|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
6-1346 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 2032.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 6 PGPQALSPFRVENLIQDINNVtgSNSIKVVRSCYIHYAQVLTELSAEQKNVLEVLLTYDSpldtQNDEYSKQLFDaiked 85
Cdd:PRK05297 5 RGSPALSAFRLQKLLARLQAA--VLPVTSIYAEYVHFADLSAPLSAEEQAKLERLLTYGP----AEHEPAGRLFL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 86 kvgsdlgddtylirILPRAGTVSPWASKATNIAAVCGLDHsIKKIERGVALLIKvipgFPIADHLNELSLKSVFDRMTQT 165
Cdd:PRK05297 74 --------------VTPRPGTISPWSSKATDIAHNCGLAG-IRRIERGIAYYVE----AALSAEQRAALAALLHDRMTES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 166 LYiNEIPPMSALFHFELPKDITTFPLVsdeatGSPKELLQKTNKDLGLALDAGEIDYLVHVFVEvLKRDPTDVELFMFAQ 245
Cdd:PRK05297 135 VF-ADLDDAEALFSHHEPKPLTSVDVL-----GGGRAALEAANVELGLALAEDEIDYLVEAFTK-LGRNPTDVELMMFAQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 246 VNSEHCRHKIFNADWTIDGLKKDLSLFQMIRNTHKTTPDYIISAYSDNAAVVdtenQGFF---FAPDSTTKEWKATKETI 322
Cdd:PRK05297 208 ANSEHCRHKIFNADWTIDGEEQPKSLFKMIKNTHETNPDGVLSAYKDNAAVM----EGSKvgrFFPDPDTGRYGYHQEPA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 323 PMLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGHKQPWELDIGKPSHIASSLDIMI 402
Cdd:PRK05297 284 HILMKVETHNHPTAISPFPGAATGSGGEIRDEGATGRGSKPKAGLTGFSVSNLRIPGFEQPWEEDYGKPERIASALDIMI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 403 EAPLGSAAFNNEFGRPCINGYFRTLTTKVKNTQnkEEIRGFHKPIMIAGGLGTVRPKFALKnKPITAGSPIIVLGGESML 482
Cdd:PRK05297 364 EGPLGGAAFNNEFGRPNLLGYFRTFEQKVNSHN--EEVRGYHKPIMLAGGIGNIRADHVQK-GEIPVGAKLIVLGGPAMR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 483 IGLGGGAASSVASGEGSAELDFASVQRGNPEMERRCQQVIDACVSLGDANPIQSIHDVGAGGLSNALPELVHDSGLGAKF 562
Cdd:PRK05297 441 IGLGGGAASSMASGQSSEDLDFASVQRGNPEMERRCQEVIDRCWQLGDDNPILSIHDVGAGGLSNAFPELVNDGGRGGRF 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 563 DVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFATSENRLLVEDSFLETTPINLDMSIL 642
Cdd:PRK05297 521 DLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEAICERERCPFAVVGEATEERHLTLEDSHFDNKPVDLPLDVL 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 643 FGKPPKMSREAKTEPLKLPTADLKVIpSLDEAVKRVLNLPSVASKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTN 722
Cdd:PRK05297 601 LGKPPKMHRDVKTVKAKGPALDYSGI-DLAEAVERVLRLPTVASKSFLITIGDRSVTGLVARDQMVGPWQVPVADCAVTA 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 723 TSLgDSicKTGEALAMGERPVNALISAAASAKLSVAESLLNLFAADVKSLKHVKLSANWMSPASHQGEGSKLYEAVQAIG 802
Cdd:PRK05297 680 ASY-DG--YAGEAMAMGERTPVALLDAAASARMAVGEALTNIAAAPIGDLKRIKLSANWMAAAGHPGEDARLYDAVKAVG 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 803 LDLCPELGVSIPVGKDSMSMKMKWDD----KEVTAPLSLNITAFSPVSDTSKTWTPLLKKDSDSVLVLVDLAAKKEKsLG 878
Cdd:PRK05297 757 MELCPALGITIPVGKDSLSMKTKWQEggedKEVTSPLSLIISAFAPVEDVRKTLTPQLRTDKDTALLLIDLGRGKNR-LG 835
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 879 GSALLQVFNQVGDSSPTVHDNRTLRGLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVKIPVQDDAVFKS 958
Cdd:PRK05297 836 GSALAQVYNQLGDKAPDVDDAEDLKGFFNAIQALVAEGLLLAYHDRSDGGLLTTLAEMAFAGHCGLDIDLDALGDDALAA 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 959 LFSEELGAVFQISASKLETFQQILSKHNVTDEYIEIvGSPDfNSQQIKIADaNDSVIFEDTRGKLQQVWSSTSYQMQRLR 1038
Cdd:PRK05297 916 LFNEELGAVIQVRAADRDAVEAILAEHGLSDCVHVI-GKPN-AGDRIVITR-NGKTVFSESRTELRRWWSETSYQMQRLR 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1039 DNPKYADEEFANILDDKDPGLHYTLTFDPSDDLEIPKTLNTIRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLI 1118
Cdd:PRK05297 993 DNPECADQEFDAILDQADPGLNVKLTFDPNEDIAAPFIATGARPKVAILREQGVNSHVEMAAAFDRAGFDAIDVHMSDLL 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1119 DGRVHLDDFVGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRQQFVKFFqEREDTFAFGACNGCQFLTRLKDLIPGCENWP 1198
Cdd:PRK05297 1073 AGRVTLEDFKGLVACGGFSYGDVLGAGEGWAKSILFNPRLRDQFEAFF-ARPDTFALGVCNGCQMMSNLKEIIPGAEHWP 1151
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1199 TMERNFSEQYEARVCMVEITDetgnEKSVFLNGMGGSKFPIAVAHGEGRAKFANDgALQKFESGDLGSIRYVDNYGNVTQ 1278
Cdd:PRK05297 1152 RFVRNRSEQFEARFSLVEVQE----SPSIFLQGMAGSRLPIAVAHGEGRAEFPDA-HLAALEAKGLVALRYVDNHGQVTE 1226
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130388545 1279 RFPYNPNGSVNGIAGIRSPNGRVLAMMPHPERVCRLEANSWYPEgkfgEWKGYGPWIRLFRNARKWVG 1346
Cdd:PRK05297 1227 TYPANPNGSPNGITGLTTADGRVTIMMPHPERVFRTVQNSWHPE----EWGEDSPWMRMFRNARKWVG 1290
|
|
| FGAM_synt |
TIGR01735 |
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
7-1345 |
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: 1619.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 7 GPQALSPFRVENLIQDINNvTGSNsIKVVRSCYIHYAQVLTELSAEQKNVLEVLLTYDSPLDTQndeyskqlfdaikEDK 86
Cdd:TIGR01735 4 GPSALSGFRLEKLLQKLQT-KVPE-LTGVYAEFCYFVGWESALTADEEEKLQLLLLAGSVLEPP-------------QSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 87 VGSdlgddtYLIRILPRAGTVSPWASKATNIAAVCGLDhSIKKIERGVALLIKVipGFPIADHLNELSLKSVFDRMTQTL 166
Cdd:TIGR01735 69 LGR------GLLEVGPRLGTISPWSSKATSIARNCGLA-KVDRIERGRRYYLSG--AHPLSEEQEAQAAALLHDRMTESV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 167 YINEIPpMSALFHFELPKDITTFPLVsdeatGSPKELLQKTNKDLGLALDAGEIDYLVHVFVEvLKRDPTDVELFMFAQV 246
Cdd:TIGR01735 140 LPHEIE-AFELFSVPEPLNLTTIDVL-----GGGRLALEKANQELGLALDEDEIDYLTKRFQE-LQRNPSDVELMMFAQA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 247 NSEHCRHKIFNADWTIDGLKKDLSLFQMIRNTHKTTPDYIISAYSDNAAVVDTENQGFFFAPDSTTKEWKATKE-TIPML 325
Cdd:TIGR01735 213 NSEHCRHKIFNADWIIDGKKQDKSLFQMIKSTHEANPENTVSAYKDNSSVIEGHKVGRLRPDPPTRPEYRQHQEdLVHIL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 326 IKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGHKQPWELDIGKPSHIASSLDIMIEAP 405
Cdd:TIGR01735 293 MKVETHNHPTAIAPFPGASTGAGGEIRDEGATGRGAKPKAGLTGFCVSNLNIPGLEQPWEDPFQKPERIASPLDIMIEAP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 406 LGSAAFNNEFGRPCINGYFRTLTTKVknTQNKEEIRGFHKPIMIAGGLGTVRPKFALKNKPiTAGSPIIVLGGESMLIGL 485
