALPLYHIFALTANGLVFMkigGCNHLISNPRDM--PGFVKELKKTRFTAFTGVNTLFNGLLNTPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 532 TKEI--PSLHHAFFVGDILTKRDCLRLQTIAqNVNIINMYGTTETQRAVSYFEIpsraqdsTFLEVQKDImpagkGMHNV 609
Cdd:PRK08751 323 FDQIdfSSLKMTLGGGMAVQRSVAERWKQVT-GLTLVEAYGLTETSPAACINPL-------TLKEYNGSI-----GLPIP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 610 QLLVVNRHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPdlnkekfvpnwfvspskwvEEDKKISKDEPWrefylgprdrlY 689
Cdd:PRK08751 390 STDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRP-------------------EETAKVMDADGW-----------L 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 690 RTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQnVTLVRRDKDEEPILISYVVPKETPELEnfks 769
Cdd:PRK08751 440 HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE-VAAVGVPDEKSGEIVKVVIVKKDPALT---- 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254566307 770 ssddlddlndpivkslllyrelIKDLKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK08751 515 ----------------------AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PLN02503 |
PLN02503 |
fatty acyl-CoA reductase 2 |
943-1106 |
1.30e-08 |
|
fatty acyl-CoA reductase 2
Pssm-ID: 215279 [Multi-domain] Cd Length: 605 Bit Score: 59.49 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 943 ESTSAGSDEQVVDYFQDAKDLVSS-----------QLLDSYKSRLALSNAELINI---------FLTGATGFLGSYILKD 1002
Cdd:PLN02503 59 ERSRVGSSQQHVAACRDAGSLVLSpngkgqpeiavKDLVPYGSSSAVEMADGIGIaeflrgknfLITGATGFLAKVLIEK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1003 LLERDLDV-QVYAHVRAKDEESGLERLRNT----------GKVYGIWNEEWTSRIKV-VIADLSKDKLGLSGEKYAELAN 1070
Cdd:PLN02503 139 ILRTNPDVgKIYLLIKAKDKEAAIERLKNEvidaelfkclQETHGKSYQSFMLSKLVpVVGNVCESNLGLEPDLADEIAK 218
|
170 180 190
....*....|....*....|....*....|....*.
gi 254566307 1071 TIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLA 1106
Cdd:PLN02503 219 EVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFA 254
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
985-1269 |
1.39e-08 |
|
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: 56.78 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERdlDVQVYAHVRAKDEESGLERLrntgkvygiwneewtsRIKVVIADLskdklglsgEK 1064
Cdd:COG0702 1 KILVTGATGFIGRRVVRALLAR--GHPVRALVRDPEKAAALAAA----------------GVEVVQGDL---------DD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 YAELANT---IDLIIHngaLVHwvYPYSKLRDANVISTINVLNLAASGKPKQFGFVSStstldtehyitlsdtlteqged 1141
Cdd:COG0702 54 PESLAAAlagVDAVFL---LVP--SGPGGDFAVDVEGARNLADAAKAAGVKRIVYLSA---------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1142 gipesddlLGSSKGLGTGYGQSKWAAEYIIRRAferGLRGAIIRPGYVTGhsrtgacNTDDFLLRMlkgcAELGK--LPN 1219
Cdd:COG0702 107 --------LGADRDSPSPYLRAKAAVEEALRAS---GLPYTILRPGWFMG-------NLLGFFERL----RERGVlpLPA 164
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 254566307 1220 ISNTVNMVPVDHVALVVTASSLHPTAEEGhcVVQVTGHPRIRFNEFLNAL 1269
Cdd:COG0702 165 GDGRVQPIAVRDVAEAAAAALTDPGHAGR--TYELGGPEALTYAELAAIL 212
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
3-213 |
6.16e-08 |
|
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: 56.61 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG-PTLSVLPRDYNRPVAGKVIEankTFDISD-----ILPFLnKANEPSVTQFTapLAVFAVLVYRLTG 76
Cdd:cd19533 186 ERDRAFWTEQFEDlPEPVSLARRAPGRSLAFLRR---TAELPPeltrtLLEAA-EAHGASWPSFF--IALVAAYLHRLTG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 77 DDDIVILT------DSPKKQNLPFVV-----RLQVDPSKSFVDVSKQVGEQyLESLERAT--PLKDIVTHLKESKQLP-- 141
Cdd:cd19533 260 ANDVVLGVpvmgrlGAAARQTPGMVAntlplRLTVDPQQTFAELVAQVSRE-LRSLLRHQryRYEDLRRDLGLTGELHpl 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 142 -----NY-PPIFRLSFQTAKKVQQlsTLVEGSTRDLAIFL-----ENNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVN 210
Cdd:cd19533 339 fgptvNYmPFDYGLDFGGVVGLTH--NLSSGPTNDLSIFVydrddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAA 416
|
...
gi 254566307 211 KAP 213
Cdd:cd19533 417 ADP 419
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
276-809 |
6.30e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 57.06 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 276 QTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGL 355
Cdd:PRK06164 32 EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 356 IV------LEKAGVLDQLVEDyiknELSLVSRISNLKIEAD---GNVLGGDVDGKDALYdyqQFKTRRTGVLVGPDSNPT 426
Cdd:PRK06164 112 VVwpgfkgIDFAAILAAVPPD----ALPPLRAIAVVDDAADatpAPAPGARVQLFALPD---PAPPAAAGERAADPDAGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 427 LSFT-SGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDK------------FTMLSGIAHDpiqrdmftplflGAQLLI 493
Cdd:PRK06164 185 LLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVllaalpfcgvfgFSTLLGALAG------------GAPLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 494 -PTSDDIGTPGKLAEwmqtygATVTHL---TPAMGQLL-SAQATKEIPSLHHaFFVGDILTKRDCLRLQTIAQNVNIINM 568
Cdd:PRK06164 253 ePVFDAARTARALRR------HRVTHTfgnDEMLRRILdTAGERADFPSARL-FGFASFAPALGELAALARARGVPLTGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 569 YGTTETQRAVSyfeipsrAQDSTfLEVQKDIMPAGKGMH-NVQLLVVNRHDRSkTCAIGEVGEIYVRAAGLAEQYRGQPD 647
Cdd:PRK06164 326 YGSSEVQALVA-------LQPAT-DPVSVRIEGGGRPASpEARVRARDPQDGA-LLPDGESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 648 LNKEKFVPnwfvspskwveedkkiskdepwrefylgprDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDT 727
Cdd:PRK06164 397 ATARALTD------------------------------DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 728 HISRHPLIRqNVTLVRRDKDEEPILISYVVPKETPELENfksssddlddlndpivkslllyreliKDLKAHLKKTLASYA 807
Cdd:PRK06164 447 ALEALPGVA-AAQVVGATRDGKTVPVAFVIPTDGASPDE--------------------------AGLMAACREALAGFK 499
|
..
