|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
5-1358 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 2028.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 5 ILPGPKALSQFRVDNLIKDINSYTNStsvINELRSCYIHYVNgIAQNLSEQDTKLLEVLLTYDsaldiandplarqlnda 84
Cdd:PRK05297 3 ILRGSPALSAFRLQKLLARLQAAVLP---VTSIYAEYVHFAD-LSAPLSAEEQAKLERLLTYG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 85 vannlPSSALGEDTYLIrVVPRSGTISPWSSKATNIAHVCGLqDKVQRIERGLALLIKTvpgfPLLENLNDISLKCVYDR 164
Cdd:PRK05297 62 -----PAEHEPAGRLFL-VTPRPGTISPWSSKATDIAHNCGL-AGIRRIERGIAYYVEA----ALSAEQRAALAALLHDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 165 MTQQLYlTEPPNTMSIFTHEEPKPLVHVPLTpkdtkQSPKDILSKANTELGLALDSGEMEYLIHAFVEtMKRDPTDVELF 244
Cdd:PRK05297 131 MTESVF-ADLDDAEALFSHHEPKPLTSVDVL-----GGGRAALEAANVELGLALAEDEIDYLVEAFTK-LGRNPTDVELM 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 245 MFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLD-SENDAFFfaPNSTTKEWTSTKE 323
Cdd:PRK05297 204 MFAQANSEHCRHKIFNADWTIDGEEQPKSLFKMIKNTHETNPDGVLSAYKDNAAVMEgSKVGRFF--PDPDTGRYGYHQE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 324 RIPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALDI 403
Cdd:PRK05297 282 PAHILMKVETHNHPTAISPFPGAATGSGGEIRDEGATGRGSKPKAGLTGFSVSNLRIPGFEQPWEEDYGKPERIASALDI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 404 MIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQgkEEIRGFHKPIMIAGGFGTVRPQFALKNtPITPGSCLIVLGGQS 483
Cdd:PRK05297 362 MIEGPLGGAAFNNEFGRPNLLGYFRTFEQKVNSHN--EEVRGYHKPIMLAGGIGNIRADHVQKG-EIPVGAKLIVLGGPA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 484 MLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGA 563
Cdd:PRK05297 439 MRIGLGGGAASSMASGQSSEDLDFASVQRGNPEMERRCQEVIDRCWQLGDDNPILSIHDVGAGGLSNAFPELVNDGGRGG 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 564 KFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEMP 643
Cdd:PRK05297 519 RFDLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEAICERERCPFAVVGEATEERHLTLEDSHFDNKPVDLPLD 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 644 ILFGKPPKMSRETITEALNLPEANLSEIpSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGV 723
Cdd:PRK05297 599 VLLGKPPKMHRDVKTVKAKGPALDYSGI-DLAEAVERVLRLPTVASKSFLITIGDRSVTGLVARDQMVGPWQVPVADCAV 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 724 TGTSL-GEtiisTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQ 802
Cdd:PRK05297 678 TAASYdGY----AGEAMAMGERTPVALLDAAASARMAVGEALTNIAAAPIGDLKRIKLSANWMAAAGHPGEDARLYDAVK 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 803 ALGLDLCPALGVAIPVGKDSMSMKMKWDD----KEVTAPLSLNITAFAPVFNTSKTWTPLLnRNTDDSVLVLVDLSAKQe 878
Cdd:PRK05297 754 AVGMELCPALGITIPVGKDSLSMKTKWQEggedKEVTSPLSLIISAFAPVEDVRKTLTPQL-RTDKDTALLLIDLGRGK- 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 879 tKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHqqKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINID-- 956
Cdd:PRK05297 832 -NRLGGSALAQVYNQLGDKAPDVDDAEDLKGFFNAIQALV--AEGLLLAYHDRSDGGLLTTLAEMAFAGHCGLDIDLDal 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 957 GGDLesqLTNLFNEELGAVFQISAKNLSKFEKILNENGVAkEYISIVGKPSfQSQEIKIINSttNDVIYANSRSELEQTW 1036
Cdd:PRK05297 909 GDDA---LAALFNEELGAVIQVRAADRDAVEAILAEHGLS-DCVHVIGKPN-AGDRIVITRN--GKTVFSESRTELRRWW 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1037 SKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQMEMAWCFQQAGF 1116
Cdd:PRK05297 982 SETSYQMQRLRDNPECADQEFDAILDQADPGLNVKLTFDPNEDIAAPFIATGARPKVAILREQGVNSHVEMAAAFDRAGF 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1117 NSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNeRQDTFAFGACNGCQFLSRL 1196
Cdd:PRK05297 1062 DAIDVHMSDLLAGRVTLEDFKGLVACGGFSYGDVLGAGEGWAKSILFNPRLRDQFEAFFA-RPDTFALGVCNGCQMMSNL 1140
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1197 KDIIPGCENWPSFERNVSEQYEARVCMVQISQEKdnsseeSVFLNGMAGSKLPIAVAHGEGKATFSKsaEQLEKFEKDGL 1276
Cdd:PRK05297 1141 KEIIPGAEHWPRFVRNRSEQFEARFSLVEVQESP------SIFLQGMAGSRLPIAVAHGEGRAEFPD--AHLAALEAKGL 1212
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1277 CCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPegkyEEWGGYGPWIRLFRSARRW 1356
Cdd:PRK05297 1213 VALRYVDNHGQVTETYPANPNGSPNGITGLTTADGRVTIMMPHPERVFRTVQNSWHP----EEWGEDSPWMRMFRNARKW 1288
|
..