Cdd:TIGR01735 373 LGAAAFNNEFGRPNLLGYFRTFELKA--SLPGGQVRGYHKPIMLAGGIGSIDAEHIQKGEI-EPGALLIVLGGPAMLIGL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 486 GGGAASSVASGEGSAELDFASVQRGNPEMERRCQQVIDACVSLGDANPIQSIHDVGAGGLSNALPELVHDSGLGAKFDVR 565
Cdd:TIGR01735 450 GGGAASSMVSGTNTADLDFASVQRGNPEMERRCQEVIDRCWQLGEKNPIISIHDVGAGGLSNALPELIHDGGRGAVIDLR 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 566 RVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFATSENRLLVED-------------SFLET 632
Cdd:TIGR01735 530 AVPLDDPGLSPLEIWCNESQERYVLLVRAENLEIFTAICERERCPFAVVGTATGDGRLTLVDdtpvrrngqgdapSHFPN 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 633 TPINLDMSILFGKPPKMSREAKTEPlkLPTADLKVIPSLD--EAVKRVLNLPSVASKSFLITIGDRSVTGLIDRDQFVGP 710
Cdd:TIGR01735 610 NPVDLPLEVLLGKMPKMTRFVQRKA--PMLQPLDIPPGLDlhEALERVLRLPAVASKRFLITIGDRSVGGLVARDQMVGP 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 711 WQVPVADVGVTNTSLGDSickTGEALAMGERPVNALISAAASAKLSVAESLLNLFAADVKSLKHVKLSANWMSPASHQGE 790
Cdd:TIGR01735 688 WQTPLADVAVTAASFDTY---TGEAMAIGERPPKALLDPKASARLAVGEAITNLAAALVGDLSDVKLSANWMAAAGHPGE 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 791 GSKLYEAVQAIgLDLCPELGVSIPVGKDSMSMKMKWDD----KEVTAPLSLNITAFSPVSDTSKTWTPLLKKDS-DSVLV 865
Cdd:TIGR01735 765 DAALYDAVKAV-SELCPALGIAIPVGKDSLSMKTRWQDngetKSVTAPGSLVISAFAPVPDVRKTVTPDLKHDKgDSHLL 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 866 LVDLAAKKEKsLGGSALLQVFNQVGDSSPTVHDNRTLRGLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLN 945
Cdd:TIGR01735 844 LVDLGPGKNR-LGGSALAQVFGQLGGDCPDLDDPERLKAFFAVMQGLVAEGLLLAYHDRSDGGLVTTLLEMAFAGHCGLD 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 946 VKIPVQDDAVFKSLFSEELGAVFQISASKLETFQQILSKHNVTDEYIEIVGSPDFNSQQIKIadaNDSVIFEDTRGKLQQ 1025
Cdd:TIGR01735 923 VDLDALGDSLFAVLFNEELGAVIQVAKPDLAAVLELLRAAGLTALILGIGTPTGHPMIRISV---NGATLLSEKRSELRD 999
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1026 VWSSTSYQMQRLRDNPKYADEEFANILDDKDPGLHYTLTFDPSDDLEIPKTLNTIRPKVAILREQGVNGQMEMAWCFQQA 1105
Cdd:TIGR01735 1000 IWEETSFQLQRLRDNPECAEEEFEGLRDRDGPGLKLPLTFDVNEDIAAPFINKGVKPKVAILREQGVNGDREMAAAFDRA 1079
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1106 GFNSVDVTMTDLIDGRVHLDDFVGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRQQFVKFFQeREDTFAFGACNGCQFLT 1185
Cdd:TIGR01735 1080 GFEAWDVHMSDLLAGRVHLDEFRGLAACGGFSYGDVLGAGKGWAKSILFNPRLRDQFQAFFK-RPDTFSLGVCNGCQMLS 1158
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1186 RLKDLIPGCENWPTMERNFSEQYEARVCMVEITDETgnekSVFLNGMGGSKFPIAVAHGEGRAKFANDGALQKFESGDLG 1265
Cdd:TIGR01735 1159 NLLEWIPGTENWPHFVRNNSERFEARVASVRVGESP----SIMLRGMAGSRLPVAVAHGEGYAAFSSPELQAQADASGLA 1234
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1266 SIRYVDNYGNVTQRFPYNPNGSVNGIAGIRSPNGRVLAMMPHPERVCRLEANSWYPEgkfgEWKGYGPWIRLFRNARKWV 1345
Cdd:TIGR01735 1235 ALRYIDDDGNPTEAYPLNPNGSPGGIAGITSCDGRVTIMMPHPERVFRAWQNSWRPE----DWDEDTPWLRLFRNARNWL 1310
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
44-1344 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 1040.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 44 QVLTELSAEQKNVLEVLL--TYDSpldtQNDEYSKQLFDAIKEdkvgsdlGDDTYLIRILPRAGTVSPWASKATNIAAVC 121
Cdd:PLN03206 27 GLESPLSAEKLETLKWLLreTFEP----ENLGTESFLEAKKSE-------GLNAVVVEVGPRLSFTTAWSTNAVSICSAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 122 GLDhSIKKIERGVALLIkVIPGFPIADHLNELSlKSVFDRMTQTLYinEIPPMSalfhFE---LPKDITTFPLVSDeatg 198
Cdd:PLN03206 96 GLT-EVTRLERSRRYLL-FSSSPLDESQINAFA-AMVHDRMTECVY--PQPLTS----FEsgvVPEPVYTVPVMEE---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 199 sPKELLQKTNKDLGLALDAGEIDYLVHVFVEVLKRDPTDVELFMFAQVNSEHCRHKIFNADWTIDGLKKDLSLFQMIRNT 278
Cdd:PLN03206 163 -GRAALEEINKEMGLAFDEQDLDYYTRLFRDDIKRDPTNVELFDIAQSNSEHSRHWFFSGKLVIDGQPMPKTLFQMVKDT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 279 HKTTPDYIISAYSDNA-AVVDTENQGFFFAPDSTTKEWKATKETIPMLIKVETHNHPTAVSPFPGAATGSGGEIRDEGAT 357
Cdd:PLN03206 242 LKANPNNSVIGFKDNSsAIRGFVVQPLRPVSPGSPSPLAPVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 358 GRGSKTKCGLSGFSVSDLLIPGHKQPWE-LDIGKPSHIASSLDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVKNTQN 436
Cdd:PLN03206 322 GRGSFVVAGTAGYCVGNLRIEGSYAPWEdSSFVYPSNLASPLQILIDASNGASDYGNKFGEPLIQGYTRTFGMRLPNGER 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 437 KEEIrgfhKPIMIAGGLGTVRPKFALKNKPiTAGSPIIVLGGESMLIGLGGGAASSVASGEGSAELDFASVQRGNPEMER 516
Cdd:PLN03206 402 REWL----KPIMFSGGIGQIDHTHLTKGEP-DIGMLVVKIGGPAYRIGMGGGAASSMVSGQNDAELDFNAVQRGDAEMSQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 517 RCQQVIDACVSLGDANPIQSIHDVGAGGLSNALPELVHDsgLGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKD 596
Cdd:PLN03206 477 KLYRVVRACVEMGEDNPIVSIHDQGAGGNCNVVKEIIYP--KGAEIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPES 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 597 LPIFEEICKRERAPYAVVGFATSENRLLVEDSFLET-----------TPINLDMSILFGKPPKMSREAKTEPLKLPTADL 665
Cdd:PLN03206 555 RDLLQSICDRERCSMAVIGTIDGSGRVVLVDSAAPEkceanglppppPAVDLDLEKVLGDMPQKTFEFKRVANKLEPLDI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 666 KVIPSLDEAVKRVLNLPSVASKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTNTSLGDSickTGEALAMGERPVNA 745
Cdd:PLN03206 635 PPGITVMDALKRVLRLPSVCSKRFLTTKVDRCVTGLVAQQQTVGPLQIPLADVAVIAQTHTGL---TGGACAIGEQPIKG 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 746 LISAAASAKLSVAESLLNLFAADVKSLKHVKLSANWMSPASHQGEGSKLYEAVQAIGlDLCPELGVSIPVGKDSMSMKMK 825
Cdd:PLN03206 712 LVDPKAMARLAVGEALTNLVWAKVTALSDVKASGNWMYAAKLDGEGADMYDAAVALR-DAMIELGVAIDGGKDSLSMAAQ 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 826 WDDKEVTAPLSLNITAFSPVSDTSKTWTPLLKKDSDSVLVLVDLAAKKEKsLGGSALLQVFNQVGDSSPTVHDNRTLRGL 905
Cdd:PLN03206 791 AGGEVVKAPGNLVISAYVTCPDITKTVTPDLKLGDDGVLLHVDLGKGKRR-LGGSALAQAYDQIGDDCPDLDDVAYLKKA 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 906 LEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVKIPVQDDAVFKSLFSEELGAVFQISASKLETFQQILSKH 985