gi 254566307 808 IP 809
Cdd:PRK06164 500 VP 501
|
|
| UDP_G4E_2_SDR_e |
cd05234 |
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
985-1196 |
9.15e-08 |
|
UDP-glucose 4 epimerase, subgroup 2, extended (e) 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. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187545 [Multi-domain] Cd Length: 305 Bit Score: 55.38 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYahvrakDEESglerlrnTGKVYGIWNEEWTSRIKVVIADLSKDKLGLSGEk 1064
Cdd:cd05234 1 RILVTGGAGFIGSHLVDRLLEEGNEVVVV------DNLS-------SGRRENIEPEFENKAFRFVKRDLLDTADKVAKK- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yaelanTIDLIIHNGAlvhwvypYSKLR----------DANVISTINVLNLAASGKPKQFGFvSSTSTLdtehYitlsdt 1134
Cdd:cd05234 67 ------DGDTVFHLAA-------NPDVRlgatdpdidlEENVLATYNVLEAMRANGVKRIVF-ASSSTV----Y------ 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 1135 lteqGE-DGIPESDDllGSSKGLGTgYGQSKWAAE-YIIRRAFERGLRGAIIRPGYVTGHSRTG 1196
Cdd:cd05234 123 ----GEaKVIPTPED--YPPLPISV-YGASKLAAEaLISAYAHLFGFQAWIFRFANIVGPRSTH 179
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
609-834 |
1.13e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 56.15 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 609 VQLLVVNRHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEKFVPN-WFvspskwveedkkiskdepwrefylgprdr 687
Cdd:PRK07787 302 VETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADgWF----------------------------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 688 lyRTGDLGRYLPTGDCEVSGR-ADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELEn 766
Cdd:PRK07787 353 --RTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAAD- 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 767 fksssddlddlndpivkslllyrELIkdlkAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFP 834
Cdd:PRK07787 430 -----------------------ELI----DFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
259-575 |
1.36e-07 |
|
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: 55.90 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 259 PDRTCVVETKsflnPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAY 338
Cdd:cd05921 9 PDRTWLAERE----GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 339 PPARQNVylqvAKPAGLIVLEKAGVLdqLVEDYIKNELSLVSrisnlkIEADGN---VLGGDVDGKDALYDYQQFKTRRT 415
Cdd:cd05921 85 SLMSQDL----AKLKHLFELLKPGLV--FAQDAAPFARALAA------IFPLGTplvVSRNAVAGRGAISFAELAATPPT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 416 GVL------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLA---------YYFP---------WMSKTFNLSENDKFTMLsg 471
Cdd:cd05921 153 AAVdaafaaVGPDTVAKFLFTSGSTGLPKAVINTQRMLCanqamleqtYPFFgeeppvlvdWLPWNHTFGGNHNFNLV-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 472 iahdpiqrdmftpLFLGAQLLI----PTSDDIGTPGK-LAEWMQTYGATV----THLTPAMGQlLSAQATKEIPSLHHAF 542
Cdd:cd05921 231 -------------LYNGGTLYIddgkPMPGGFEETLRnLREISPTVYFNVpagwEMLVAALEK-DEALRRRFFKRLKLMF 296
|
330 340 350
....*....|....*....|....*....|....*...
gi 254566307 543 FVG-----DILTKRDCLRLQTIAQNVNIINMYGTTETQ 575
Cdd:cd05921 297 YAGaglsqDVWDRLQALAVATVGERIPMMAGLGATETA 334
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
565-834 |
1.71e-07 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 55.53 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 565 IINMYGTTETqravsyfeipSRAQDSTFLEVQKDIMPAGKGMHNVQLLVVNRHDRSktCAIGEVGEIYVRAAGLAEQYRG 644
Cdd:PRK13382 340 IYNNYNATEA----------GMIATATPADLRAAPDTAGRPAEGTEIRILDQDFRE--VPTGEVGTIFVRNDTQFDGYTS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 645 QPDlnkekfvpnwfvspskwveedkkiskdepwREFYLGprdrLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGE 724
Cdd:PRK13382 408 GST------------------------------KDFHDG----FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 725 IDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKE----TPElenfksssddlddlndpivkslllyrelikDLKAHLK 800
Cdd:PRK13382 454 VEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPgasaTPE------------------------------TLKQHVR 503
|
250 260 270
....*....|....*....|....*....|....
gi 254566307 801 KTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPFP 834
Cdd:PRK13382 504 DNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
3-213 |
1.94e-07 |
|
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: 55.35 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG-PTLSVLPRDYNRPVAGKVIEANKTFDISDIL--PFLNKANEPSVTQFTAPLAVFAVLVYRLTGDDD 79
Cdd:cd19538 189 ARQLAYWKKQLAGlPDEIELPTDYPRPAESSYEGGTLTFEIDSELhqQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 80 IVIltDSP----KKQNLP-----FV--VRLQVDPS--KSFVDVSKQVGEQYLESLERA-TPLKDIVTHLKESKQlPNYPP 145
Cdd:cd19538 269 IPI--GSPvagrNDDSLEdlvgfFVntLVLRTDTSgnPSFRELLERVKETNLEAYEHQdIPFERLVEALNPTRS-RSRHP 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 146 IFR--LSFQTAK----KVQQLSTLVE----GSTR-DLAI-FLENNTSIN-------IYYNSLLYTHNRIAYFSQQFSSFI 206
Cdd:cd19538 346 LFQimLALQNTPqpslDLPGLEAKLElrtvGSAKfDLTFeLREQYNDGTpngiegfIEYRTDLFDHETIEALAQRYLLLL 425
|
....*..
gi 254566307 207 DEVNKAP 213
Cdd:cd19538 426 ESAVENP 432
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
6-213 |
3.05e-07 |
|
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: 54.72 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 6 LNYWANILDG-PTLSVLPRDYNRP-VAG-KVIEANKTFDISDILPFLNKANEPSVTQFTAPLAVFAVLVYRLTGDDDIVI 82
Cdd:cd19066 190 LAYWTSYLHGlPPPLPLPKAKRPSqVASyEVLTLEFFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 83 LT-----DSPKKQNL------PFVVRLQVDPSKSFVDVSKQVGEQYLESLERA-TPLKDIVTHLKESKQLPNyPPIFRLS 150
Cdd:cd19066 270 GLtflnrPDEAVEDTiglflnLLPLRIDTSPDATFPELLKRTKEQSREAIEHQrVPFIELVRHLGVVPEAPK-HPLFEPV 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 151 FQTAKKVQQLS------------TLVEGSTRDLAIFL----ENNTSINIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAP 213
Cdd:cd19066 349 FTFKNNQQQLGktggfifttpvyTSSEGTVFDLDLEAsedpDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
674-928 |
3.68e-07 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 55.09 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 674 DEPWREFYLGPRDRLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILI 753
Cdd:COG3319 366 AALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 754 SYVVPKETPELEnfksssddlddlndpivkslllyrelikdlKAHLKKTLASYAIPTIIVPMAKLPLNPNGKVDKPKLPF 833
Cdd:COG3319 446 AAVVAAAALAAA------------------------------ALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 834 PDTVQLAAVAQKSSAEvddsefTTTELQIKDLWLQVLPnpPASISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTI 913
Cdd:COG3319 496 AAPAAAAAAAAAPAPA------AALELALALLLLLLLG--LGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLAL 567
|
250
....*....|....*
gi 254566307 914 FKHPTVKLFAAEVDR 928
Cdd:COG3319 568 LLAPTLAALAAALAA 582
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
848-928 |
1.13e-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: 48.02 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 848 AEVDDSEFTTTELQ-IKDLWLQVL-PNPPASISLEDSFFDLGGHSILATRMIFELRRKLAVDLPLGTIFKHPTVKLFAAE 925
Cdd:smart00823 2 AALPPAERRRLLLDlVREQVAAVLgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
|
...