gi 6321498 1357 VG 1358
Cdd:PRK05297 1289 VG 1290
|
|
| FGAM_synt |
TIGR01735 |
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
5-1357 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 188163 [Multi-domain] Cd Length: 1310 Bit Score: 1616.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 5 ILPGPKALSQFRVDNLIKDINSY-TNSTSVINElrscYIHYVnGIAQNLSEQDTKLLEVLLTYDSALDIANDPLARQLnd 83
Cdd:TIGR01735 1 FLRGPSALSGFRLEKLLQKLQTKvPELTGVYAE----FCYFV-GWESALTADEEEKLQLLLLAGSVLEPPQSPLGRGL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 84 avannlpssalgedtylIRVVPRSGTISPWSSKATNIAHVCGLqDKVQRIERGLALLIKTvpGFPLLENLNDISLKCVYD 163
Cdd:TIGR01735 74 -----------------LEVGPRLGTISPWSSKATSIARNCGL-AKVDRIERGRRYYLSG--AHPLSEEQEAQAAALLHD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 164 RMTQQLyLTEPPNTMSIFTHEEPKPLVHVPLTPKDtkqspKDILSKANTELGLALDSGEMEYLIHAFVEtMKRDPTDVEL 243
Cdd:TIGR01735 134 RMTESV-LPHEIEAFELFSVPEPLNLTTIDVLGGG-----RLALEKANQELGLALDEDEIDYLTKRFQE-LQRNPSDVEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 244 FMFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLDSENDAFFFAPNSTTKEWTSTKE 323
Cdd:TIGR01735 207 MMFAQANSEHCRHKIFNADWIIDGKKQDKSLFQMIKSTHEANPENTVSAYKDNSSVIEGHKVGRLRPDPPTRPEYRQHQE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 324 R-IPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALD 402
Cdd:TIGR01735 287 DlVHILMKVETHNHPTAIAPFPGASTGAGGEIRDEGATGRGAKPKAGLTGFCVSNLNIPGLEQPWEDPFQKPERIASPLD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 403 IMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQGkeEIRGFHKPIMIAGGFGTVRPQFALKNTPiTPGSCLIVLGGQ 482
Cdd:TIGR01735 367 IMIEAPLGAAAFNNEFGRPNLLGYFRTFELKASLPGG--QVRGYHKPIMLAGGIGSIDAEHIQKGEI-EPGALLIVLGGP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 483 SMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLG 562
Cdd:TIGR01735 444 AMLIGLGGGAASSMVSGTNTADLDFASVQRGNPEMERRCQEVIDRCWQLGEKNPIISIHDVGAGGLSNALPELIHDGGRG 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 563 AKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVED------------ 630
Cdd:TIGR01735 524 AVIDLRAVPLDDPGLSPLEIWCNESQERYVLLVRAENLEIFTAICERERCPFAVVGTATGDGRLTLVDdtpvrrngqgda 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 631 -PLLKTTPIDLEMPILFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQ 709
Cdd:TIGR01735 604 pSHFPNNPVDLPLEVLLGKMPKMTRFVQRKAPMLQPLDIPPGLDLHEALERVLRLPAVASKRFLITIGDRSVGGLVARDQ 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 710 FVGPWQVPVADVGVTGTSLGETiisTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPAS 789
Cdd:TIGR01735 684 MVGPWQTPLADVAVTAASFDTY---TGEAMAIGERPPKALLDPKASARLAVGEAITNLAAALVGDLSDVKLSANWMAAAG 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 790 HQGEGSKLYEAVQALgLDLCPALGVAIPVGKDSMSMKMKWDD----KEVTAPLSLNITAFAPVFNTSKTWTPLLNRNTDD 865
Cdd:TIGR01735 761 HPGEDAALYDAVKAV-SELCPALGIAIPVGKDSLSMKTRWQDngetKSVTAPGSLVISAFAPVPDVRKTVTPDLKHDKGD 839
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 866 SVLVLVDLSAKQetKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLhqQKEDIVLAYHDRSDGGLLITLLEMAF 945
Cdd:TIGR01735 840 SHLLLVDLGPGK--NRLGGSALAQVFGQLGGDCPDLDDPERLKAFFAVMQGL--VAEGLLLAYHDRSDGGLVTTLLEMAF 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 946 ASRCGLEINIDgGDLESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFQSQEIKiINSTTndvIY 1025
Cdd:TIGR01735 916 AGHCGLDVDLD-ALGDSLFAVLFNEELGAVIQVAKPDLAAVLELLRAAGLTALILGIGTPTGHPMIRIS-VNGAT---LL 990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1026 ANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQM 1105
Cdd:TIGR01735 991 SEKRSELRDIWEETSFQLQRLRDNPECAEEEFEGLRDRDGPGLKLPLTFDVNEDIAAPFINKGVKPKVAILREQGVNGDR 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1106 EMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFnERQDTFAFG 1185
Cdd:TIGR01735 1071 EMAAAFDRAGFEAWDVHMSDLLAGRVHLDEFRGLAACGGFSYGDVLGAGKGWAKSILFNPRLRDQFQAFF-KRPDTFSLG 1149
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1186 ACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQekdnssEESVFLNGMAGSKLPIAVAHGEGKATFSkSA 1265
Cdd:TIGR01735 1150 VCNGCQMLSNLLEWIPGTENWPHFVRNNSERFEARVASVRVGE------SPSIMLRGMAGSRLPVAVAHGEGYAAFS-SP 1222
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1266 EQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPegkyEEWGGYGP 1345
Cdd:TIGR01735 1223 ELQAQADASGLAALRYIDDDGNPTEAYPLNPNGSPGGIAGITSCDGRVTIMMPHPERVFRAWQNSWRP----EDWDEDTP 1298
|
1370
....*....|..
gi 6321498 1346 WIRLFRSARRWV 1357
Cdd:TIGR01735 1299 WLRLFRNARNWL 1310
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
95-1356 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 1007.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 95 GEDTYLIRVVPRSGTISPWSSKATNIAHVCGLQdKVQRIERGLALLIKTvpGFPLLENLNDISLKCVYDRMTQQLYlTEP 174
Cdd:PLN03206 66 GLNAVVVEVGPRLSFTTAWSTNAVSICSACGLT-EVTRLERSRRYLLFS--SSPLDESQINAFAAMVHDRMTECVY-PQP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 175 pnTMSIFTHEEPKPLVHVPLTPKDTKQspkdiLSKANTELGLALDSGEMEYLIHAFVETMKRDPTDVELFMFAQVNSEHC 254
Cdd:PLN03206 142 --LTSFESGVVPEPVYTVPVMEEGRAA-----LEEINKEMGLAFDEQDLDYYTRLFRDDIKRDPTNVELFDIAQSNSEHS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 255 RHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNA-AVLDSENDAFFFAPNSTTKEWTSTKERIPLLIKVET 333
Cdd:PLN03206 215 RHWFFSGKLVIDGQPMPKTLFQMVKDTLKANPNNSVIGFKDNSsAIRGFVVQPLRPVSPGSPSPLAPVDRDLDILLTAET 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 334 HNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWE-LNIGKPYHIASALDIMIEAPLGSA 412
Cdd:PLN03206 295 HNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVAGTAGYCVGNLRIEGSYAPWEdSSFVYPSNLASPLQILIDASNGAS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 413 AFNNEFGRPCINGYFRTLTTKVLNHQGKEEIrgfhKPIMIAGGFGTVRPQFALKNTPiTPGSCLIVLGGQSMLIGLGGGA 492