Cdd:PLN03206 870 FEATQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINVDLPSSGHSAFETLFAEELGLVLEVSRKNLDAVMEKLAAA 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 986 NVTDEYIEIVGSpdfnSQQIKIADANDSVIFEDTrGKLQQVWSSTSYQMQRLRDNPKYADEEFANILDDKDPglHYTLTF 1065
Cdd:PLN03206 950 GVTAEVIGQVTA----SPLIEVKVDGATCLSEKT-ASLRDMWEETSFQLEKLQRLESCVAQEKEGLKSRKAP--TWKLSF 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1066 DPSddLEIPKTLN-TIRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLIDGRVHLDDFVGLAACGGFSYGDVLGA 1144
Cdd:PLN03206 1023 TPA--FTDKKIMNaTSKPKVAIIREEGSNGDREMAAAFYAAGFEPWDVTMSDLLNGRISLDDFRGIVFVGGFSYADVLDS 1100
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1145 GAGWAKSVLYHEGVRQQFVKFFQeREDTFAFGACNGCQfLTRLKDLIPGC-----------ENWPTMERNFSEQYEARVC 1213
Cdd:PLN03206 1101 AKGWAGSIRFNEPLLQQFQEFYN-RPDTFSLGVCNGCQ-LMALLGWVPGPqvggglgaggdPSQPRFVHNESGRFECRFT 1178
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1214 MVEItdetGNEKSVFLNGMGGSKFPIAVAHGEGRAKFANDGALQKFESGDLGSIRYVDNYGNVTQRFPYNPNGSVNGIAG 1293
Cdd:PLN03206 1179 SVTI----EDSPAIMLKGMEGSTLGVWAAHGEGRAYFPDESVLDEVLKSNLAPVRYCDDDGEPTEQYPFNPNGSPLGIAA 1254
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 2130388545 1294 IRSPNGRVLAMMPHPERVCRLEANSWYPEgkfgEW----KGYGPWIRLFRNARKW 1344
Cdd:PLN03206 1255 LCSPDGRHLAMMPHPERCFLMWQFPWYPK----EWgvdpAGPSPWLKMFQNAREW 1305
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
198-1040 |
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: 882.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 198 GSPKELLQKTNKDLGLALDAGEIDYLVhvfvEVLKRDPTDVELFMFAQVNSEHCRHKIFNADWtidglkkdlSLFqmirn 277
Cdd:COG0046 7 EGGREALEEANRELGLALSDDEYDYIV----EILGRNPTDVELGMFSQMWSEHCSYKSSNALL---------KSL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 278 thKTTPDYIISAYSDNAAVVD-TENQGFffapdsttkewkatketipmLIKVETHNHPTAVSPFPGAATGSGGEIRDEGa 356
Cdd:COG0046 69 --PTEGPRVLSGPGDNAGVVDiGDGLAV--------------------VFKVESHNHPSAIEPYQGAATGVGGIIRDIF- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 357 tGRGSKTKCGLSGFSVSDLlipghKQPWeldigkpshiASSLDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVkntqn 436
Cdd:COG0046 126 -GMGARPIAGLDSLRFGNL-----DQPP----------ASPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYE----- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 437 keeirgfHKPIMIAGGLGTVRPKFALKNKPITAGSPIIVLGGESMLIGLGGGAASSVASGEGSaELDFASVQRGNPEMER 516
Cdd:COG0046 185 -------GNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDS-ELDRPAVQVGDPFMEK 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 517 RCQQVIDACvslGDANPIQSIHDVGAGGLSNALPELVHDSGLGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKD 596
Cdd:COG0046 257 RLIEAILEL---GDTGLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 597 LPIFEEICKRERAPYAVVGFATSENRLLVEDSflETTPINLDMSILFGKPPKMSREAKtEPLKLPTADLKVIPSLDEAVK 676
Cdd:COG0046 334 LEEFEAIFERWRLPAAVIGEVTDDGRLVVTDH--GETVADLPLDFLAGGAPKYHRPAK-RPAYLEPLDLPEPIDLEEALL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 677 RVLNLPSVASKSFLITIGDRSVTGLIDRDQfvgpwqvPVADVGVtnTSLGDSicKTGEALAMGERPVNALISAAASAKLS 756
Cdd:COG0046 411 RLLSSPNVASKEWLYRQYDREVGGNTVRDP-------GVADAAV--VRVDGT--YKGLAMSTGENPRYALLDPYAGARMA 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 757 VAESLLNLFAADVKSLkHVKLSANWMSPAsHQGEGSKLYEAVQAIGlDLCPELGVSIPVGKDSMSMKMKwdDKEVTAPLS 836
Cdd:COG0046 480 VAEAARNLAAVGAEPL-AITDCLNWGNPE-KPEEMAQLVEAVKGLA-DACRALGIPVPSGNVSLYNETK--DGKVAIPPT 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 837 LNITAFSPVSDTSKTWTPLLKKDSDSVLVLvdlaAKKEKSLGGSALLQVFNQVGDSSPTVhDNRTLRGLLEAIIELHNSD 916
Cdd:COG0046 555 PVIGAVGLVDDVRKTVTPDLKKEGDLLYLI----GETKNELGGSEYAQVLGQLGGEPPDV-DLEAEKALFEAVQELIREG 629
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 917 IVQAYHDVSDGGLLVTLLEMAFASRCGLNVKIP-VQDDAVFKSLFSEELG-AVFQISASKLETFQQILSKHNVTdeyIEI 994
Cdd:COG0046 630 LILAAHDVSDGGLAVALAEMAFAGGLGADIDLDaLGDLRPDAALFSESQGrAVVQVAPEDAEAVEALLAEAGLP---AHV 706
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 2130388545 995 VGSPDfNSQQIKIaDANDSVIFEDTRGKLQQVWSSTsyqMQRLRDN 1040
Cdd:COG0046 707 IGTVT-GDDRLVI-RRGGETLLSLSLAELRDAWEET---LPRLRDN 747
|
|
| GATase_5 |
pfam13507 |
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
1081-1345 |
6.17e-145 |
|
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: 440.40 E-value: 6.17e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1081 RPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLIDGRVHLDDFVGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRQ 1160
Cdd:pfam13507 1 KPRVAILREPGTNGEYEMAAAFERAGFDAVDVHMSDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1161 QFVKFFQeREDTFAFGACNGCQFLTRLKdLIPGC-----ENWPTMERNFSEQYEARVCMVEITDETgneKSVFLNGMGGS 1235
Cdd:pfam13507 81 AFEAFFN-RPDTFSLGICNGCQLLSKLG-LIPGGegdlaERWPTLTRNDSGRFESRWVNVKISEKS---PSVFLRGMDGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1236 KFPiaVAHGEGRAKFANDGALQKFESGDLGSIRYVDNYGNVTQRFPYNPNGSVNGIAGIRSPNGRVLAMMPHPERVCRLE 1315
Cdd:pfam13507 156 GLP--VAHGEGRFVFRSEEVLARLEANGQVALRYVDNAGNPTEEYPFNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPW 233
|
250 260 270
....*....|....*....|....*....|
gi 2130388545 1316 ANSWYPEgkfGEWKGYGPWIRLFRNARKWV 1345
Cdd:pfam13507 234 QWPHWPP---GEWEEVSPWLRLFRNARKWV 260
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
239-637 |
1.75e-127 |
|
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: 396.07 E-value: 1.75e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 239 ELFMFAQVNSEHCRHKIFNadwtidglkkdlSLFQMIRnthkttpdyiisaysdnaAVVdtenqgfffapdsttkewkat 318
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFK------------SLLKMIW------------------AVV--------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 319 ketipmlIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGrgSKTKCGLSGFSVSDLLIPGHKqpweldigkPSHIASSL 398