gi 254566307 926 VDR 928
Cdd:smart00823 82 LAA 84
|
|
| FR_SDR_e |
cd08958 |
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ... |
989-1234 |
1.68e-06 |
|
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. 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: 187661 [Multi-domain] Cd Length: 293 Bit Score: 51.42 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 989 TGATGFLGSYILKDLLERDLdvQVYAHVRAKDEESGLERLRNtgkvygiwNEEWTSRIKVVIADLSKDK------LGLSG 1062
Cdd:cd08958 4 TGASGFIGSWLVKRLLQRGY--TVRATVRDPGDEKKVAHLLE--------LEGAKERLKLFKADLLDYGsfdaaiDGCDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1063 EKYaeLANTIDLIIhngalvhwVYPYSKLRDANVISTINVLNLAA-SGKPKQFGFVSSTSTldtehyITLSDTLTEQGEd 1141
Cdd:cd08958 74 VFH--VASPVDFDS--------EDPEEEMIEPAVKGTLNVLEACAkAKSVKRVVFTSSVAA------VVWNPNRGEGKV- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1142 gIPESD----DLLgssKGLGTGYGQSKWAAEyiiRRAF----ERGLRGAIIRPGYVTGHSRTGACNTD-DFLLRMLKGCA 1212
Cdd:cd08958 137 -VDESCwsdlDFC---KKTKLWYALSKTLAE---KAAWefaeENGLDLVTVNPSLVVGPFLQPSLNSSsQLILSLLKGNA 209
|
250 260
....*....|....*....|..
gi 254566307 1213 ELgkLPNisNTVNMVPVDHVAL 1234
Cdd:cd08958 210 EM--YQN--GSLALVHVDDVAD 227
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
421-827 |
1.96e-06 |
|
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: 51.95 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 421 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHD-PIQRDMFTPLFLGAQLLI---PTS 496
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSfGLTGCLWLPLLSGIKVVFhpnPLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 497 ddigtPGKLAEWMQTYGATVTHLTPA-MGQLLSAQATKEIPSLHHAFFVGDILtkRDCLRlqTIAQN---VNIINMYGTT 572
Cdd:cd05909 226 -----YKKIPELIYDKKATILLGTPTfLRGYARAAHPEDFSSLRLVVAGAEKL--KDTLR--QEFQEkfgIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 573 ETQRAVSyfeipsraqdstfleVQKDIMPA-----GKGMHNVQLLVVNRHDRSKTcAIGEVGEIYVRAAGLAEQYRGQPD 647
Cdd:cd05909 297 ECSPVIS---------------VNTPQSPNkegtvGRPLPGMEVKIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 648 LNKEKFVPNWfvspskwveedkkiskdepwrefylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDT 727
Cdd:cd05909 361 LTSFAFGDGW-------------------------------YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIED 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 728 HISRHpLIRQN---VTLVRRDKDEEPILISYVVPKETPElenfksssddlddlndpivkslllyrelikDLKAHLKKT-L 803
Cdd:cd05909 410 ILSEI-LPEDNevaVVSVPDGRKGEKIVLLTTTTDTDPS------------------------------SLNDILKNAgI 458
|
410 420
....*....|....*....|....
gi 254566307 804 ASYAIPTIIVPMAKLPLNPNGKVD 827
Cdd:cd05909 459 SNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1-213 |
2.14e-06 |
|
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: 51.92 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1 MSEENLNYWANILDGPTLSVLP----RDYNRPVAGKVIEANKTFDISdilpflnkANEPSVTQFTAPLAVFAVLVYRLTG 76
Cdd:cd19542 168 SQEESLQYWRKYLQGASPCAFPslspKRPAERSLSSTRRSLAKLEAF--------CASLGVTLASLFQAAWALVLARYTG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 77 DDDIV---ILT----DSPKKQNL--PF----VVRLQVDPSKSFVDVSKQVGEQYLESLE-RATPLKDIVTHLKESKQLPN 142
Cdd:cd19542 240 SRDVVfgyVVSgrdlPVPGIDDIvgPCintlPVRVKLDPDWTVLDLLRQLQQQYLRSLPhQHLSLREIQRALGLWPSGTL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 143 YPPIFrlSFQTA----------KKVQQLSTLVEGSTRDLAIFLENNTS---INIYYNSLLYTHNRIAYFSQQFSSFIDEV 209
Cdd:cd19542 320 FNTLV--SYQNFeaspeselsgSSVFELSAAEDPTEYPVAVEVEPSGDslkVSLAYSTSVLSEEQAEELLEQFDDILEAL 397
|
....