Cdd:PLN03206 375 DYGNKFGEPLIQGYTRTFGMRLPNGERREWL----KPIMFSGGIGQIDHTHLTKGEP-DIGMLVVKIGGPAYRIGMGGGA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 493 ASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDndLGAKFDIRKVLS 572
Cdd:PLN03206 450 ASSMVSGQNDAELDFNAVQRGDAEMSQKLYRVVRACVEMGEDNPIVSIHDQGAGGNCNVVKEIIYP--KGAEIDIRAVVV 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 573 LEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKT-----------TPIDLE 641
Cdd:PLN03206 528 GDHTLSVLEIWGAEYQEQDALLIKPESRDLLQSICDRERCSMAVIGTIDGSGRVVLVDSAAPEkceanglppppPAVDLD 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 642 MPILFGKPPK----MSRETIT-EALNLPEANlseipSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQV 716
Cdd:PLN03206 608 LEKVLGDMPQktfeFKRVANKlEPLDIPPGI-----TVMDALKRVLRLPSVCSKRFLTTKVDRCVTGLVAQQQTVGPLQI 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 717 PVADVGVTGTSLGETiisTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSK 796
Cdd:PLN03206 683 PLADVAVIAQTHTGL---TGGACAIGEQPIKGLVDPKAMARLAVGEALTNLVWAKVTALSDVKASGNWMYAAKLDGEGAD 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 797 LYEAVQALGlDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWTPLLnRNTDDSVLVLVDLSAK 876
Cdd:PLN03206 760 MYDAAVALR-DAMIELGVAIDGGKDSLSMAAQAGGEVVKAPGNLVISAYVTCPDITKTVTPDL-KLGDDGVLLHVDLGKG 837
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 877 QetKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKedIVLAYHDRSDGGLLITLLEMAFASRCGLEINID 956
Cdd:PLN03206 838 K--RRLGGSALAQAYDQIGDDCPDLDDVAYLKKAFEATQDLIAKR--LISAGHDISDGGLVVTLLEMAFAGNCGINVDLP 913
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 957 GGDlESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEyisIVGKPSFQSQEIKIINSTTndvIYANSRSELEQTW 1036
Cdd:PLN03206 914 SSG-HSAFETLFAEELGLVLEVSRKNLDAVMEKLAAAGVTAE---VIGQVTASPLIEVKVDGAT---CLSEKTASLRDMW 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1037 SKTSYEMQKLRDNPKTAEEEFASITDDRDPglQYALTYNPA-DDMKIglELSSQRPKVAILREQGVNGQMEMAWCFQQAG 1115
Cdd:PLN03206 987 EETSFQLEKLQRLESCVAQEKEGLKSRKAP--TWKLSFTPAfTDKKI--MNATSKPKVAIIREEGSNGDREMAAAFYAAG 1062
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1116 FNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNeRQDTFAFGACNGCQFLSR 1195
Cdd:PLN03206 1063 FEPWDVTMSDLLNGRISLDDFRGIVFVGGFSYADVLDSAKGWAGSIRFNEPLLQQFQEFYN-RPDTFSLGVCNGCQLMAL 1141
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1196 LkDIIPGC-----------ENWPSFERNVSEQYEARVCMVQISQEKdnsseeSVFLNGMAGSKLPIAVAHGEGKATFSKS 1264
Cdd:PLN03206 1142 L-GWVPGPqvggglgaggdPSQPRFVHNESGRFECRFTSVTIEDSP------AIMLKGMEGSTLGVWAAHGEGRAYFPDE 1214
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1265 aEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPegkyEEWG--- 1341
Cdd:PLN03206 1215 -SVLDEVLKSNLAPVRYCDDDGEPTEQYPFNPNGSPLGIAALCSPDGRHLAMMPHPERCFLMWQFPWYP----KEWGvdp 1289
|
1290
....*....|....*.
gi 6321498 1342 -GYGPWIRLFRSARRW 1356
Cdd:PLN03206 1290 aGPSPWLKMFQNAREW 1305
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
203-1049 |
0e+00 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439816 [Multi-domain] Cd Length: 747 Bit Score: 855.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 203 PKDILSKANTELGLALDSGEMEYLihafVETMKRDPTDVELFMFAQVNSEHCRHKIFNADWtidgikqqftlfqmirnth 282
Cdd:COG0046 9 GREALEEANRELGLALSDDEYDYI----VEILGRNPTDVELGMFSQMWSEHCSYKSSNALL------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 283 KLNP---EYTISAYSDNAAVLD-SENDAfffapnsttkewtstkeripLLIKVETHNHPTAVSPFPGAATGSGGEIRDEG 358
Cdd:COG0046 66 KSLPtegPRVLSGPGDNAGVVDiGDGLA--------------------VVFKVESHNHPSAIEPYQGAATGVGGIIRDIF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 359 atGRGSKTKCGLSGFSVSDLlipgnEQPWelnigkpyhiASALDIMIEAPLGSAAFNNEFGRPCINGYFRTlttkvlnHQ 438
Cdd:COG0046 126 --GMGARPIAGLDSLRFGNL-----DQPP----------ASPRYILIGVVAGIADYGNCFGVPTVGGEVRF-------DE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 439 GKEeirgfHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSAdLDFASVQRGNPEME 518
Cdd:COG0046 182 SYE-----GNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSE-LDRPAVQVGDPFME 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 519 RRCQQVIDACVAlgnNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQ 598
Cdd:COG0046 256 KRLIEAILELGD---TGLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 599 DLSIFEEICKRERAPFAVVGHATAEQKLIVEDPllKTTPIDLEMPILFGKPPKMSRETITEALnLPEANLSEIPSLQDAI 678
Cdd:COG0046 333 KLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDH--GETVADLPLDFLAGGAPKYHRPAKRPAY-LEPLDLPEPIDLEEAL 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 679 QRVLNLPSVGSKSFLITIGDRSVTGLIDRDQfvgpwqvPVADVGVtgTSLGETiiSTGEAMAMGEKPVNALISASASAKL 758
Cdd:COG0046 410 LRLLSSPNVASKEWLYRQYDREVGGNTVRDP-------GVADAAV--VRVDGT--YKGLAMSTGENPRYALLDPYAGARM 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 759 SVAESLLNIFAADVKSLnHIKLSANWMSPAsHQGEGSKLYEAVQALGlDLCPALGVAIPVGKDSMSMKMKwdDKEVTAPL 838
Cdd:COG0046 479 AVAEAARNLAAVGAEPL-AITDCLNWGNPE-KPEEMAQLVEAVKGLA-DACRALGIPVPSGNVSLYNETK--DGKVAIPP 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 839 SLNITAFAPVFNTSKTWTPLLnrNTDDSVLVLVDlsakqETK-SLGASALLQVYNQVGNKSPTVyDNAILKGFLESLIQL 917
Cdd:COG0046 554 TPVIGAVGLVDDVRKTVTPDL--KKEGDLLYLIG-----ETKnELGGSEYAQVLGQLGGEPPDV-DLEAEKALFEAVQEL 625
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 918 HQqkEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELG-AVFQISAKNLSKFEKILNENGVA 996
Cdd:COG0046 626 IR--EGLILAAHDVSDGGLAVALAEMAFAGGLGADIDLDALGDLRPDAALFSESQGrAVVQVAPEDAEAVEALLAEAGLP 703
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 6321498 997 keyISIVGKPSfQSQEIKIinSTTNDVIYANSRSELEQTWSKTsyeMQKLRDN 1049
Cdd:COG0046 704 ---AHVIGTVT-GDDRLVI--RRGGETLLSLSLAELRDAWEET---LPRLRDN 747
|
|
| GATase_5 |
pfam13507 |
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
1090-1357 |
1.68e-143 |
|
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230.
