|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
12-1230 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 1932.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 12 VIAVESNHQLTPDESNKLCWLFGEAVMESEENLKGCFVGPRREMITPWSTNAVEITQNMGLEGISRIEEYFPVKDEN--- 88
Cdd:PRK05297 37 VHFADLSAPLSAEEQAKLERLLTYGPAEHEPAGRLFLVTPRPGTISPWSSKATDIAHNCGLAGIRRIERGIAYYVEAals 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 89 ---------ADYDPMLQRMYKGLDQ-NVFTTNRQPEPIIYIED-------LEVYNEKEGLALSKEEMDYLKKVEKDLGRK 151
Cdd:PRK05297 117 aeqraalaaLLHDRMTESVFADLDDaEALFSHHEPKPLTSVDVlgggraaLEAANVELGLALAEDEIDYLVEAFTKLGRN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 152 LTDSEVFGFAQINSEHCRHKIFGGTFIIDGVEQESSLFQMIKKTTQENPNKIISAYKDNVAFAEGPVVEQFAPaDHSKPd 231
Cdd:PRK05297 197 PTDVELMMFAQANSEHCRHKIFNADWTIDGEEQPKSLFKMIKNTHETNPDGVLSAYKDNAAVMEGSKVGRFFP-DPDTG- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 232 FFQVKDIKSVISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGGGKGSWPIAGTAVYMTSYPRTEEG-REWEEILPvRKW 310
Cdd:PRK05297 275 RYGYHQEPAHILMKVETHNHPTAISPFPGAATGSGGEIRDEGATGRGSKPKAGLTGFSVSNLRIPGFeQPWEEDYG-KPE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 311 LYQTPEQILIKASNGASDFGNKFGQPLICGSVLTFEHTE---NKEVYGYDKVIMLAGGVGYGTQRDCLKGTPEAGNKVVV 387
Cdd:PRK05297 354 RIASALDIMIEGPLGGAAFNNEFGRPNLLGYFRTFEQKVnshNEEVRGYHKPIMLAGGIGNIRADHVQKGEIPVGAKLIV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 388 IGGDNYRIGLGGGSVSSVDTGRYSSGIELNAVQRANAEMQKRANNVVRALCE-EEVNPVVSIHDHGSAGHVNCLSELVEE 466
Cdd:PRK05297 434 LGGPAMRIGLGGGAASSMASGQSSEDLDFASVQRGNPEMERRCQEVIDRCWQlGDDNPILSIHDVGAGGLSNAFPELVND 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 467 --CGGLIDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRFAFQQAD-GVRPF 543
Cdd:PRK05297 514 ggRGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEAICERERCPFAVVGEATEERHLTLEDSHfDNKPV 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 544 DLAVEQMFGSSPKTYMVDKTVERHYEMPKYELSKLHEYLTNVLQLEAVACKDWLTNKVDRSVTGKVARQQCQGELQLPLS 623
Cdd:PRK05297 594 DLPLDVLLGKPPKMHRDVKTVKAKGPALDYSGIDLAEAVERVLRLPTVASKSFLITIGDRSVTGLVARDQMVGPWQVPVA 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 624 DCGVVALDYRGEKGIATSIGHAPQAALADPAAGSILSVSEALTNLVWAPMAEgMDSISLSANWMWPCRsQEGEDARLYTA 703
Cdd:PRK05297 674 DCAVTAASYDGYAGEAMAMGERTPVALLDAAASARMAVGEALTNIAAAPIGD-LKRIKLSANWMAAAG-HPGEDARLYDA 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 704 VKALS-DFCCALQINVPTGKDSLSMTQKYPNG---EKVISPGTVIVSAGGEVSDVKKVVSPVLVNNEKTTLYHIDFSFDE 779
Cdd:PRK05297 752 VKAVGmELCPALGITIPVGKDSLSMKTKWQEGgedKEVTSPLSLIISAFAPVEDVRKTLTPQLRTDKDTALLLIDLGRGK 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 780 LKLGGSAFAQSLGKVGDEVPCVQDAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCFSNvEGGLEISLDKMKE 859
Cdd:PRK05297 832 NRLGGSALAQVYNQLGDKAPDVDDAEDLKGFFNAIQALVAEGLLLAYHDRSDGGLLTTLAEMAFAG-HCGLDIDLDALGD 910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 860 eDIVKILFAENPGIVIQISDKHKDEVKKILEDAGVG--YIKLGKPT-DERHILVSKDGATYQFGIDYMRDVWYSSSYLLD 936
Cdd:PRK05297 911 -DALAALFNEELGAVIQVRAADRDAVEAILAEHGLSdcVHVIGKPNaGDRIVITRNGKTVFSESRTELRRWWSETSYQMQ 989
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 937 RKQSMNGCAKARFENYKMQPvefafMPEFKGKLSqYGITPDRRTP-----SGIRAAIIREKGTNGEREMAYSLYLAGFDV 1011
Cdd:PRK05297 990 RLRDNPECADQEFDAILDQA-----DPGLNVKLT-FDPNEDIAAPfiatgARPKVAILREQGVNSHVEMAAAFDRAGFDA 1063
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1012 KDVTMTDLISGRETLEDVNMIVYCGGFSNSDVLGSAKGWAGGFLFNPKAKEALDKFYAREDTLSLGICNGCQLMMELGLI 1091