gi 254566307 210 NKAP 213
Cdd:cd19542 398 LANP 401
|
|
| UDP_invert_4-6DH_SDR_e |
cd05237 |
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ... |
986-1119 |
4.75e-06 |
|
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: 49.92 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERDL-DVQVYAHvrakdEESGLERLRNTgkvygIWNEEWTSRIKVVIADL-SKDKLGLSGE 1063
Cdd:cd05237 5 ILVTGGAGSIGSELVRQILKFGPkKLIVFDR-----DENKLHELVRE-----LRSRFPHDKLRFIIGDVrDKERLRRAFK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1064 KYAelantIDLIIHNGALVHwV----YPYSKLRDANVISTINVLNLAASGKPKQFGFVSS 1119
Cdd:cd05237 75 ERG-----PDIVFHAAALKH-VpsmeDNPEEAIKTNVLGTKNVIDAAIENGVEKFVCIST 128
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
245-831 |
5.38e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 50.93 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 245 GAIQDIFSDNAEKFPDRTCVVETKsflnpnsQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGV 324
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRH-------QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 325 LKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLE--KAgvldqlvEDYIKNELSLVSRISNLKIEADG--------NVL 394
Cdd:PRK12583 91 ARIGAILVNINPAYRASELEYALGQSGVRWVICADafKT-------SDYHAMLQELLPGLAEGQPGALAcerlpelrGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 395 GGDVDGKDALYDYQQFKTRRTGVL----------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSEND 464
Cdd:PRK12583 164 SLAPAPPPGFLAWHELQARGETVSrealaerqasLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 465 K----------FTM----LSGIAHdpiqrdmftplflGAQLLIPTS--DDIGTPGKLAEwmqtYGATVTHLTPAM--GQL 526
Cdd:PRK12583 244 RlcvpvplyhcFGMvlanLGCMTV-------------GACLVYPNEafDPLATLQAVEE----ERCTALYGVPTMfiAEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 527 LSAQ-ATKEIPSLHHAffvgdILTKRDCLRlQTIAQNVNIINM------YGTTETQravsyfeiPSRAQDSTFLEVQKDI 599
Cdd:PRK12583 307 DHPQrGNFDLSSLRTG-----IMAGAPCPI-EVMRRVMDEMHMaevqiaYGMTETS--------PVSLQTTAADDLERRV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 600 MPAGKGMHNVQLLVVnrHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDLNKEkfvpnwfvspskwveedkKISKDEpWre 679
Cdd:PRK12583 373 ETVGRTQPHLEVKVV--DPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAE------------------SIDEDG-W-- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 680 fylgprdrlYRTGDLGRYLPTGDCEVSGRADDQVkIRGFR-IELGEIDTHISRHPLIRQ-NVTLVRRDKDEEPIlISYVV 757
Cdd:PRK12583 430 ---------MHTGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADvQVFGVPDEKYGEEI-VAWVR 498
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 758 --PKETPELENFksssddlddlndpivkslllyRELIKDLKAHLKktlasyaIPTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:PRK12583 499 lhPGHAASEEEL---------------------REFCKARIAHFK-------VPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-696 |
5.57e-06 |
|
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: 50.54 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 278 RTFTYKQIDQASNIVGNYLVHTGIKRG--DVVMIYAyrGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGL 355
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGmrAVLMVPP--GPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 356 IVLEKAgvldqlvedyiknelslvsrisnlkieadgnvlggdvdgkdalydyqqfktrrtgvlvgpDSNPTLSFTSGSEG 435
Cdd:cd05910 79 IGIPKA------------------------------------------------------------DEPAAILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 436 IPKGVLGRHFSLAyyfpwmsktfnlSENDKFTMLSGIAHDpiQRDMFT-PLF------LGAQLLIPTSDDI----GTPGK 504
Cdd:cd05910 99 TPKGVVYRHGTFA------------AQIDALRQLYGIRPG--EVDLATfPLFalfgpaLGLTSVIPDMDPTrparADPQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 505 LAEWMQTYGATVTHLTPAMGQLLS---AQATKEIPSLHHAFFVGDILTKRDCLRLQTI-AQNVNIINMYGTTEtqrAVSY 580
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLERVArycAQHGITLPSLRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGATE---ALPV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 581 FEIPSRAQDST----------------FLEVQKDIMPAGKGMhnvqllvVNRHDRSKTCAIGEVGEIYVRAAGLAEQYRG 644
Cdd:cd05910 242 SSIGSRELLATttaatsggagtcvgrpIPGVRVRIIEIDDEP-------IAEWDDTLELPRGEIGEITVTGPTVTPTYVN 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 254566307 645 QPDLNkekfvpnwfvSPSKWVEEDKKIskdepwrefylgprdrLYRTGDLGR 696
Cdd:cd05910 315 RPVAT----------ALAKIDDNSEGF----------------WHRMGDLGY 340
|
|
| PLN02996 |
PLN02996 |
fatty acyl-CoA reductase |
986-1106 |
6.51e-06 |
|
fatty acyl-CoA reductase
Pssm-ID: 215538 [Multi-domain] Cd Length: 491 Bit Score: 50.47 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGsyilKDLLERDLDVQ-----VYAHVRAKDEESGLERLRNT--GKV-YGIWNEEWTSRI------KVVI- 1050
Cdd:PLN02996 14 ILVTGATGFLA----KIFVEKILRVQpnvkkLYLLLRASDAKSATQRLHDEviGKDlFKVLREKLGENLnsliseKVTPv 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 1051 -ADLSKDKLGLSGEKYA-ELANTIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLA 1106
Cdd:PLN02996 90 pGDISYDDLGVKDSNLReEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFA 147
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
236-826 |
1.09e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 50.02 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 236 ANLDWSGYRgAIQDIFSDNAEKFPDRTCVVetksflnpnSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGV 315
Cdd:PRK07059 15 AEIDASQYP-SLADLLEESFRQYADRPAFI---------CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 316 DLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLIVLEK-AGVLDQLVEDyiknelslvSRISNLKIEADGNVL 394
Cdd:PRK07059 85 QYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENfATTVQQVLAK---------TAVKHVVVASMGDLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 395 G-----------------------GDVDGKDALYDYQQFKTRRtgVLVGPDSNPTLSFTSGSEGIPKGVLGRHFSL---- 447
Cdd:PRK07059 156 GfkghivnfvvrrvkkmvpawslpGHVRFNDALAEGARQTFKP--VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIvanv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 448 ----AYYFPWMSK-----------------TFNLSENDKFTMLSGiahdpiqrdmftplflGAQLLIPTSDDIgtPGKLA 506
Cdd:PRK07059 234 lqmeAWLQPAFEKkprpdqlnfvcalplyhIFALTVCGLLGMRTG----------------GRNILIPNPRDI--PGFIK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 507 EWMQtYGatvTHLTPAMGQLLSAQatkeipsLHHAFFvgdilTKRDCLRLQT-----------IAQN------VNIINMY 569
Cdd:PRK07059 296 ELKK-YQ---VHIFPAVNTLYNAL-------LNNPDF-----DKLDFSKLIVangggmavqrpVAERwlemtgCPITEGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 570 GTTETQRAVSyfeipsrAQDSTFLEVQKDImpagkGMHNVQLLVVNRHDRSKTCAIGEVGEIYVRAAGLAEQYRGQPDln 649
Cdd:PRK07059 360 GLSETSPVAT-------CNPVDATEFSGTI-----GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPD-- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 650 kekfvpnwfvspskwvEEDKKISKDEpwrefylgprdrLYRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHI 729
Cdd:PRK07059 426 ----------------ETAKVMTADG------------FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 730 SRHPLIRQNVTLVRRDKDEEPILISYVVPKEtPELENfksssddlddlndpivkslllyreliKDLKAHLKKTLASYAIP 809
Cdd:PRK07059 478 ASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-PALTE--------------------------EDVKAFCKERLTNYKRP 530
|
650
....*....|....*..