Cdd:cd02203 30 -------FKVETHNHPSAIEPFGGAATGVGGIIRDILSMG--ARPIALLDGLRFGDLDIPGYE---------PKGKLSPR 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 399 DIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVkntqnkeeirgfHKPIMIAGGLGTVRPKFALKNKPITAGSPIIVLGG 478
Cdd:cd02203 92 RILDGVVAGISDYGNCIGIPTVGGEVRFDPSYY------------GNPLVNVGCVGIVPKDHIVKSKAPGPGDLVVLVGG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 479 ESMLIGLGGGAASSVASGEGSAELDFASVQRGNPEMERRCQQVIDACVslgDANPIQSIHDVGAGGLSNALPELVHDSGL 558
Cdd:cd02203 160 RTGRDGIGGATFSSKELSENSSELDRPAVQVGDPFMEKKLQEAILEAR---ETGLIVGIQDLGAGGLSSAVSEMAAKGGL 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130388545 559 GAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFATSENRLLVEDSflETTPINL 637
Cdd:cd02203 237 GAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTDDGRLRLYYK--GEVVADL 313
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
1084-1342 |
9.03e-98 |
|
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: 312.63 E-value: 9.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1084 VAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLIDGRVHLDDFVGLAACGGFSYGDVLGAGAGWAKSVLyhegvRQQFV 1163
Cdd:cd01740 1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASPL-----LMEEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1164 KFFQEReDTFAFGACNGCQFLTRLKDLIPGCENWPTMERNFSEQYearvCMVEITDEtgNEKSVFLNG-MGGSKFPIAVA 1242
Cdd:cd01740 76 KEFAER-GGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQN----RFVTLRVE--NNDSPFTKGyMEGEVLRIPVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1243 HGEGRAKFANDGALQKFESGDLgsIRYVDNYGNVTQRFPYNPNGSVNGIAGIRSPNGRVLAMMPHPERVCRLEANswype 1322
Cdd:cd01740 149 HGEGRFYADDETLAELEENGQI--AQYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPWQW----- 221
|
250 260
....*....|....*....|
gi 2130388545 1323 gkfGEWKGYGPWIRLFRNAR 1342
Cdd:cd01740 222 ---ERLLGGSDGLKLFRNAV 238
|
|
| PurL2 |
COG0047 |
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1082-1346 |
1.00e-94 |
|
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: 303.90 E-value: 1.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1082 PKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLidgRVHLDDFVGLAACGGFSYGDVLGAGAGWAKSVlyhegVRQQ 1161
Cdd:COG0047 1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDL---RTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSP-----IMDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1162 FVKFFqeREDTFAFGACNGCQFLTRLkDLIPGceNWPTMERNFSEQYEARVCMVEITdetgNEKSVFLNGM-GGSKFPIA 1240
Cdd:COG0047 73 VREFA--RRGGLVLGICNGFQILTEL-GLLPG--IWPALTRNRSLRFICRWVYLRVE----NNDSPFTSGMeAGEVIPIP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1241 VAHGEGRAkFANDGALQKFESGDLGSIRYVDNYGNVTqrFPYNPNGSVNGIAGIRSPNGRVLAMMPHPERVCRleanSWY 1320
Cdd:COG0047 144 IAHGEGRY-VADEETLAELEANGQVAFRYVDADGNVT--YPANPNGSLNNIAGITNEDGNVLGMMPHPERAVE----PLL 216
|
250 260
....*....|....*....|....*..
gi 2130388545 1321 -PEgkfgewkGYGPWIRLFRNARKWVG 1346
Cdd:COG0047 217 gPG-------ESTDGLRIFRSAVKYFG 236
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
325-617 |
4.19e-93 |
|
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: 301.14 E-value: 4.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 325 LIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIpghkqpweldigkpshiaSSLDIMIEA 404
Cdd:cd02193 4 AMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGIDAKPIALSANWMASAGHP------------------GEDAILYDA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 405 PLGSAAFNNEFGRPCINGYFRTlTTKVKNTQNKEEIRGFHKPIMIAGGLGTVRPKFALKNKPITAGSPIIVLGGESMLIG 484
Cdd:cd02193 66 VKGVAELCNQLGLPIPVGKDRM-SMKTRWQEGNEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 485 LGGGAASSVAsgEGSAELDFASVQRGNPEMERRCQQVIDACVSLGdanPIQSIHDVGAGGLSNALPELVHDSGLGAKFDV 564
Cdd:cd02193 145 LGGTALASVA--LSYRQLGDKSAQVRDPAQEKGFYEAMQALVAAG---KLLAWHDRGAGGLLVALAELVFAGHCGVQVDL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2130388545 565 RRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFA 617
Cdd:cd02193 220 AALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEAQYGLADCVHVLGQA 272
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
227-962 |
5.34e-74 |
|
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: 261.85 E-value: 5.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 227 FVEVLKRDPTDVELFMFAQVNSEHCRHKifnadwtidGLKKDLSLFqmirnthKTTPDYIISAYSDNAAVVDTENqgfff 306
Cdd:TIGR01736 9 IREILGREPNDTELAMFSAMWSEHCSYK---------SSKKLLKQF-------PTKGPNVIQGPGEDAGVVDIGD----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 307 apdsttkEWKATketipmlIKVETHNHPTAVSPFPGAATGSGGEIRD---EGAtgrgsktkcglSGFSVSDLLIPGhkqp 383
Cdd:TIGR01736 68 -------GYAVV-------FKMESHNHPSAIEPYNGAATGVGGILRDilsMGA-----------RPIALLDSLRFG---- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 384 wELDIGKPSHIassLDIMIEaplGSAAFNNEFGRPCINGyfrtlttkvkntqnkeEIRgFHK-----PIMIAGGLGTVRP 458
Cdd:TIGR01736 119 -PLDDPKNRYL---FEGVVA---GISDYGNRIGVPTVGG----------------EVE-FDEsyngnPLVNVMCVGLVRK 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 459 KFALKNKPITAGSPIIVLGGESMLIGLGGGAASSVASGEGSAELDFASVQRGNPEMErrcQQVIDACVSLGDANPIQSIH 538
Cdd:TIGR01736 175 DDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEELSEEAEEEDRPAVQVGDPFTE---KLLIEATLEAVDTGLVKGIK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 539 DVGAGGLSNALPELVHDSGLGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFAT 618
Cdd:TIGR01736 252 DLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVIGEVT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 619 SENRLLVEdsFLETTPINLDMSILfGKPPKMSREakTEPLKLPTADLKVIP--SLDEAVKRVLNLPSVASKSFLI----- 691
Cdd:TIGR01736 332 DEGRIRLY--YKGEVVADLPIELL-ADAPEYERP--SEPPKYPEEEKEPEPpaDLEDAFLKVLSSPNIASKEWVYrqydh 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 692 TIGDRSVtglidrdqfvgpwQVPVADVGV---TNTSlgdsicKTGEALAMGERPVNALISAAASAKLSVAESLLNLFAAD 768