Pssm-ID: 463904 [Multi-domain] Cd Length: 260 Bit Score: 436.93 E-value: 1.68e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1090 RPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRS 1169
Cdd:pfam13507 1 KPRVAILREPGTNGEYEMAAAFERAGFDAVDVHMSDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1170 QFSKFFNeRQDTFAFGACNGCQFLSRLKdIIPGC-----ENWPSFERNVSEQYEARVCMVQISQEKDnsseeSVFLNGMA 1244
Cdd:pfam13507 81 AFEAFFN-RPDTFSLGICNGCQLLSKLG-LIPGGegdlaERWPTLTRNDSGRFESRWVNVKISEKSP-----SVFLRGMD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1245 GSKLPiaVAHGEGKATFsKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVC 1324
Cdd:pfam13507 154 GSGLP--VAHGEGRFVF-RSEEVLARLEANGQVALRYVDNAGNPTEEYPFNPNGSPLGIAGICSPDGRVLGLMPHPERVF 230
|
250 260 270
....*....|....*....|....*....|...
gi 6321498 1325 RLEANSWYPEgkyEEWGGYGPWIRLFRSARRWV 1357
Cdd:pfam13507 231 RPWQWPHWPP---GEWEEVSPWLRLFRNARKWV 260
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
242-640 |
8.02e-130 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100034 [Multi-domain] Cd Length: 313 Bit Score: 402.62 E-value: 8.02e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 242 ELFMFAQVNSEHCRHKIFNadwtidgikqqfTLFQMIRNthklnpeytisaysdnaavldsendafffapnsttkewtst 321
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFK------------SLLKMIWA----------------------------------------- 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 322 keripLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGrgSKTKCGLSGFSVSDLLIPGNEqpwelnigkPYHIASAL 401
Cdd:cd02203 28 -----VVFKVETHNHPSAIEPFGGAATGVGGIIRDILSMG--ARPIALLDGLRFGDLDIPGYE---------PKGKLSPR 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 402 DIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVlnhqgkeeirgfHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGG 481
Cdd:cd02203 92 RILDGVVAGISDYGNCIGIPTVGGEVRFDPSYY------------GNPLVNVGCVGIVPKDHIVKSKAPGPGDLVVLVGG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 482 QSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVAlgnNNPIQSIHDVGAGGLSNALPELVHDNDL 561
Cdd:cd02203 160 RTGRDGIGGATFSSKELSENSSELDRPAVQVGDPFMEKKLQEAILEARE---TGLIVGIQDLGAGGLSSAVSEMAAKGGL 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321498 562 GAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPllKTTPIDL 640
Cdd:cd02203 237 GAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTDDGRLRLYYK--GEVVADL 313
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
328-620 |
2.46e-97 |
|
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100029 [Multi-domain] Cd Length: 272 Bit Score: 313.08 E-value: 2.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 328 LIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIpgneqpwelnigkpyhiaSALDIMIEA 407
Cdd:cd02193 4 AMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGIDAKPIALSANWMASAGHP------------------GEDAILYDA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 408 PLGSAAFNNEFGRPCINGYFRTLTTKVlNHQGKEEIRGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIG 487
Cdd:cd02193 66 VKGVAELCNQLGLPIPVGKDRMSMKTR-WQEGNEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 488 LGGGAASSVAsgEGSADLDFASVQRGNPEMERRCQQVIDACVALGnnnPIQSIHDVGAGGLSNALPELVHDNDLGAKFDI 567
Cdd:cd02193 145 LGGTALASVA--LSYRQLGDKSAQVRDPAQEKGFYEAMQALVAAG---KLLAWHDRGAGGLLVALAELVFAGHCGVQVDL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 6321498 568 RKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHA 620
Cdd:cd02193 220 AALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEAQYGLADCVHVLGQA 272
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
1093-1354 |
1.95e-93 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 300.69 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1093 VAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLyhegvRSQFS 1172
Cdd:cd01740 1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASPL-----LMEEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1173 KFFNERqDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYearvcmvqISQEKDNSSEESVFLNG-MAGSKLPIA 1251
Cdd:cd01740 76 KEFAER-GGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQN--------RFVTLRVENNDSPFTKGyMEGEVLRIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1252 VAHGEGKATFSKSAEQLEKFEKDGlccIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANsw 1331
Cdd:cd01740 147 VAHGEGRFYADDETLAELEENGQI---AQYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPWQW-- 221
|
250 260
....*....|....*....|...
gi 6321498 1332 ypegkyEEWGGYGPWIRLFRSAR 1354
Cdd:cd01740 222 ------ERLLGGSDGLKLFRNAV 238
|
|
| PurL2 |
COG0047 |
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1091-1358 |
6.45e-92 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439817 [Multi-domain] Cd Length: 236 Bit Score: 296.20 E-value: 6.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1091 PKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLlegRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVlyhegVRSQ 1170
Cdd:COG0047 1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDL---RTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSP-----IMDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1171 FSKFFneRQDTFAFGACNGCQFLSRLkDIIPGceNWPSFERNVSEQYEARVCMVQISqekdnsSEESVFLNGM-AGSKLP 1249
Cdd:COG0047 73 VREFA--RRGGLVLGICNGFQILTEL-GLLPG--IWPALTRNRSLRFICRWVYLRVE------NNDSPFTSGMeAGEVIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1250 IAVAHGEGKATFSksAEQLEKFEKDGLCCIRYVDNYGNVTErfPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEAN 1329
Cdd:COG0047 142 IPIAHGEGRYVAD--EETLAELEANGQVAFRYVDADGNVTY--PANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLG 217
|
250 260
....*....|....*....|....*....
gi 6321498 1330 SwypegkyeewGGYGPWIRLFRSARRWVG 1358
Cdd:COG0047 218 P----------GESTDGLRIFRSAVKYFG 236
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
720-1005 |
1.03e-68 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100035 [Multi-domain] Cd Length: 264 Bit Score: 232.04 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 720 DVGVTGTSLGETiisTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLnHIKLSANWMSPASHQGEGSKLYE 799
Cdd:cd02204 1 DAAVLRIPGETD---KGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPL-AITDCLNFGNPEKPEGEMGQLVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 800 AVQALGlDLCPALGVAIPVGKDSMSMKMKWddkeVTAPLSLNITAFAPVFNTSKTWTPLLNRntDDSVLVLVDLSAKQet 879
Cdd:cd02204 77 AVLGLG-DACRALGTPVIGGKDSLYNETEG----VAIPPTLVIGAVGVVDDVRKIVTLDFKK--EGDLLYLIGETKDE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 880 ksLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKedIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGD 959