gi 254566307 810 TIIVPMAKLPLNPNGKV 826
Cdd:PRK07059 531 KFVEFRTELPKTNVGKI 547
|
|
| UDP_AE_SDR_e |
cd05256 |
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ... |
985-1210 |
1.21e-05 |
|
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187566 [Multi-domain] Cd Length: 304 Bit Score: 48.76 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVyahvrakdeesglerLRN--TGKVYGIwnEEWTSRIKVVIADLSKDKLGlsg 1062
Cdd:cd05256 1 RVLVTGGAGFIGSHLVERLLERGHEVIV---------------LDNlsTGKKENL--PEVKPNVKFIEGDIRDDELV--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1063 ekyAELANTIDLIIHNGALVhwVYPYS-----KLRDANVISTINVLNLAASGKPKQFGFVSSTSTLdtehyitlsdtlte 1137
Cdd:cd05256 61 ---EFAFEGVDYVFHQAAQA--SVPRSiedpiKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVY-------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1138 QGEDGIPESDDLLGSSKglgTGYGQSKWAAEYIIrRAFER--GLRGAIIR------PGYVTGHSRTGACNTddFLLRMLK 1209
Cdd:cd05256 122 GDPPYLPKDEDHPPNPL---SPYAVSKYAGELYC-QVFARlyGLPTVSLRyfnvygPRQDPNGGYAAVIPI--FIERALK 195
|
.
gi 254566307 1210 G 1210
Cdd:cd05256 196 G 196
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
57-147 |
1.38e-05 |
|
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: 49.38 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 57 VTQFTAPLAVFAVLVYRLTGDDDIVI-LTDS----PKKQN--------LPfvVRLQVDPSKSFVDVSKQVGEQYLESLER 123
Cdd:cd19532 239 VTPFHFYLAALQVLLARLLDVDDICIgIADAnrtdEDFMEtigfflnlLP--LRFRRDPSQTFADVLKETRDKAYAALAH 316
|
90 100
....*....|....*....|....*
gi 254566307 124 AT-PLKDIVTHLKESKQlPNYPPIF 147
Cdd:cd19532 317 SRvPFDVLLDELGVPRS-ATHSPLF 340
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
480-768 |
1.57e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.99 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 480 DMFT---PLFLGAQLL----IPTSddIGTPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKE-----IPSLHHAFFVGDI 547
Cdd:COG1541 137 GLFTgglGLHYGAERLgatvIPAG--GGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEgidprDLSLKKGIFGGEP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 548 LTkrDCLRlQTIAQ--NVNIINMYGTTETQRAVSYfEipSRAQDstflevqkdimpagkGMH---NVQLLVVNRHDRSKT 622
Cdd:COG1541 215 WS--EEMR-KEIEErwGIKAYDIYGLTEVGPGVAY-E--CEAQD---------------GLHiweDHFLVEIIDPETGEP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 623 CAIGEVGEIYVRAaglaeqyrgqpdLNKEKFvpnwfvspskwveedkkiskdepwrefylgPRDRlYRTGDLGRYLPtGD 702
Cdd:COG1541 274 VPEGEEGELVVTT------------LTKEAM------------------------------PLIR-YRTGDLTRLLP-EP 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 703 CE----------VSGRADDQVKIRGFRIELGEIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELENFK 768
Cdd:COG1541 310 CPcgrthprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEALA 385
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
689-735 |
2.24e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 48.97 E-value: 2.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 254566307 689 YRTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTHISRHPLI 735
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
|
|
| Arna_like_SDR_e |
cd05257 |
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ... |
985-1186 |
2.95e-05 |
|
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: 47.68 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDldvqvyAHVRAKDeesglerLRNTGKVYGIWNEEWTSRIKVVIADLSKdklGLSGEK 1064
Cdd:cd05257 1 NVLVTGADGFIGSHLTERLLREG------HEVRALD-------IYNSFNSWGLLDNAVHDRFHFISGDVRD---ASEVEY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yaeLANTIDLIIHNGALVHWVYPY---SKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHYITlsdtlteqged 1141
Cdd:cd05257 65 ---LVKKCDVVFHLAALIAIPYSYtapLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVP----------- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254566307 1142 gIPESDDLLGSSKGlGTGYGQSKWAAEYIIRRAF-ERGLRGAIIRP 1186
Cdd:cd05257 131 -IDEDHPLLYINKP-RSPYSASKQGADRLAYSYGrSFGLPVTIIRP 174
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
4-213 |
3.42e-05 |
|
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: 48.14 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 4 ENLNYWANILDGPTLSVLPRDYNRPVAGKVIEANKTFDISDILPFLNK--ANEPSVTQFTAPLAVFAVLVYRLTGDDDIV 81
Cdd:cd19539 190 ELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRelAKRARSSLFMVLLAAYCVLLRRYTGQTDIV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 82 ILTDSPKKQNLPF-----------VVRLQVDPSKSFVDVSKQVGEQYLES-LERATPLKDIVTHLKESKQlPNYPPIFRL 149
Cdd:cd19539 270 VGTPVAGRNHPRFestvgffvnllPLRVDVSDCATFRDLIARVRKALVDAqRHQELPFQQLVAELPVDRD-AGRHPLVQI 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 150 SFQ---TAKKVQQLSTLVE---------GSTRDL-AIFLENNTSI--NIYYNSLLYTHNRIAYFSQQFSSFIDEVNKAP 213
Cdd:cd19539 349 VFQvtnAPAGELELAGGLSytegsdipdGAKFDLnLTVTEEGTGLrgSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| UDP_G4E_5_SDR_e |
cd05264 |
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ... |
985-1210 |
4.36e-05 |
|
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase 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: 187574 [Multi-domain] Cd Length: 300 Bit Score: 47.31 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYAHvRAKDEESGLERLRNTGKVYGiwneewtsrikvVIADLSKdklglsgek 1064
Cdd:cd05264 1 RVLIVGGNGFIGSHLVDALLEEGPQVRVFDR-SIPPYELPLGGVDYIKGDYE------------NRADLES--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 yaELANtIDLIIHngaLVHWVYPYSKLRD------ANVISTINVLNLAASGKPKQFGFVSSTSTLdtehYitlsdtlTEQ 1138
Cdd:cd05264 59 --ALVG-IDTVIH---LASTTNPATSNKNpildiqTNVAPTVQLLEACAAAGIGKIIFASSGGTV----Y-------GVP 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 1139 GEDGIPESDDLLGSSKglgtgYGQSKWAAEYIIR-RAFERGLRGAIIRPG--YVTGHS---RTGACNTddFLLRMLKG 1210
Cdd:cd05264 122 EQLPISESDPTLPISS-----YGISKLAIEKYLRlYQYLYGLDYTVLRISnpYGPGQRpdgKQGVIPI--ALNKILRG 192
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
724-825 |
7.59e-05 |
|
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: 42.15 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 724 EIDTHISRHPLIRQNVTLVRRDKDEEPILISYVVPKETPELenfksssddlddlndpivkslllyreLIKDLKAHLKKTL 803
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL--------------------------LEEELVAHVREEL 54
|
90 100
....*....|....*....|..