Cdd:TIGR01736 407 EVQTRTV-------------VKPGEDAAVlriKETG------KLGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVG 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 769 VKSLKHVKlSANWMSPashqgEGSKLY----EAVQAIGlDLCPELGVSIPVGKDSMSMkmkwDDKEVTAPLSLNITAFSP 844
Cdd:TIGR01736 468 AEPLAAVD-CLNFGNP-----ERPEVYwqfvEAVKGLG-DACRALGTPVVGGNVSLYN----ETNGVPIAPTPTIGMVGL 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 845 VSDTSKTWTPLLKKDSDSVLVLvdlaAKKEKSLGGSALLQ-VFNQVGDSSPTVhDNRTLRGLLEAIIELHNSDIVQAYHD 923
Cdd:TIGR01736 537 VEDVEKLLTSNFKKEGDAIYLI----GETKDELGGSEYLRvIHGIVSGQVPAV-DLEEEKELADAVREAIRAGLVSAAHD 611
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2130388545 924 VSDGGLLVTLLEMAFASRCGLNVKIP-VQDDAVFKSLFSE 962
Cdd:TIGR01736 612 VSRGGLAVALAEMAAASGIGAEVDIDeIASARPDELLFSE 651
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
717-977 |
8.86e-72 |
|
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: 240.90 E-value: 8.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 717 DVGVTNTSLGDsicKTGEALAMGERPVNALISAAASAKLSVAESLLNLFAADVKSLkHVKLSANWMSPASHQGEGSKLYE 796
Cdd:cd02204 1 DAAVLRIPGET---DKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPL-AITDCLNFGNPEKPEGEMGQLVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 797 AVQAIGlDLCPELGVSIPVGKDSMSMKMKWddkeVTAPLSLNITAFSPVSDTSKTWTPLLKKDsDSVLVLVDLAAKKeks 876
Cdd:cd02204 77 AVLGLG-DACRALGTPVIGGKDSLYNETEG----VAIPPTLVIGAVGVVDDVRKIVTLDFKKE-GDLLYLIGETKDE--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 877 LGGSALLQVFNQVGDSSPTVHDNRTLRGLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVKIPVqDDAVF 956
Cdd:cd02204 148 LGGSEYALAYHGLGGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSK-DDAED 226
|
250 260
....*....|....*....|.
gi 2130388545 957 KSLFSEELGAVFQISASKLET 977
Cdd:cd02204 227 ELLFSESLGRVLVEVKPENEE 247
|
|
| FGAM-synthase |
TIGR01857 |
phosphoribosylformylglycinamidine synthase, clade II; This model represents a single-molecule ... |
180-1310 |
4.24e-67 |
|
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: 248.99 E-value: 4.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 180 FELPKDITT---FPLVSDEAtgspkelLQKTNKDLGLALDAGEIDYLVHVFVEVlKRDPTDVELFMFAQVNSEHCRHKIF 256
Cdd:TIGR01857 156 SESPKEVETltgFESYDAED-------LAKFKAEQGLAMSLEDLKFIQDYFKSI-GRNPTETEIKVLDTYWSDHCRHTTF 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 257 NA---DWTIDGLK-----------------------KDLSLFQM-------IRNTHKTTpDYIISAYSDNAAV-VDTENQ 302
Cdd:TIGR01857 228 ETelkHVTFSDSKfqkqlkkayedylamreelgrseKPVTLMDMatifakyLRKNGKLD-DLEVSEEINACSVeIEVDVD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 303 GFffapdstTKEWKatketipMLIKVETHNHPTAVSPFPGAATGSGGEIRDEgatgrgsktkcgLSGFS--VSDLLIPGH 380
Cdd:TIGR01857 307 GV-------KEPWL-------LMFKNETHNHPTEIEPFGGAATCIGGAIRDP------------LSGRSyvYQAMRVTGA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 381 KQPWEldigkpsHIASSLD-------IMIEAPLGSAAFNNEFGrpcingyfrTLTTKVKntqnkeEIR--GFHKPIMIAG 451
Cdd:TIGR01857 361 GDPTV-------PISETLKgklpqrkITTTAAHGYSSYGNQIG---------LATGQVS------EIYhpGYVAKRMEVG 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 452 GLGTVRPKFALKNKPITAGSPIIVLGGESMLIGLGGGAASSVASGEGSAELDFASVQRGNPEMERRCQQVI---DACvsl 528
Cdd:TIGR01857 419 AVVAATPKENVVREKPEPGDVIILLGGKTGRDGIGGATGSSKEHTVESLELCGAEVQKGNAPEERKIQRLFrngNVT--- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 529 gdaNPIQSIHDVGAGGLSNALPELVHdsglGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRER 608
Cdd:TIGR01857 496 ---RLIKKCNDFGAGGVSVAIGELAD----GLEIDLNKVPKKYEGLNGTELAISESQERMAVVVSPEDVDAFLAYCNEEN 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 609 APYAVVGFATSENRLL----------VEDSFLETTPINLDMSIlfgKPPKMSREAKTEPLKLPTADLKvipslDEAVKRV 678
Cdd:TIGR01857 569 LEATVVATVTEKPRLVmnwngktivdLSRRFLDTNGVRQVIDA---KVVDKDVKLPEERQKTSAETLE-----EDWLKVL 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 679 LNLpSVASKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTNTSLGDSICKTGEALAMGERPVNALISAAASAKLSVA 758
Cdd:TIGR01857 641 SDL-NVASQKGLQERFDSSVGAGTVLMPLGGKYQLTPTEASVAKLPVLGGETHTASAIAWGFNPYIAEWSPYHGAAYAVI 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 759 ESLLNLFAADVKSLKhVKLS------------ANWMSPAshqgegSKLYEAVQA-IGLDLcPELGvsipvGKDSMSMKMk 825
Cdd:TIGR01857 720 ESLAKLVAAGADYKK-ARLSfqeyfekldkdaERWGKPF------AALLGAIKAqIDLGL-PAIG-----GKDSMSGTF- 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 826 wddKEVTAPLSLNITAFSpVSDTSKTWTPLLkKDSDSVLVLVDLAAKKEKSLGGSALLQVFNQvgdssptvhdnrtlrgl 905
Cdd:TIGR01857 786 ---EELTVPPTLISFAVT-TANSRRVISPEF-KAAGENIYLIPGQALEDGTIDFDLLKENFAQ----------------- 843
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 906 LEAIIELHnsDIVQAYhDVSDGGLLVTLLEMAFASRCGLNVKIPVQDDavfksLFSEELGAvFQISASKLETFQQILSKH 985
Cdd:TIGR01857 844 IEELIADH--KVVSAS-AVKYGGVAESLAKMTFGNRIGAELNNPELED-----LFTAQYGS-FIFESPEELSIANVEKIG 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 986 NVTDEYIEIVGSPDFNSQQIKIAdandsviFEdtrGKLQQVWSSTSYQMQRLRDNPKYADEEfanilddkdpglhytltf 1065
Cdd:TIGR01857 915 QTTADFVLKVNGEKLDLEELESA-------WE---GKLEEVFPSKFEDKKETVEVPAVASEK------------------ 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1066 dpsddlEIPKTLNTI-RPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLIDGRV---------HLDDFVGLAACGG 1135
Cdd:TIGR01857 967 ------KVIKAKEKVeKPRVVIPVFPGTNSEYDSAKAFEKEGAEVNLVIFRNLNEEALvesvetmvdEIDKSQILMLPGG 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1136 FSYGDVLGAGAGWAKSVLYHEGVRQQFVKFFQerEDTFAFGACNGCQFLTRL-----KDLIPGCENWPTMERNFSEQYEA 1210
Cdd:TIGR01857 1041 FSAGDEPDGSAKFIAAILRNPKVRVAIDSFLA--RDGLILGICNGFQALVKSgllpyGNIEAANETSPTLTYNDINRHVS 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1211 RVCMVEITdetgNEKSVFLNGMG-GSKFPIAVAHGEGRAkFANDGAL-QKFESGDLGSiRYVDNYGNVTQRFPYNPNGSV 1288
Cdd:TIGR01857 1119 KIVRTRIA----STNSPWLSGVSvGDIHAIPVSHGEGRF-VASDEVLaELRENGQIAT-QYVDFNGKPSMDSKYNPNGSS 1192
|
1210 1220
....*....|....*....|..