Cdd:cd02204 148 --LGGSEYALAYHGLGGGAPPLVDLEREKALFDAVQELIKEG--LVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6321498 960 LESQLtnLFNEELGAVFQISAKNLSKFEKiLNENGVakeYISIVGK 1005
Cdd:cd02204 224 AEDEL--LFSESLGRVLVEVKPENEEVFE-AEEAGV---PATVIGT 263
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
588-1316 |
1.57e-64 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 241.08 E-value: 1.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 588 QERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVED-------PLLKTTPIDLEMPILFGKPPKMSRETITEA 660
Cdd:PHA03366 495 KNTHEGGEGVTPLDALKRACRLAGCPVHILGRTVPLPGIHFVNdlgnpvyGELRDDQFKPTFPLQPSRPLSPVSATSEDT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 661 LNLPEAnlSEIP----SLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVT------GTSLGE 730
Cdd:PHA03366 575 RPSPQD--ESIDwalfNLNSTLLQILSHPTVGSKEYIVRHIDRCGNGRVAQQPGVGPLDLPVSDYSIVvhssvkTRRAIE 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 731 TIIST--------------------------------GEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHI 778
Cdd:PHA03366 653 TPSSTedltyqeadelinspltwfdpddesvlhpavpGTCSALGEQGYKVQLDPILGAKYAIVEALTNLMLAPVANLEDI 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 779 KLSAN--WMSPASHQGEgskLYEAVQAlGLDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWT 856
Cdd:PHA03366 733 TITLSvtWPPTDQAASE---LYRALAA-CKEFCRELGVNFTFTSASSSPRQDQPPQPGPLFNTIVFTASAPVPSSTPRLT 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 857 PLLNRNtdDSVLVLVDLSAKqetKSLGASALLQVYNQVGNKSPTVYDNAILKGFleSLIQlHQQKEDIVLAYHDRSDGGL 936
Cdd:PHA03366 809 PDLKKP--GSALVHLSISPE---YTLAGSVFEQIFGLKSGTLPDISPSYLKNLF--RAVQ-HLISEGLVVSGHDVSDGGL 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 937 LITLLEMAFASRCGLEINIDGGdlESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVakeYISIVGKPSFQSQEIKII 1016
Cdd:PHA03366 881 IACLAEMALAGGRGVTITVPAG--EDPLQFLFSETPGVVIEVPPSHLSAVLTRLRSRNI---ICYPIGTVGPSGPSNTFS 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1017 NSTTNDVIYANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASitD-----DRDPGLQYALTYNPaddmkigLEL---SS 1088
Cdd:PHA03366 956 VSHNGTVLFRESLSSLRSTWRSFSDEQFELLRPDLTEESMYRK--DygnneVDLGPLEEGLTTSP-------LRLytcPD 1026
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1089 QRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFhLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVR 1168
Cdd:PHA03366 1027 KRHRVAVLLLPGCPGPHALLAAFTNAGFDPYPVSIEELKDGTF-LDEFSGLVIGGSSGAEDSYTGARAAVAALLSNPAVR 1105
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1169 SQFSKFFNeRQDTF--AFGACnGCQFLSRLK----------DIIPGCENWPSF-ERNVSEQYEARVCMVQISQekdnsSE 1235
Cdd:PHA03366 1106 DALLRFLN-RPDTFslGCGEL-GCQILFALKavgstapspvPGTETEEQWPITlEPNASGLYESRWLNFYIPE-----TT 1178
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1236 ESVFLNGMAGSKLPiAVAHGE--GkatFS-KSAEQLEKFEKDGLCCIRYvdnYG-NVTER-----FPFNPNGSTNgIAGI 1306
Cdd:PHA03366 1179 KSVALRPLRGSVLP-CWAQGThlG---FRyPNDGMEYILRNSGQIAATF---HGaDVDPGnparhYPRNPTGNSN-VAGL 1250
|
810
....*....|
gi 6321498 1307 KSPNGRVLAM 1316
Cdd:PHA03366 1251 CSADGRHLAL 1260
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
218-1036 |
1.06e-63 |
|
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273781 [Multi-domain] Cd Length: 715 Bit Score: 231.42 E-value: 1.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 218 LDSGEMEYlihaFVETMKRDPTDVELFMFAQVNSEHCRHK---IFNADWTIDGikqqftlfqmirnthklnpEYTISAYS 294
Cdd:TIGR01736 1 LSDEEMEL----IREILGREPNDTELAMFSAMWSEHCSYKsskKLLKQFPTKG-------------------PNVIQGPG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 295 DNAAVLDSENdafffapnsttkEWTstkeripLLIKVETHNHPTAVSPFPGAATGSGGEIRD---EGAtgrgsktkcglS 371
Cdd:TIGR01736 58 EDAGVVDIGD------------GYA-------VVFKMESHNHPSAIEPYNGAATGVGGILRDilsMGA-----------R 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 372 GFSVSDLLIPGNeqpweLNIGKPYHIasaLDIMIEaplGSAAFNNEFGRPCINGyfrtlttkvlnhqgkeEIRgFHK--- 448
Cdd:TIGR01736 108 PIALLDSLRFGP-----LDDPKNRYL---FEGVVA---GISDYGNRIGVPTVGG----------------EVE-FDEsyn 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 449 --PIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMErrcQQVID 526
Cdd:TIGR01736 160 gnPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEELSEEAEEEDRPAVQVGDPFTE---KLLIE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 527 ACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEI 606
Cdd:TIGR01736 237 ATLEAVDTGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEI 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 607 CKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEmpiLFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPS 686
Cdd:TIGR01736 317 FEKYELPASVIGEVTDEGRIRLYYKGEVVADLPIE---LLADAPEYERPSEPPKYPEEEKEPEPPADLEDAFLKVLSSPN 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 687 VGSKSFLI-----TIGDRSVtglidrdqfvgpwQVPVADVGV---TGTSLGetiistGEAMAMGEKPVNALISASASAKL 758
Cdd:TIGR01736 394 IASKEWVYrqydhEVQTRTV-------------VKPGEDAAVlriKETGKL------GLALTADCNPRYVYLDPYAGAAG 454
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 759 SVAESLLNIFAADVKSL---NHIklsaNWMSPashqgEGSKLY----EAVQALGlDLCPALGVAIPVGKDSMSMkmkwDD 831
Cdd:TIGR01736 455 AVAEAYRNLAAVGAEPLaavDCL----NFGNP-----ERPEVYwqfvEAVKGLG-DACRALGTPVVGGNVSLYN----ET 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 832 KEVTAPLSLNITAFAPVFNTSKTWTplLNRNTDDSVLVLVDlsakqETK-SLGASALLQ-VYNQVGNKSPTVyDNAILKG 909
Cdd:TIGR01736 521 NGVPIAPTPTIGMVGLVEDVEKLLT--SNFKKEGDAIYLIG-----ETKdELGGSEYLRvIHGIVSGQVPAV-DLEEEKE 592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 910 FLESLIQLhqQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELGAVfqISAKNLSKFEKI 989
Cdd:TIGR01736 593 LADAVREA--IRAGLVSAAHDVSRGGLAVALAEMAAASGIGAEVDIDEIASARPDELLFSESNGRA--IVAVPEEKAEEA 668
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 6321498 990 LNENGVAKEYISIVGKPSFqsqeikiiNSTTNDVIYANSRSELEQTW 1036
Cdd:TIGR01736 669 VKSKGVPAKVIGKTGGDRL--------TIKTGDDTISVSVKELRDAW 707
|
|
| FGAM-synthase |
TIGR01857 |
phosphoribosylformylglycinamidine synthase, clade II; This model represents a single-molecule ... |
207-1322 |
1.58e-61 |
|
phosphoribosylformylglycinamidine synthase, clade II; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This model represents a second clade of these enzymes found in Clostridia, Bifidobacteria and Streptococcus species. This enzyme performs the fourth step in IMP biosynthesis (the precursor of all purines) from PRPP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 130916 [Multi-domain] Cd Length: 1239 Bit Score: 231.27 E-value: 1.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 207 LSKANTELGLALDSGEMEyLIHAFVETMKRDPTDVELFMFAQVNSEHCRHKIFNA---DWTIDGIKQQFTLFQMIRNTHK 283