gi 254566307 804 ASYAIPTIIVPMAKLPLNPNGK 825
Cdd:pfam13193 55 GPYAVPKEVVFVDELPKTRSGK 76
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
3-122 |
9.88e-05 |
|
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: 46.58 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 3 EENLNYWANILDG-PTLSVLPRDYNRPV----AGkvieANKTFDISDILpfLNK----ANEPSVTQFTAPLAVFAVLVYR 73
Cdd:cd19531 189 ERQLAYWREQLAGaPPVLELPTDRPRPAvqsfRG----ARVRFTLPAEL--TAAlralARREGATLFMTLLAAFQVLLHR 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 74 LTGDDDIVILT-----DSPKKQNL--PFV----VRLQVDPSKSFVDVSKQVGEQYLESLE 122
Cdd:cd19531 263 YSGQDDIVVGTpvagrNRAELEGLigFFVntlvLRTDLSGDPTFRELLARVRETALEAYA 322
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
254-334 |
1.47e-04 |
|
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: 46.40 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 254 NAEKFPDRTCVV-ETksflNPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFS 332
Cdd:cd05966 62 HLKERGDKVAIIwEG----DEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHS 137
|
..
gi 254566307 333 VI 334
Cdd:cd05966 138 VV 139
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
254-440 |
1.71e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 45.77 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 254 NAEKFPDRTCVVETKSflnpnsqTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSV 333
Cdd:PRK13390 6 HAQIAPDRPAVIVAET-------GEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 334 IDPAYPPARQNVylqVAKPAGLIVLEKAGVLDQLVEDyIKNELSLvsRISnlkieadgnvLGGDVDGkdaLYDYQQFKTR 413
Cdd:PRK13390 79 INHHLTAPEADY---IVGDSGARVLVASAALDGLAAK-VGADLPL--RLS----------FGGEIDG---FGSFEAALAG 139
|
170 180
....*....|....*....|....*..
gi 254566307 414 RTGVLVGPDSNPTLSFTSGSEGIPKGV 440
Cdd:PRK13390 140 AGPRLTEQPCGAVMLYSSGTTGFPKGI 166
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2-213 |
2.00e-04 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 45.52 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 2 SEENLNYWANILDGPTLSVLPrdYNRPVAGKVIEANKTFDISDILPFLNK--ANEPSVTQFTAPLAVFAVLVYRLTGDDD 79
Cdd:cd19536 184 QAASERYWREYLAGATLATLP--ALSEAVGGGPEQDSELLVSVPLPVRSRslAKRSGIPLSTLLLAAWALVLSRHSGSDD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 80 IVI-LTDSPKKQN--------------LPFVVRLQVDpskSFVDVSKQVGEQYLESLE-RATPLKDIVTHlkeSKQLPNY 143
Cdd:cd19536 262 VVFgTVVHGRSEEttgaerllglflntLPLRVTLSEE---TVEDLLKRAQEQELESLShEQVPLADIQRC---SEGEPLF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 144 PPIFR-----LSFQTAKKVQQLSTLV------EGSTRDLAIFLEN---NTSINIYYNSLLYTHNRIAYFSQQFSSFIDEV 209
Cdd:cd19536 336 DSIVNfrhfdLDFGLPEWGSDEGMRRgllfseFKSNYDVNLSVLPkqdRLELKLAYNSQVLDEEQAQRLAAYYKSAIAEL 415
|
....
gi 254566307 210 NKAP 213
Cdd:cd19536 416 ATAP 419
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
277-441 |
2.73e-04 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 45.38 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 277 TRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAKPAGLI 356
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 357 VLEKAGVLDQLVEDYIKNELSLVSRISNLKIEADGNvlgGDVDGKDALYDYqqfktrrtgvlvGPDSNPTLSFTSGSEGI 436
Cdd:PRK05857 119 VAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHS---LDAASLAGNADQ------------GSEDPLAMIFTSGTTGE 183
|
....*
gi 254566307 437 PKGVL 441
Cdd:PRK05857 184 PKAVL 188
|
|
| SDR_a5 |
cd05243 |
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ... |
985-1129 |
4.02e-04 |
|
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: 43.38 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERdlDVQVYAHVRAKDEESGLERlrntgkvygiwneewtSRIKVVIADLSKDklglsgEK 1064
Cdd:cd05243 1 KVLVVGATGKVGRHVVRELLDR--GYQVRALVRDPSQAEKLEA----------------AGAEVVVGDLTDA------ES 56
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254566307 1065 YAELANTIDLII--HNGALVHWVYPYSKLRDANvistINVLNLAASGKPKQFGFVSSTSTLDTEHYI 1129
Cdd:cd05243 57 LAAALEGIDAVIsaAGSGGKGGPRTEAVDYDGN----INLIDAAKKAGVKRFVLVSSIGADKPSHPL 119
|
|
| UDP_GE_SDE_e |
cd05253 |
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ... |
984-1121 |
4.49e-04 |
|
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended 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: 187563 [Multi-domain] Cd Length: 332 Bit Score: 44.25 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 984 INIFLTGATGFLGSYILKDLLERDLDV------QVYAHVRAKdeESGLERLRNTGKvygiwneewTSRIKVVIADLSK-D 1056
Cdd:cd05253 1 MKILVTGAAGFIGFHVAKRLLERGDEVvgidnlNDYYDVRLK--EARLELLGKSGG---------FKFVKGDLEDREAlR 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254566307 1057 KLGLSGEkyaelantIDLIIHNGALVHWVY----PYSKLrDANVISTINVLNLAASGKPKQFGFVSSTS 1121
Cdd:cd05253 70 RLFKDHE--------FDAVIHLAAQAGVRYslenPHAYV-DSNIVGFLNLLELCRHFGVKHLVYASSSS 129
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
989-1234 |
4.72e-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: 43.89 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 989 TGATGFLGSYILKDLLERDlDVQvyaHVRAKDEESGLERLRNTGKVygiwneewtSRIKVVIADL-SKDKLglsgekyAE 1067
Cdd:pfam01073 3 TGGGGFLGRHIIKLLVREG-ELK---EVRVFDLRESPELLEDFSKS---------NVIKYIQGDVtDKDDL-------DN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1068 LANTIDLIIHNGAL--VHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSSTSTLDTEHYitlsdtlteqGEDGIPE 1145
Cdd:pfam01073 63 ALEGVDVVIHTASAvdVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSY----------GQPILNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1146 SDDLLGSSKgLGTGYGQSKWAAEYIIRRAFERGLRGA------IIRPGYVTGHSrtgacntDDFLLRMLKGCAELG-KLP 1218
Cdd:pfam01073 133 DEETPYEST-HQDAYPRSKAIAEKLVLKANGRPLKNGgrlytcALRPAGIYGEG-------DRLLVPFIVNLAKLGlAKF 204
|
250
....*....|....*....