gi 2130388545 1289 NGIAGIRSPNGRVLAMMPHPER 1310
Cdd:TIGR01857 1193 LAIEGITSPDGRIFGKMGHSER 1214
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
209-1030 |
9.59e-67 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 240.78 E-value: 9.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 209 KDLGLALDagEIDYLVhvfvEVLKRDPTDVELFMFAQVNSEHCRHKifNAdwtidglKKDLSLFqmirnthKTTPDYIIS 288
Cdd:PRK01213 9 AEMGLTDD--EYERIR----EILGREPNFTELGMFSVMWSEHCSYK--SS-------KPLLRKF-------PTKGPRVLQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 289 AYSDNAAVVDTENqgfffapdsttkEWKATketipmlIKVETHNHPTAVSPFPGAATGSGGEIRDEgatgrgsktkcgls 368
Cdd:PRK01213 67 GPGENAGVVDIGD------------GQAVV-------FKIESHNHPSAVEPYQGAATGVGGILRDI-------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 369 gFS-------VSDLLIPGhkqpwELDIGKPSHIassLDIMIEaplGSAAFNNEFGRPCINGyfrtlttkvkntqnkeEIR 441
Cdd:PRK01213 114 -FSmgarpiaLLDSLRFG-----ELDHPKTRYL---LEGVVA---GIGGYGNCIGVPTVGG----------------EVY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 442 gFHK-----PIMIAGGLGTVRPKFALKNKPITAGSPIIVLGGESMLIGLGGgaaSSVAS---GEGSAElDFASVQRGNPE 513
Cdd:PRK01213 166 -FDEsyngnPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGG---ASFASaelSEESEE-KRPAVQVGDPF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 514 MERRcqqVIDACVSLGDANPIQSIHDVGAGGLSNALPELVHDSGLGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCS 593
Cdd:PRK01213 241 MEKL---LIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVK 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 594 QKDLPIFEEICKRERAPYAVVGFATSENRLLVEdsFLETTPINLDMSILFGKPPKMSREAKtEPlKLPTADLKVIPSLDE 673
Cdd:PRK01213 318 PGKEEEVLAIFEKWDLDAAVIGEVTDDGRLRVY--HHGEVVADVPAEALADEAPVYDRPYK-EP-AYLDELQADPEDLKE 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 674 AVKRVLNLPSVASKSFlitigdrsvtglIDR--DQFVGpwqvpvadvgvTNTSL---GDS----ICKTGEALAMgerpvn 744
Cdd:PRK01213 394 ALLKLLSSPNIASKEW------------VYEqyDHEVQ-----------TNTVVkpgGDAavlrIRGGGKGLAL------ 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 745 aliSAAAS-----------AKLSVAESLLNLFA------ADVKSLkhvklsaNWMSPashqgEGSKLY----EAVQAIGl 803
Cdd:PRK01213 445 ---TTDCNpryvyldpyegAKLAVAEAARNLAAvgatplAITDCL-------NFGNP-----EKPEVMwqfvEAVRGLA- 508
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 804 DLCPELGvsIPV--GKdsmsmkmkwddkeVtaplSL----NITAFSP---------VSDTSKTWTPLLKKDSDSVLVLVD 868
Cdd:PRK01213 509 DACRALG--TPVvgGN-------------V----SLynetGGTAIYPtpvigmvglIDDVSKRTTSGFKKEGDLIYLLGE 569
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 869 LAAkkekSLGGSALLQVF-NQVGDSSPTVHDNRTLRgLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVK 947
Cdd:PRK01213 570 TKD----ELGGSEYLKVIhGHVGGRPPKVDLEAEKR-LQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGLGAEVD 644
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 948 IPVQDDAvFKSLFSEELG-AVFQISASKLETFQQILSKHNVTDEYIEIVGspdfnSQQIKIADANDSVIFEdtrgkLQQV 1026
Cdd:PRK01213 645 LSDGLRP-DALLFSESQGrYVVSVPPENEEAFEALAEAAGVPATRIGVVG-----GDALKVKGNDTESLEE-----LREA 713
|
....
gi 2130388545 1027 WSST 1030
Cdd:PRK01213 714 WEGA 717
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
670-1304 |
2.47e-65 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 243.78 E-value: 2.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 670 SLDEAVKRVLNLPSVASKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTNTSL---------GDSI----------- 729
Cdd:PHA03366 589 NLNSTLLQILSHPTVGSKEYIVRHIDRCGNGRVAQQPGVGPLDLPVSDYSIVVHSSvktrraietPSSTedltyqeadel 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 730 -------------CKT-----GEALAMGERPVNALISAAASAKLSVAESLLNLFAADVKSLKHVKLSAN--WMSPASHQG 789
Cdd:PHA03366 669 inspltwfdpddeSVLhpavpGTCSALGEQGYKVQLDPILGAKYAIVEALTNLMLAPVANLEDITITLSvtWPPTDQAAS 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 790 EgskLYEAVQAiGLDLCPELGVSIPVGKDSMSMKMKWDDKEVTAPLSLNITAFSPVSDTSKTWTPLLKKdSDSVLVLvdL 869
Cdd:PHA03366 749 E---LYRALAA-CKEFCRELGVNFTFTSASSSPRQDQPPQPGPLFNTIVFTASAPVPSSTPRLTPDLKK-PGSALVH--L 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 870 AAKKEKSLGGSALLQVFNQVGDSSPTVhDNRTLRGLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVKIP 949
Cdd:PHA03366 822 SISPEYTLAGSVFEQIFGLKSGTLPDI-SPSYLKNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALAGGRGVTITVP 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 950 VQDDAVFKsLFSEELGAVFQISASKLETFQQILSKHNVTDEYIEIVGSPDfNSQQIKIADaNDSVIFEDTRGKLQQVWSS 1029
Cdd:PHA03366 901 AGEDPLQF-LFSETPGVVIEVPPSHLSAVLTRLRSRNIICYPIGTVGPSG-PSNTFSVSH-NGTVLFRESLSSLRSTWRS 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1030 TSYQMQRLRDNPKYADEEFA-----NILDDKDPGLHytLTFDPsddLEIPKTlNTIRPKVAILREQGVNGQMEMAWCFQQ 1104
Cdd:PHA03366 978 FSDEQFELLRPDLTEESMYRkdygnNEVDLGPLEEG--LTTSP---LRLYTC-PDKRHRVAVLLLPGCPGPHALLAAFTN 1051
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1105 AGFNSVDVTMTDLIDGRvHLDDFVGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRQQFVKFFQeREDTF--AFGACnGCQ 1182
Cdd:PHA03366 1052 AGFDPYPVSIEELKDGT-FLDEFSGLVIGGSSGAEDSYTGARAAVAALLSNPAVRDALLRFLN-RPDTFslGCGEL-GCQ 1128
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1183 FLTRLK----------DLIPGCENWP-TMERNFSEQYEARVCMVEITDETgneKSVFLNGMGGSKFPiAVAHGEG-RAKF 1250
Cdd:PHA03366 1129 ILFALKavgstapspvPGTETEEQWPiTLEPNASGLYESRWLNFYIPETT---KSVALRPLRGSVLP-CWAQGTHlGFRY 1204
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130388545 1251 ANDGALQK----------FESGDLGSIRYVDNYgnvtqrfPYNPNGSVNgIAGIRSPNGRVLAM 1304
Cdd:PHA03366 1205 PNDGMEYIlrnsgqiaatFHGADVDPGNPARHY-------PRNPTGNSN-VAGLCSADGRHLAL 1260
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
733-992 |
6.12e-40 |
|
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: 149.37 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 733 GEALAMGERPVNALISAAASAKLSVAESLLNLfAADVKSLKHVKLSANWMSPASHQGEGSKLYEAVQAIGlDLCPELGVS 812
Cdd:cd02193 2 GEAMKIEEHNHPAAIDPAAGAATGVGGAIRDI-AATGIDAKPIALSANWMASAGHPGEDAILYDAVKGVA-ELCNQLGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 813 IPVGKDSMSMKMKW----DDKEVTAPLSLNITAFSPVSDTSKTWTPLLKKDSdsVLVLVDLAAKKEkSLGGSALLQV--- 885
Cdd:cd02193 80 IPVGKDRMSMKTRWqegnEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGN--ALLLIGGGKGHN-GLGGTALASVals 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 886 FNQVGDSSPTVHDNRTLRGLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVKI-PVQDDAVFKS-----L 959
Cdd:cd02193 157 YRQLGDKSAQVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLaALGDDEPDMEpleiaL 236
|
250 260 270
....*....|....*....|....*....|...