Cdd:TIGR01857 176 LAKFKAEQGLAMSLEDLK-FIQDYFKSIGRNPTETEIKVLDTYWSDHCRHTTFETelkHVTFSDSKFQKQLKKAYEDYLA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 284 LNPEY-------------TISA-YSDNAAVLDS-----ENDA----FFFAPNSTTKEWTstkeripLLIKVETHNHPTAV 340
Cdd:TIGR01857 255 MREELgrsekpvtlmdmaTIFAkYLRKNGKLDDlevseEINAcsveIEVDVDGVKEPWL-------LMFKNETHNHPTEI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 341 SPFPGAATGSGGEIRDEgatgrgsktkcgLSGFS--VSDLLIPGNEQPW----ELNIGK-PYHIasaldIMIEAPLGSAA 413
Cdd:TIGR01857 328 EPFGGAATCIGGAIRDP------------LSGRSyvYQAMRVTGAGDPTvpisETLKGKlPQRK-----ITTTAAHGYSS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 414 FNNEFGrpcingyfrTLTTKVlnhqgkEEIR--GFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGG 491
Cdd:TIGR01857 391 YGNQIG---------LATGQV------SEIYhpGYVAKRMEVGAVVAATPKENVVREKPEPGDVIILLGGKTGRDGIGGA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 492 AASSVASGEGSADLDFASVQRGNPEMERRCQQVI---DACvalgnnNPIQSIHDVGAGGLSNALPELVHdndlGAKFDIR 568
Cdd:TIGR01857 456 TGSSKEHTVESLELCGAEVQKGNAPEERKIQRLFrngNVT------RLIKKCNDFGAGGVSVAIGELAD----GLEIDLN 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 569 KVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATaeqklivEDPLLKT-----TPIDLEMP 643
Cdd:TIGR01857 526 KVPKKYEGLNGTELAISESQERMAVVVSPEDVDAFLAYCNEENLEATVVATVT-------EKPRLVMnwngkTIVDLSRR 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 644 ILfgkPPKMSRETITEALNLPEANLSEIP------SLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVP 717
Cdd:TIGR01857 599 FL---DTNGVRQVIDAKVVDKDVKLPEERqktsaeTLEEDWLKVLSDLNVASQKGLQERFDSSVGAGTVLMPLGGKYQLT 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 718 VADVGVTGTSLGETIISTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVkslNHIKL--------------SAN 783
Cdd:TIGR01857 676 PTEASVAKLPVLGGETHTASAIAWGFNPYIAEWSPYHGAAYAVIESLAKLVAAGA---DYKKArlsfqeyfekldkdAER 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 784 WMSPASHQgEGSklYEAVQALGLdlcPALGvaipvGKDSMSMKMkwddKEVTAPLSLniTAFA-PVFNTSKTWTPllnrn 862
Cdd:TIGR01857 753 WGKPFAAL-LGA--IKAQIDLGL---PAIG-----GKDSMSGTF----EELTVPPTL--ISFAvTTANSRRVISP----- 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 863 tddsvlvlvdlsakqETKSLGaSALLQVYNQVgNKSPTVYDNAILKGF--LESLIQLHQQKEDIVLAYhdrsdGGLLITL 940
Cdd:TIGR01857 811 ---------------EFKAAG-ENIYLIPGQA-LEDGTIDFDLLKENFaqIEELIADHKVVSASAVKY-----GGVAESL 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 941 LEMAFASRCGLEINidggdlESQLTNLFNEELGAVFqisaknlskFEkilnengvAKEYISIVGkpsfqsqeIKIINSTT 1020
Cdd:TIGR01857 869 AKMTFGNRIGAELN------NPELEDLFTAQYGSFI---------FE--------SPEELSIAN--------VEKIGQTT 917
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1021 ND-VIYAN----SRSELEQTWSktsyemqklrdnpKTAEEEFASITDDRdpGLQYALTYNPADDMKIGLELSSQRPKVAI 1095
Cdd:TIGR01857 918 ADfVLKVNgeklDLEELESAWE-------------GKLEEVFPSKFEDK--KETVEVPAVASEKKVIKAKEKVEKPRVVI 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1096 LREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGrfHLDDFIG-----------LAACGGFSYGDVLGAGAGWAKSVLYH 1164
Cdd:TIGR01857 983 PVFPGTNSEYDSAKAFEKEGAEVNLVIFRNLNEE--ALVESVEtmvdeidksqiLMLPGGFSAGDEPDGSAKFIAAILRN 1060
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1165 EGVRSQFSKFFNerQDTFAFGACNGCQFLSRL-----KDIIPGCENWPSFERNVSEQYEARVCMVQIsqekdnSSEESVF 1239
Cdd:TIGR01857 1061 PKVRVAIDSFLA--RDGLILGICNGFQALVKSgllpyGNIEAANETSPTLTYNDINRHVSKIVRTRI------ASTNSPW 1132
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1240 LNGMA-GSKLPIAVAHGEGKatFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMP 1318
Cdd:TIGR01857 1133 LSGVSvGDIHAIPVSHGEGR--FVASDEVLAELRENGQIATQYVDFNGKPSMDSKYNPNGSSLAIEGITSPDGRIFGKMG 1210
|
....
gi 6321498 1319 HPER 1322
Cdd:TIGR01857 1211 HSER 1214
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
213-1034 |
5.67e-51 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 193.40 E-value: 5.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 213 ELGLALDsgEMEYLihafVETMKRDPTDVELFMFAQVNSEHCRHK-------IF--NADWTIDGIKqqftlfqmirnthk 283
Cdd:PRK01213 10 EMGLTDD--EYERI----REILGREPNFTELGMFSVMWSEHCSYKsskpllrKFptKGPRVLQGPG-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 284 lnpeytisaysDNAAVLD-SENDAFFFapnsttkewtstkeriplliKVETHNHPTAVSPFPGAATGSGGEIRD---EGA 359
Cdd:PRK01213 70 -----------ENAGVVDiGDGQAVVF--------------------KIESHNHPSAVEPYQGAATGVGGILRDifsMGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 360 tgrgsktkcglsgfsvsdllipgneqpwelnigKPyhIASaLDimieaPL-------------------GSAAFNNEFGR 420
Cdd:PRK01213 119 ---------------------------------RP--IAL-LD-----SLrfgeldhpktryllegvvaGIGGYGNCIGV 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 421 PCINGyfrtlttkvlnhqgkeEIRgFHK-----PIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGgaaSS 495
Cdd:PRK01213 158 PTVGG----------------EVY-FDEsyngnPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGG---AS 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 496 VAS---GEGSADlDFASVQRGNPEMERRcqqVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLS 572
Cdd:PRK01213 218 FASaelSEESEE-KRPAVQVGDPFMEKL---LIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPL 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 573 LEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVE-------DpllktTPIDLempiL 645
Cdd:PRK01213 294 REEGMTPYEIMLSESQERMLLVVKPGKEEEVLAIFEKWDLDAAVIGEVTDDGRLRVYhhgevvaD-----VPAEA----L 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 646 FGKPPKMSRETITEAlnLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLI-----TIGDRSVtglidrdqfvgpwQVPVAD 720
Cdd:PRK01213 365 ADEAPVYDRPYKEPA--YLDELQADPEDLKEALLKLLSSPNIASKEWVYeqydhEVQTNTV-------------VKPGGD 429
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 721 VGV-----TGTSLgetiistgeAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSL---NHIklsaNWMSPashqg 792
Cdd:PRK01213 430 AAVlrirgGGKGL---------ALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATPLaitDCL----NFGNP----- 491
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 793 EGSKLY----EAVQALGlDLCPALGvaIPV--GKdsmsmkmkwddkeVtaplSL-NITAFAPVFNT------------SK 853
Cdd:PRK01213 492 EKPEVMwqfvEAVRGLA-DACRALG--TPVvgGN-------------V----SLyNETGGTAIYPTpvigmvgliddvSK 551
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 854 TwTPLLNRNTDDSVLVLvdlsakQETK-SLGASALLQV-YNQVGNKSPTVyDNAILKGFLESLIQLhqQKEDIVLAYHDR 931
Cdd:PRK01213 552 R-TTSGFKKEGDLIYLL------GETKdELGGSEYLKViHGHVGGRPPKV-DLEAEKRLQELVREA--IREGLVTSAHDV 621
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 932 SDGGLLITLLEMAFASRCGLEINIDGGDLESQLtnLFNEELG-AVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFqs 1010
Cdd:PRK01213 622 SEGGLAVALAEMAIAGGLGAEVDLSDGLRPDAL--LFSESQGrYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDAL-- 697
|
890 900
....*....|....*....|....