gi 254566307 1219 NI---SNTVNMVPVDHVAL 1234
Cdd:pfam01073 205 KTgddNNLSDRVYVGNVAW 223
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2-213 |
6.24e-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: 43.84 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 2 SEENLNYWANILDG--PTLSvLPRDYNRPVAGKVIEANKTFDISDILpfLNK----ANEPSVTQFTAPLAVFAVLVYRLT 75
Cdd:cd20484 184 GEEHRAYWKQQLSGtlPILE-LPADRPRSSAPSFEGQTYTRRLPSEL--SNQiksfARSQSINLSTVFLGIFKLLLHRYT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 76 GDDDIVILTDS---PKKQ---------N-LPfvVRLQVDPSKSFVDVSKQVGEQYLESLERAT-PLKDIVTHLKeSKQLP 141
Cdd:cd20484 261 GQEDIIVGMPTmgrPEERfdsligyfiNmLP--IRSRILGEETFSDFIRKLQLTVLDGLDHAAyPFPAMVRDLN-IPRSQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 142 NYPPIFRLSF--QTAKKVQQLSTLVEGSTRDLAIFL-------------------ENNTSINIYYNSLLYTHNRIAYFSQ 200
Cdd:cd20484 338 ANSPVFQVAFfyQNFLQSTSLQQFLAEYQDVLSIEFvegihqegeyelvlevyeqEDRFTLNIKYNPDLFDASTIERMME 417
|
250
....*....|...
gi 254566307 201 QFSSFIDEVNKAP 213
Cdd:cd20484 418 HYVKLAEELIANP 430
|
|
| AR_like_SDR_e |
cd05193 |
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ... |
988-1191 |
6.59e-04 |
|
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: 43.37 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 988 LTGATGFLGSYILKDLLERDLDVQvyAHVRA---KDEESGLERLRntgkvygiwneEWTSRIKVVIADLSkDKLGlsgek 1064
Cdd:cd05193 3 VTGASGFVASHVVEQLLERGYKVR--ATVRDpskVKKVNHLLDLD-----------AKPGRLELAVADLT-DEQS----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 YAELANTIDLIIHNGALVH-WVYPYSKLRDANVISTINVLNLAASGKP-KQFGFVSSTSTLdtehyitlsdTLTEQGEDG 1142
Cdd:cd05193 64 FDEVIKGCAGVFHVATPVSfSSKDPNEVIKPAIGGTLNALKAAAAAKSvKRFVLTSSAGSV----------LIPKPNVEG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 1143 I-----PESDDLLGSSKGLGTG-YGQSKWAAEYI-IRRAFERGLRGAIIRPGYVTG 1191
Cdd:cd05193 134 IvldekSWNLEEFDSDPKKSAWvYAASKTLAEKAaWKFADENNIDLITVIPTLTIG 189
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
277-466 |
7.87e-04 |
|
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: 43.57 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 277 TRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGvlkagatfsvidpaypparqnvylqvakpagli 356
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLG--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 357 vLEKAGVLDQLVEDYIKNElSLVSRISNLKIEAdgnVLggdVDGKDALyDYQQFKTRRTGVLVGPDSNPTLSFTSGSEGI 436
Cdd:cd05939 48 -LAKIGVETALINSNLRLE-SLLHCITVSKAKA---LI---FNLLDPL-LTQSSTEPPSQDDVNFRDKLFYIYTSGTTGL 118
|
170 180 190
....*....|....*....|....*....|....
gi 254566307 437 PKGVLGRHFSlaYYfpWMS----KTFNLSENDKF 466
Cdd:cd05939 119 PKAAVIVHSR--YY--RIAagayYAFGMRPEDVV 148
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
276-768 |
8.84e-04 |
|
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: 43.57 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 276 QTRTFTYKQIDQASNIVGNYLVHT-GIKRGDVVMIYAYRGVDLMVAVMGVLKAGATfsvidpaypPARQNVYLqvaKPAG 354
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNL---SGDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 355 LIvlekagvldqlvedyikneLSLvsRISNLKIeadgnvlggdvdgkdalydyqqfktrrtgVLVGPDSNPTLSFTSGSE 434
Cdd:cd05937 70 LI-------------------HCL--KLSGSRF-----------------------------VIVDPDDPAILIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 435 GIPKGVL---GRHFSLAYYFpwmSKTFNLSENDKftmlsgiahdpiqrdMFT--PLFLGAQLLIPTSDDIGTPGKLAE-- 507
Cdd:cd05937 100 GLPKAAAiswRRTLVTSNLL---SHDLNLKNGDR---------------TYTcmPLYHGTAAFLGACNCLMSGGTLALsr 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 508 -------WMQTY--GAT-VTHLTPAMGQLLSAQATKEiPSLHHAFFV------GDILTK-RDCLRLQTIAQnvniinMYG 570
Cdd:cd05937 162 kfsasqfWKDVRdsGATiIQYVGELCRYLLSTPPSPY-DRDHKVRVAwgnglrPDIWERfRERFNVPEIGE------FYA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 571 TTE-----TQRAVSYFEIPSRAQDSTFLEVQkdimpagkgMHNVQLLVVNRHD------RSKT-----CAIGEVGEIYVR 634
Cdd:cd05937 235 ATEgvfalTNHNVGDFGAGAIGHHGLIRRWK---------FENQVVLVKMDPEtddpirDPKTgfcvrAPVGEPGEMLGR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 635 AaglaeqyrgqPDLNKEKFvpnwfvsPSKWVEED---KKISKDepwrEFYLGprDRLYRTGDLGRYLPTGDCEVSGRADD 711
Cdd:cd05937 306 V----------PFKNREAF-------QGYLHNEDateSKLVRD----VFRKG--DIYFRTGDLLRQDADGRWYFLDRLGD 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 712 QVKIRGFRIELGEIDTHISRHPLIRQ------------------NVTLVRRDKDEEPI------------LISYVVP--- 758
Cdd:cd05937 363 TFRWKSENVSTTEVADVLGAHPDIAEanvygvkvpghdgragcaAITLEESSAVPTEFtksllaslarknLPSYAVPlfl 442
|
570
....*....|...
gi 254566307 759 KETPELE---NFK 768
Cdd:cd05937 443 RLTEEVAttdNHK 455
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
426-831 |
1.26e-03 |
|
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: 43.22 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 426 TLSFTSGSEGIPKGVLGRHFSLAY-YFPWMSKTFNLSENDKFTMLS--GIAHDPIQrDMFTPLFLGAQLLI---PTSDdi 499
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSHSSLGLgLKVNGRYWLDLTASDIMWNTSdtGWIKSAWS-SLFEPWIQGACVFVhhlPRFD-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 500 gtPGKLAEWMQTYGATVTHLTPAMGQLLSAQATKEI--PSLHHAFFVGDILTKRDC--LRLQTiaqNVNIINMYGTTETQ 575
Cdd:cd05928 255 --PLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYkfPSLQHCVTGGEPLNPEVLekWKAQT---GLDIYEGYGQTETG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 576 RAVSYFEipsraqdstFLEVQKDIMpaGKGM--HNVQLLvvnrHDRSKTCAIGEVGEIYVRAA-----GLAEQYRGQPDL 648
Cdd:cd05928 330 LICANFK---------GMKIKPGSM--GKASppYDVQII----DDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 649 NKEKFVPNwfvspskwveedkkiskdepwreFYLgprdrlyrTGDLGRYLPTGDCEVSGRADDQVKIRGFRIELGEIDTH 728
Cdd:cd05928 395 TAATIRGD-----------------------FYL--------TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 729 ISRHPLIRQNVTLVRRDKDEEPILISYVVPkeTPElenFKSSSDdlddlndpivkslllyRELIKDLKAHLKKTLASYAI 808
Cdd:cd05928 444 LIEHPAVVESAVVSSPDPIRGEVVKAFVVL--APQ---FLSHDP----------------EQLTKELQQHVKSVTAPYKY 502
|
410 420
....*....|....*....|...