gi 2130388545 960 FSEELGAVFQISASKLETFQQILSKHNVTDEYI 992
Cdd:cd02193 237 FESQERGVIQVRAEDRDAVEEAQYGLADCVHVL 269
|
|
| PRK01175 |
PRK01175 |
phosphoribosylformylglycinamidine synthase I; Provisional |
1082-1324 |
1.82e-38 |
|
phosphoribosylformylglycinamidine synthase I; Provisional
Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 144.90 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1082 PKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLIDGRVHLDDFVGLAACGGFSYGDVLGAGAGWA---KSVLYHEgv 1158
Cdd:PRK01175 4 IRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAAERKSVSDYDCLVIPGGFSAGDYIRAGAIFAarlKAVLRKD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1159 RQQFVKffqerEDTFAFGACNGCQFLTRLkDLIPGCENWP-----TMERNFSEQYEARVCMVEITdetgNEKSVFLNGMG 1233
Cdd:PRK01175 82 IEEFID-----EGYPIIGICNGFQVLVEL-GLLPGFDEIAekpemALTVNESNRFECRPTYLKKE----NRKCIFTKLLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1234 GSKFPIAVAHGEGRAKFANDGALQKFESGDLGSIRYVDNYGNvTQRFPYNPNGSVNGIAGIRSPNGRVLAMMPHPERV-- 1311
Cdd:PRK01175 152 KDVFQVPVAHAEGRVVFSEEEILERLIENDQIVFRYVDENGN-YAGYPWNPNGSIYNIAGITNEKGNVIGLMPHPERAfy 230
|
250
....*....|....*..
gi 2130388545 1312 ----CRLEANSWYPEGK 1324
Cdd:PRK01175 231 gyqhPYWEKEEDYGDGK 247
|
|
| FGAM_synth_I |
TIGR01737 |
phosphoribosylformylglycinamidine synthase I; In some species, ... |
1083-1312 |
3.04e-36 |
|
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: 137.12 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1083 KVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLIdgrvhLDDFVGLAACGGFSYGDVLGAGAGWAKSVLYHEgvrqqf 1162
Cdd:TIGR01737 2 KVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGS-----LPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1163 VKFFQEReDTFAFGACNGCQFLTRLkDLIPGcenwpTMERNFSEQYEARVCMVEITdetgNEKSVFLNGMG-GSKFPIAV 1241
Cdd:TIGR01737 71 VREFAEK-GVPVLGICNGFQILVEA-GLLPG-----ALLPNDSLRFICRWVYLRVE----NADTIFTKNYKkGEVIRIPI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130388545 1242 AHGEGRAkFANDGALQKFESGDLGSIRYVDNYGNVTQrfPYNPNGSVNGIAGIRSPNGRVLAMMPHPERVC 1312
Cdd:TIGR01737 140 AHGEGRY-YADDETLARLESNDQVVFRYCDEDGDVAE--EANPNGSVGNIAGIVNERGNVLGMMPHPERAS 207
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
323-615 |
1.52e-34 |
|
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: 132.13 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 323 PMLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATgrGSKTKCGLSGFSVSDLLipghkqpweldigkpshiasSLDIMI 402
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAM--GARPIALLASLSLSNGL--------------------EVDILE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 403 EAPLGSAAFNNEFGRPCINGYFRTLTTKVKntqnkeeirgfHKPIMIAGGLGTVRPKFALKNKPITAGSPIIVLGgesml 482
Cdd:cd00396 59 DVVDGVAEACNQLGVPIVGGHTSVSPGTMG-----------HKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 483 iglgggaassvasgegsaeldfasvqrgnpemerrcQQVIDACVSLGDANpiqSIHDVGAGGLSNALPELVHDSGLGAKF 562
Cdd:cd00396 123 ------------------------------------VDAVLELVAAGDVH---AMHDITDGGLLGTLPELAQASGVGAEI 163
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2130388545 563 DVRRVLTLEPGMS-----PMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVG 615
Cdd:cd00396 164 DLEAIPLDEVVRWlcvehIEEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
469-623 |
2.05e-33 |
|
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: 126.31 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 469 AGSPIIVLGGesmlIGLGGGAASSVAsgEGSAELDFASVQRGNPEMERRCQQVIDACVSLGdaNPIQSIHDVGAGGLSNA 548
Cdd:pfam02769 2 PGDVLILLGS----SGLHGAGLSLSR--KGLEDSGLAAVQLGDPLLEPTLIYVKLLLAALG--GLVKAMHDITGGGLAGA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130388545 549 LPELVHDSGLGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFATSENRL 623
Cdd:pfam02769 74 LAEMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRL 148
|
|
| FGAR-AT_N |
pfam18076 |
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain ... |
39-178 |
2.95e-29 |
|
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: 112.95 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 39 YIHYAQVLTELSAEQKNVLEVLLTYDSPLDTQNDEYSkqlfdaikedkvgsdlgddtyLIRILPRAGTVSPWASKATNIA 118
Cdd:pfam18076 2 YVHFVELEAPLSAAERARLEQLLTYGPPLEEPEPEGE---------------------LLLVTPRLGTISPWSSKATDIA 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 119 AVCGLDHsIKKIERGVALLIKvipGFPIADHLNELSLKSVFDRMTQTLYiNEIPPMSALF 178
Cdd:pfam18076 61 HNCGLDA-VRRIERGIAYYLT---GKPLSAAELAALAALLHDRMTESVL-TDLEDAAALF 115
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
1083-1312 |
4.10e-27 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 110.59 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1083 KVAILREQGVNGQMEMAWCFQ-QAGFNSVDV--TMTDLidgrvhlDDFVGLAACGGFSYGDVLGAGAGWAKS-VLyhEGV 1158
Cdd:PRK03619 2 KVAVIVFPGSNCDRDMARALRdLLGAEPEYVwhKETDL-------DGVDAVVLPGGFSYGDYLRCGAIAAFSpIM--KAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 1159 RQqFVKffqerEDTFAFGACNGCQFLTRLkDLIPGcenwpTMERNFSEQYearVC-MVEITDEtgNEKSVFLNGMG-GSK 1236
Cdd:PRK03619 73 KE-FAE-----KGKPVLGICNGFQILTEA-GLLPG-----ALTRNASLKF---ICrDVHLRVE--NNDTPFTSGYEkGEV 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130388545 1237 FPIAVAHGEGRAkFANDGALQKFESGDLGSIRYVDNygnvtqrfpyNPNGSVNGIAGIRSPNGRVLAMMPHPERVC 1312
Cdd:PRK03619 136 IRIPIAHGEGNY-YADEETLKRLEGNGQVVFRYCDE----------NPNGSVNDIAGIVNEKGNVLGMMPHPERAV 200
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
222-625 |
3.82e-26 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 115.34 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 222 YLvHVFVEVLKRDPTDVELFMFAQVNSEHCRHKifnadwtidglkkdlslfqmirNTHKTTPDYIISAYSDNAAVVDTeN 301
Cdd:PRK14090 3 YL-NILEEKLGREPTFVELQAFSVMWSEHCGYS----------------------HTKKYIRRLPKTGFEGNAGVVNL-D 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 302 QGFFFApdsttkewkatketipmlIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKtkcglsgfSVSDLLipghk 381
Cdd:PRK14090 59 DYYSIA------------------FKIESHNHPSAIEPYNGAATGVGGIIRDVLAMGARPT--------AIFDSL----- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 382 qpweldigkpsHIASSLDIMIEaplGSAAFNNEFGRPCINGYFRtlttkVKNTQNkeeirgfHKPIMIAGGLGTVRPKFA 461
Cdd:PRK14090 108 -----------HMSRIIDGIIE---GIADYGNSIGVPTVGGELR-----ISSLYA-------HNPLVNVLAAGVVRNDML 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 462 LKNKPITAGSPIIVLGGESMLIGLGGGA-ASSVASGEGSAELdfaSVQRGNPEMERrcqQVIDACVSLGDANPIQSIHDV 540
Cdd:PRK14090 162 VDSKASRPGQVIVIFGGATGRDGIHGASfASEDLTGEKATKL---SIQVGDPFAEK---MLIEAFLEMVEEGLVEGAQDL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 541 GAGGLSNALPELVHDSGLGAKFDVRRVLTLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEEICKRERAPYAVVGFATSE 620
Cdd:PRK14090 236 GAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVAEVIDD 315
|
....*
gi 2130388545 621 NRLLV 625
Cdd:PRK14090 316 PIYRV 320
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
204-254 |
5.94e-24 |
|
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: 95.61 E-value: 5.94e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2130388545 204 LQKTNKDLGLALDAGEIDYLVHVFVEvLKRDPTDVELFMFAQVNSEHCRHK 254
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYFAG-LGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
733-992 |
5.53e-17 |
|
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: 81.29 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 733 GEALAMGERPVNALISAAASAKLSVAESLLNLFAADVKSLKhvkLSANWMSPASHqgEGSKLYEAVQAIGlDLCPELGVS 812
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIA---LLASLSLSNGL--EVDILEDVVDGVA-EACNQLGVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 813 IPVGKDSMSMKMKWDdkevtaPLSLNITAFSpVSDTSKTWTPLLKKDSDSVLVLVdlaakkekslggsallqvfnqvgds 892
Cdd:cd00396 75 IVGGHTSVSPGTMGH------KLSLAVFAIG-VVEKDRVIDSSGARPGDVLILTG------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 893 sptvhdnrtlrglLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNVKI-PVQDDAVFKSL----------FS 961
Cdd:cd00396 123 -------------VDAVLELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLeAIPLDEVVRWLcvehieeallFN 189
|
250 260 270
....*....|....*....|....*....|.
gi 2130388545 962 EELGAVFQISASKLETFQQILSKHNVTDEYI 992
Cdd:cd00396 190 SSGGLLIAVPAEEADAVLLLLNGNGIDAAVI 220
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
877-1000 |
3.71e-11 |
|
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: 62.75 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 877 LGGSALLQVFNQVGDS---SPTVHDNRTLRGLLEAIIEL-HNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNV---KIP 949
Cdd:pfam02769 14 LHGAGLSLSRKGLEDSglaAVQLGDPLLEPTLIYVKLLLaALGGLVKAMHDITGGGLAGALAEMAPASGVGAEIdldKVP 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2130388545 950 VQDDAVFKS--LFSEELG-AVFQISASKLETFQQILSKHNVTDEYI-EIVGSPDF 1000
Cdd:pfam02769 94 IFEELMLPLemLLSENQGrGLVVVAPEEAEAVLAILEKEGLEAAVIgEVTAGGRL 148
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
389-615 |
4.94e-08 |
|
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: 55.62 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 389 GKPSHIASSL---------DIM---IEAPLGSAAFNNEFGRPCINGyfrtlttKV--KNTQNKEEIrgfhKPIMIAGGLG 454
Cdd:cd02204 50 ADPLAITDCLnfgnpekpeGEMgqlVEAVLGLGDACRALGTPVIGG-------KDslYNETEGVAI----PPTLVIGAVG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 455 TVRPKfalkNKPIT-----AGSPIIVLGGESMLIGLGGGAASSVASGEGSAELDfasvqrgNPEMERRCQQVIDACVslg 529
Cdd:cd02204 119 VVDDV----RKIVTldfkkEGDLLYLIGETKDELGGSEYALAYHGLGGGAPPLV-------DLEREKALFDAVQELI--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 530 DANPIQSIHDVGAGGLSNALPELVHDSGLGAKFDvrrvltLEPGMSPMEIWCNESQERYVLGCSQKDLPIFEeiCKRERA 609
Cdd:cd02204 185 KEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVD------LSKDDAEDELLFSESLGRVLVEVKPENEEVFE--AEEAGV 256
|
....*.
gi 2130388545 610 PYAVVG 615
Cdd:cd02204 257 PATVIG 262
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
905-987 |
1.51e-03 |
|
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: 42.46 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 905 LLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNV---KIPVQDDavfkSLFSEE-LGA------VFQISASK 974
Cdd:cd02203 199 LQEAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIdldKVPLREP----GMSPWEiWISesqermLLVVPPED 274
|
90
....*....|...
gi 2130388545 975 LETFQQILSKHNV 987
Cdd:cd02203 275 LEEFLAICKKEDL 287
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
900-953 |
3.23e-03 |
|
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: 41.04 E-value: 3.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130388545 900 RTLRGLLEAIIELHNSDI-----VQAYHDVSDGGLLVTLLEMAFASRCGLNV---KIPVQDD 953
Cdd:cd06061 187 REAAKLFYKISVVKEALIaaeagVTAMHDATEGGILGALWEVAEASGVGLRIekdKIPIRQE 248
|
|
| POLO_box_Plk4_3 |
cd13116 |
C-terminal (third) polo-box domain (PBD) of polo-like kinase 4 (Plk4/Sak); The polo-like Ser ... |
1221-1283 |
4.60e-03 |
|
C-terminal (third) polo-box domain (PBD) of polo-like kinase 4 (Plk4/Sak); The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.
Pssm-ID: 240559 Cd Length: 81 Bit Score: 37.57 E-value: 4.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130388545 1221 TGNEKSVFLNGMG-GSKFPiavaHGEGRAKFaNDGALQKFESGDLGSIRYVDNYGNVTqRFPYN 1283
Cdd:cd13116 2 SNVLKKVFVPGVGwASQLS----SGEIWVQY-NDGSQLTVSPNRSSTITYTSSDGTVT-RYNQS 59
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
898-1018 |
7.03e-03 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 40.15 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130388545 898 DNRTLRGLLEAIIELHNSDIVQAYHDVSDGGLLVTLLEMAFASRCGLNV---KIPVQDDA-------VFKSlfseeLGAV 967
Cdd:COG2144 188 PPERLRAQLELLPELAEAGLVTAAKDISNPGIIGTLGMLLECSGVGATIdldAIPRPEGVdlerwlkAFPS-----FGFL 262
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2130388545 968 FQISASKLETFQQILSKHNVTdeyIEIVGSPDfNSQQIKIADANDSVIFED 1018
Cdd:COG2144 263 LTVPPENVDEVLARFAARGIT---AAVIGEVT-DSRRLTLRDGGERATFFD 309
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