gi 6321498 1011 qEIKIINSTTNDVIYANSRSELEQ 1034
Cdd:PRK01213 698 -KVKGNDTESLEELREAWEGALPR 720
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
736-989 |
9.90e-41 |
|
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100029 [Multi-domain] Cd Length: 272 Bit Score: 151.68 E-value: 9.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 736 GEAMAMGEKPVNALISASASAKLSVAESLLNIfAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQALGlDLCPALGVA 815
Cdd:cd02193 2 GEAMKIEEHNHPAAIDPAAGAATGVGGAIRDI-AATGIDAKPIALSANWMASAGHPGEDAILYDAVKGVA-ELCNQLGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 816 IPVGKDSMSMKMKW----DDKEVTAPLSLNITAFAPVFNTSKTwtpLLNRNTDDSVLVLVDLSAKQEtkSLGASALLQV- 890
Cdd:cd02193 80 IPVGKDRMSMKTRWqegnEQREMTHPPSLVISAFGRVRDDRHT---LPQLSTEGNALLLIGGGKGHN--GLGGTALASVa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 891 --YNQVGNKSPTVYDNAILKGFLESLIQLHQqkEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINI-----DGGDLESQ 963
Cdd:cd02193 155 lsYRQLGDKSAQVRDPAQEKGFYEAMQALVA--AGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLaalgdDEPDMEPL 232
|
250 260
....*....|....*....|....*.
gi 6321498 964 LTNLFNEELGAVFQISAKNLSKFEKI 989
Cdd:cd02193 233 EIALFESQERGVIQVRAEDRDAVEEA 258
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
472-630 |
5.28e-39 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 142.49 E-value: 5.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 472 PGSCLIVLGGqsmlIGLGGGAASSVAsgEGSADLDFASVQRGNPEMERRCQQVIDACVALGNnnPIQSIHDVGAGGLSNA 551
Cdd:pfam02769 2 PGDVLILLGS----SGLHGAGLSLSR--KGLEDSGLAAVQLGDPLLEPTLIYVKLLLAALGG--LVKAMHDITGGGLAGA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321498 552 LPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVED 630
Cdd:pfam02769 74 LAEMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
326-618 |
8.29e-36 |
|
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 135.99 E-value: 8.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 326 PLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATgrGSKTKCGLSGFSVSDLLipgneqpwelnigkpyhiasALDIMI 405
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAM--GARPIALLASLSLSNGL--------------------EVDILE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 406 EAPLGSAAFNNEFGRPCINGYFRTLTTKvlnhqgkeeirGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGgqsml 485
Cdd:cd00396 59 DVVDGVAEACNQLGVPIVGGHTSVSPGT-----------MGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 486 iglgggaassvasgegsadldfasvqrgnpemerrcQQVIDACVALGnnnPIQSIHDVGAGGLSNALPELVHDNDLGAKF 565
Cdd:cd00396 123 ------------------------------------VDAVLELVAAG---DVHAMHDITDGGLLGTLPELAQASGVGAEI 163
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321498 566 DIRKVLSLEPGMS-----PMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVG 618
Cdd:cd00396 164 DLEAIPLDEVVRWlcvehIEEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| PRK01175 |
PRK01175 |
phosphoribosylformylglycinamidine synthase I; Provisional |
1089-1337 |
7.95e-34 |
|
phosphoribosylformylglycinamidine synthase I; Provisional
Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 131.42 E-value: 7.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1089 QRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWA---KSVLyhe 1165
Cdd:PRK01175 2 ESIRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAAERKSVSDYDCLVIPGGFSAGDYIRAGAIFAarlKAVL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1166 gvRSQFSKFFNERQdtFAFGACNGCQFLSRLkDIIPGCENWP-----SFERNVSEQYEARVCMVQISQEKdnsseeSVFL 1240
Cdd:PRK01175 79 --RKDIEEFIDEGY--PIIGICNGFQVLVEL-GLLPGFDEIAekpemALTVNESNRFECRPTYLKKENRK------CIFT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1241 NGMAGSKLPIAVAHGEGKATFSKSaEQLEKFEKDGLCCIRYVDNYGNvTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHP 1320
Cdd:PRK01175 148 KLLKKDVFQVPVAHAEGRVVFSEE-EILERLIENDQIVFRYVDENGN-YAGYPWNPNGSIYNIAGITNEKGNVIGLMPHP 225
|
250 260
....*....|....*....|...
gi 6321498 1321 ERV------CRLEANSWYPEGKY 1337
Cdd:PRK01175 226 ERAfygyqhPYWEKEEDYGDGKI 248
|
|
| FGAM_synth_I |
TIGR01737 |
phosphoribosylformylglycinamidine synthase I; In some species, ... |
1092-1324 |
5.07e-33 |
|
phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273782 [Multi-domain] Cd Length: 227 Bit Score: 127.88 E-value: 5.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1092 KVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDllegrFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEgVRsQF 1171
Cdd:TIGR01737 2 KVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYED-----GSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQE-VR-EF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1172 SKffnerQDTFAFGACNGCQFLSRLkDIIPGcenwpSFERNVSEQYEARvcmvQISQEKDNssEESVFLNGMA-GSKLPI 1250
Cdd:TIGR01737 75 AE-----KGVPVLGICNGFQILVEA-GLLPG-----ALLPNDSLRFICR----WVYLRVEN--ADTIFTKNYKkGEVIRI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321498 1251 AVAHGEGKatFSKSAEQLEKFEKDGLCCIRYVDNYGNVTErfPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVC 1324
Cdd:TIGR01737 138 PIAHGEGR--YYADDETLARLESNDQVVFRYCDEDGDVAE--EANPNGSVGNIAGIVNERGNVLGMMPHPERAS 207
|
|
| FGAR-AT_N |
pfam18076 |
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain ... |
41-174 |
5.25e-31 |
|
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT), also known as Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3), PurL and formylglycinamidine ribonucleotide (FGAM) synthase. This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide and glutamine to formylglycinamidine ribonucleotide, ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway.