gi 254566307 809 PTIIVPMAKLPLNPNGKVDKPKL 831
Cdd:cd05928 503 PRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
272-441 |
1.41e-03 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 42.96 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 272 NPNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNVYLQVAK 351
Cdd:PLN02654 113 NEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 352 PA----------GLIVLEKAGVLDQLVEDYIKNELSL-----VSRISNLKIEADGNVLGGDVDGKDALydyQQFKTRRTG 416
Cdd:PLN02654 193 PKvvitcnavkrGPKTINLKDIVDAALDESAKNGVSVgicltYENQLAMKREDTKWQEGRDVWWQDVV---PNYPTKCEV 269
|
170 180
....*....|....*....|....*
gi 254566307 417 VLVGPDSNPTLSFTSGSEGIPKGVL 441
Cdd:PLN02654 270 EWVDAEDPLFLLYTSGSTGKPKGVL 294
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
273-334 |
2.42e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.44 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254566307 273 PNSQTRTFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLKAGATFSVI 334
Cdd:PRK00174 92 DPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
247-338 |
2.50e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 42.11 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 247 IQDIFSDNAEKFPDRTCVVEtksflnPNSQTRtFTYKQIDQASNIVGNYLVHTGIKRGDVVMIYAYRGVDLMVAVMGVLK 326
Cdd:PRK08315 18 IGQLLDRTAARYPDREALVY------RDQGLR-WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAK 90
|
90
....*....|..
gi 254566307 327 AGATFSVIDPAY 338
Cdd:PRK08315 91 IGAILVTINPAY 102
|
|
| UDP_G4E_3_SDR_e |
cd05240 |
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ... |
986-1205 |
2.59e-03 |
|
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: 41.58 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 986 IFLTGATGFLGSYILKDLLERDldvqvyaHVRAKDeesGLERLRNTGkvygiwneeWTSRIKVVIADLSKDKLGLSGEKY 1065
Cdd:cd05240 1 ILVTGAAGGLGRLLARRLAASP-------RVIGVD---GLDRRRPPG---------SPPKVEYVRLDIRDPAAADVFRER 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1066 AelantIDLIIHNGALVHWVYPYSKLRDANVISTINVLNLAASGKPKQFGFVSST----STLDTEHYITLSDTLteQGED 1141
Cdd:cd05240 62 E-----ADAVVHLAFILDPPRDGAERHRINVDGTQNVLDACAAAGVPRVVVTSSVavygAHPDNPAPLTEDAPL--RGSP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 1142 GIPESDDLLgsskglgtgygqskwAAEYIIRRAFER--GLRGAIIRPGYVTGhsRTGACNTDDFLL 1205
Cdd:cd05240 135 EFAYSRDKA---------------EVEQLLAEFRRRhpELNVTVLRPATILG--PGTRNTTRDFLS 183
|
|
| GDP_Man_Dehyd |
pfam16363 |
GDP-mannose 4,6 dehydratase; |
987-1123 |
3.29e-03 |
|
GDP-mannose 4,6 dehydratase;
Pssm-ID: 465104 [Multi-domain] Cd Length: 327 Bit Score: 41.38 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 987 FLTGATGFLGSYILKDLLERdlDVQVYAHVRAKDEESgLERLRNTGKVYGiwneewTSRIKVVIADLSkDKLGLSG--EK 1064
Cdd:pfam16363 1 LITGITGQDGSYLAELLLEK--GYEVHGIVRRSSSFN-TGRLEHLYDDHL------NGNLVLHYGDLT-DSSNLVRllAE 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254566307 1065 YAelantIDLIIHNGALVHwVyPYS-----KLRDANVISTINVLNLA-ASGKPKQFGFV-SSTSTL 1123
Cdd:pfam16363 71 VQ-----PDEIYNLAAQSH-V-DVSfeqpeYTADTNVLGTLRLLEAIrSLGLEKKVRFYqASTSEV 129
|
|
| YwnB |
COG2910 |
Putative NADH-flavin reductase [General function prediction only]; |
985-1196 |
5.50e-03 |
|
Putative NADH-flavin reductase [General function prediction only];
Pssm-ID: 442154 [Multi-domain] Cd Length: 205 Bit Score: 39.84 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 985 NIFLTGATGFLGSYILKDLLERDLDVQVYAhvrakdeesglerlRNTGKVygiwnEEWTSRIKVVIADLskdklgLSGEK 1064
Cdd:COG2910 1 KIAVIGATGRVGSLIVREALARGHEVTALV--------------RNPEKL-----PDEHPGLTVVVGDV------LDPAA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 1065 YAELANTIDLIIHngAL-VHWVYPYSKLRDAnvisTINVLNLAASGKPKQFGFVSSTSTLDTEHYITLsDTlteqgeDGI 1143
Cdd:COG2910 56 VAEALAGADAVVS--ALgAGGGNPTTVLSDG----ARALIDAMKAAGVKRLIVVGGAGSLDVAPGLGL-DT------PGF 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254566307 1144 PESddllgsskglgtgygqskWAAEYIIRRAFERGLRGA-----IIRPGYVTGHSRTG 1196
Cdd:COG2910 123 PAA------------------LKPAAAAKAAAEELLRASdldwtIVRPAALTDGERTG 162
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
421-493 |
6.57e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.85 E-value: 6.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254566307 421 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMSKTFNLSENDKFTMLSGIAHD-PIQRDMFTPLFLGAQLLI 493
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSfGLTVGLFTPLLTGAEVFL 437
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
599-735 |
9.00e-03 |
|
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: 40.41 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 599 IMPAGKGMHNVQLLVVNRhDRSKTCAIGEVGEIYVRAAGLAEQYrgqpdlnkekfvpnwFVSPSkwveEDKKISKDEPWR 678
Cdd:cd05905 360 LQDSGKVLPGAQVAIVNP-ETKGLCKDGEIGEIWVNSPANASGY---------------FLLDG----ETNDTFKVFPST 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254566307 679 EFYLGPRDRLY-RTGDLGrYLPTGDCEVS-----------GRADDQVKIRGFRIELGEIDTHISR-HPLI 735
Cdd:cd05905 420 RLSTGITNNSYaRTGLLG-FLRPTKCTDLnveehdllfvvGSIDETLEVRGLRHHPSDIEATVMRvHPYR 488
|
|
| |