Pssm-ID: 465635 [Multi-domain] Cd Length: 115 Bit Score: 117.96 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 41 YIHYVNgIAQNLSEQDTKLLEVLLTYDSALDiandplarqlndavannlPSSALGEdtyLIRVVPRSGTISPWSSKATNI 120
Cdd:pfam18076 2 YVHFVE-LEAPLSAAERARLEQLLTYGPPLE------------------EPEPEGE---LLLVTPRLGTISPWSSKATDI 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6321498 121 AHVCGLqDKVQRIERGLALLIKTVpgfPLLENLNDISLKCVYDRMTQQLYLTEP 174
Cdd:pfam18076 60 AHNCGL-DAVRRIERGIAYYLTGK---PLSAAELAALAALLHDRMTESVLTDLE 109
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
223-637 |
7.81e-27 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 117.65 E-value: 7.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 223 MEYLiHAFVETMKRDPTDVELFMFAQVNSEHCRHKifnadwtidgikqqftlfqmirNTHKLNPEYTISAYSDNAAVLdS 302
Cdd:PRK14090 1 MRYL-NILEEKLGREPTFVELQAFSVMWSEHCGYS----------------------HTKKYIRRLPKTGFEGNAGVV-N 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 303 ENDAFFFApnsttkewtstkeripllIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKtkcglsgfSVSDLLipg 382
Cdd:PRK14090 57 LDDYYSIA------------------FKIESHNHPSAIEPYNGAATGVGGIIRDVLAMGARPT--------AIFDSL--- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 383 neqpwelnigkpyHIASALDIMIEaplGSAAFNNEFGRPCINGYFRTLTTKVlnhqgkeeirgfHKPIMIAGGFGTVRPQ 462
Cdd:PRK14090 108 -------------HMSRIIDGIIE---GIADYGNSIGVPTVGGELRISSLYA------------HNPLVNVLAAGVVRND 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 463 FALKNTPITPGSCLIVLGGQSMLIGLGGGA-ASSVASGEGSADLdfaSVQRGNPEMERrcqQVIDACVALGNNNPIQSIH 541
Cdd:PRK14090 160 MLVDSKASRPGQVIVIFGGATGRDGIHGASfASEDLTGEKATKL---SIQVGDPFAEK---MLIEAFLEMVEEGLVEGAQ 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 542 DVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVG--- 618
Cdd:PRK14090 234 DLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVAevi 313
|
410 420
....*....|....*....|....*.
gi 6321498 619 -----HATAEQKLIVEDP--LLKTTP 637
Cdd:PRK14090 314 ddpiyRVMYRDDLVMEVPvqLLANAP 339
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
1092-1324 |
8.66e-24 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 100.96 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1092 KVAILREQGVNGQMEMAWCFQ-QAGFNSVDVTMTDLLegrfhLDDFIGLAACGGFSYGDVLGAGAGWAKS-VLyhEGVRs 1169
Cdd:PRK03619 2 KVAVIVFPGSNCDRDMARALRdLLGAEPEYVWHKETD-----LDGVDAVVLPGGFSYGDYLRCGAIAAFSpIM--KAVK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 1170 QFSKffnerQDTFAFGACNGCQFL--SRLkdiIPGcenwpSFERNVSEQYearVC-MVQISQEkdnsSEESVFLNGM-AG 1245
Cdd:PRK03619 74 EFAE-----KGKPVLGICNGFQILteAGL---LPG-----ALTRNASLKF---ICrDVHLRVE----NNDTPFTSGYeKG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321498 1246 SKLPIAVAHGEGKatFSKSAEQLEKFEKDGLCCIRYVDNygnvterfpfNPNGSTNGIAGIKSPNGRVLAMMPHPERVC 1324
Cdd:PRK03619 134 EVIRIPIAHGEGN--YYADEETLKRLEGNGQVVFRYCDE----------NPNGSVNDIAGIVNEKGNVLGMMPHPERAV 200
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
207-257 |
2.48e-23 |
|
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT), also known as Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3), PurL and formylglycinamidine ribonucleotide (FGAM) synthase. This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. The structure analysis of Salmonella typhimurium FGAR-AT reveals that this linker domain is made up of a long hydrophilic belt with an extended conformation.
Pssm-ID: 465632 [Multi-domain] Cd Length: 50 Bit Score: 94.07 E-value: 2.48e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6321498 207 LSKANTELGLALDSGEMEYLIHAFvETMKRDPTDVELFMFAQVNSEHCRHK 257
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYF-AGLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
736-1000 |
3.11e-15 |
|
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 76.28 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 736 GEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSlnhIKLSANWMSPASHqgEGSKLYEAVQALGlDLCPALGVA 815
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARP---IALLASLSLSNGL--EVDILEDVVDGVA-EACNQLGVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 816 IPVGKDSMSMKMKWDdkevtaPLSLNITAFApvfntsktwtpllnrntddsvLVLVDLSAKQETKSLGASALLqvynqvg 895
Cdd:cd00396 75 IVGGHTSVSPGTMGH------KLSLAVFAIG---------------------VVEKDRVIDSSGARPGDVLIL------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 896 nkspTVYDNAilkgflesliqLHQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINID----------GGDLESQLT 965
Cdd:cd00396 121 ----TGVDAV-----------LELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEaipldevvrwLCVEHIEEA 185
|
250 260 270
....*....|....*....|....*....|....*
gi 6321498 966 NLFNEELGAVFQISAKNLSKFEKILNENGVAKEYI 1000
Cdd:cd00396 186 LLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVI 220
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
881-1005 |
1.53e-09 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 58.13 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 881 SLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLhQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGD- 959
Cdd:pfam02769 16 GAGLSLSRKGLEDSGLAAVQLGDPLLEPTLIYVKLLL-AALGGLVKAMHDITGGGLAGALAEMAPASGVGAEIDLDKVPi 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6321498 960 ---LESQLTNLFNEELG-AVFQISAKNLSKFEKILNENGVAkeyISIVGK 1005
Cdd:pfam02769 95 feeLMLPLEMLLSENQGrGLVVVAPEEAEAVLAILEKEGLE---AAVIGE 141
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
471-619 |
3.40e-09 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100035 [Multi-domain] Cd Length: 264 Bit Score: 59.47 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 471 TPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDfasvqrgNPEMERRCQQVIDACVALGNnnpIQSIHDVGAGGLSN 550
Cdd:cd02204 133 KEGDLLYLIGETKDELGGSEYALAYHGLGGGAPPLV-------DLEREKALFDAVQELIKEGL---VLSAHDVSDGGLAV 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321498 551 ALPELVHDNDLGAKFDIRKVLslepgmSPMEIWCNESQERYVLGVSPQDLSIFEeiCKRERAPFAVVGH 619
Cdd:cd02204 203 ALAEMAFAGGLGAEVDLSKDD------AEDELLFSESLGRVLVEVKPENEEVFE--AEEAGVPATVIGT 263
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
879-956 |
1.28e-04 |
|
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100037 [Multi-domain] Cd Length: 298 Bit Score: 45.67 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321498 879 TKSLGASALLQVYNQVGNKSPTVYDNAIL---KGFLESLIQLHQQ---KEDIVLAYHDRSDGGLLITLLEMAFASRCGLE 952
Cdd:cd06061 158 TKGAGIEGTAILANDFEEELKKRLSEEELreaAKLFYKISVVKEAliaAEAGVTAMHDATEGGILGALWEVAEASGVGLR 237
|
....
gi 6321498 953 INID 956
Cdd:cd06061 238 IEKD 241
|
|
| |