Cdd:PRK05297 1064 IDVHMSDLLAGRVTLEDFKGLVACGGFSYGDVLGAGEGWAKSILFNPRLRDQFEAFFARPDTFALGVCNGCQMMSNLKEI 1143
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1092 TPEHKEKGKMLHNDSHKFESTFVGLTIPTNRSVMFGSLSGSKLGIWVAHGEGKFSLPY-----DEDKYNVVAKY------ 1160
Cdd:PRK05297 1144 IPGAEHWPRFVRNRSEQFEARFSLVEVQESPSIFLQGMAGSRLPIAVAHGEGRAEFPDahlaaLEAKGLVALRYvdnhgq 1223
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1161 SYDEYPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQNGCYPADRknsDQVTPWIEAFVNARKWVE 1230
Cdd:PRK05297 1224 VTETYPANPNGSPNGITGLTTADGRVTIMMPHPERVFRTVQNSWHPEEW---GEDSPWMRMFRNARKWVG 1290
|
|
| FGAM_synt |
TIGR01735 |
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
13-1229 |
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: 1094.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 13 IAVESNHQLTPDESNKLCWLFGEAVMESEENL-KGCF-VGPRREMITPWSTNAVEITQNMGLEGISRIEE--------YF 82
Cdd:TIGR01735 38 VGWESALTADEEEKLQLLLLAGSVLEPPQSPLgRGLLeVGPRLGTISPWSSKATSIARNCGLAKVDRIERgrryylsgAH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 83 PVKDENAD------YDPMLQRMYKGLDQnVFTTNRQPEPI--IYI-------EDLEVYNEKEGLALSKEEMDYLKKVEKD 147
Cdd:TIGR01735 118 PLSEEQEAqaaallHDRMTESVLPHEIE-AFELFSVPEPLnlTTIdvlgggrLALEKANQELGLALDEDEIDYLTKRFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 148 LGRKLTDSEVFGFAQINSEHCRHKIFGGTFIIDGVEQESSLFQMIKKTTQENPNKIISAYKDNVAFAEGPVVEQFAPADH 227
Cdd:TIGR01735 197 LQRNPSDVELMMFAQANSEHCRHKIFNADWIIDGKKQDKSLFQMIKSTHEANPENTVSAYKDNSSVIEGHKVGRLRPDPP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 228 SKPDFFQVKDIKSVISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGGGKGSWPIAGTAVYMTSYPRTEeGRE--WEEil 305
Cdd:TIGR01735 277 TRPEYRQHQEDLVHILMKVETHNHPTAIAPFPGASTGAGGEIRDEGATGRGAKPKAGLTGFCVSNLNIP-GLEqpWED-- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 306 pvrkwLYQTPE------QILIKASNGASDFGNKFGQPLICGSVLTFE---HTENKEVYGYDKVIMLAGGVGYGTQRDCLK 376
Cdd:TIGR01735 354 -----PFQKPEriasplDIMIEAPLGAAAFNNEFGRPNLLGYFRTFElkaSLPGGQVRGYHKPIMLAGGIGSIDAEHIQK 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 377 GTPEAGNKVVVIGGDNYRIGLGGGSVSSVDTGRYSSGIELNAVQRANAEMQKRANNVVRAlCEE--EVNPVVSIHDHGSA 454
Cdd:TIGR01735 429 GEIEPGALLIVLGGPAMLIGLGGGAASSMVSGTNTADLDFASVQRGNPEMERRCQEVIDR-CWQlgEKNPIISIHDVGAG 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 455 GHVNCLSELVE--ECGGLIDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRF 532
Cdd:TIGR01735 508 GLSNALPELIHdgGRGAVIDLRAVPLDDPGLSPLEIWCNESQERYVLLVRAENLEIFTAICERERCPFAVVGTATGDGRL 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 533 AFQQADGVR--------------PFDLAVEQMFGSSPKTYMVDKTV-ERHYEMPKYELSKLHEYLTNVLQLEAVACKDWL 597
Cdd:TIGR01735 588 TLVDDTPVRrngqgdapshfpnnPVDLPLEVLLGKMPKMTRFVQRKaPMLQPLDIPPGLDLHEALERVLRLPAVASKRFL 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 598 TNKVDRSVTGKVARQQCQGELQLPLSDCGVVAL---DYRGEkgiATSIGHAPQAALADPAAGSILSVSEALTNLVWAPMA 674
Cdd:TIGR01735 668 ITIGDRSVGGLVARDQMVGPWQTPLADVAVTAAsfdTYTGE---AMAIGERPPKALLDPKASARLAVGEAITNLAAALVG 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 675 EgMDSISLSANWMWPCRsQEGEDARLYTAVKALSDFCCALQINVPTGKDSLSMTQKY-PNGEK--VISPGTVIVSAGGEV 751
Cdd:TIGR01735 745 D-LSDVKLSANWMAAAG-HPGEDAALYDAVKAVSELCPALGIAIPVGKDSLSMKTRWqDNGETksVTAPGSLVISAFAPV 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 752 SDVKKVVSPVLVNNE-KTTLYHIDFSFDELKLGGSAFAQSLGKVGDEVPCVQDAEYFRDAFLAVQELVNKGLILAGHDIS 830
Cdd:TIGR01735 823 PDVRKTVTPDLKHDKgDSHLLLVDLGPGKNRLGGSALAQVFGQLGGDCPDLDDPERLKAFFAVMQGLVAEGLLLAYHDRS 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 831 AGGLITTLLEMCFSNvEGGLEISLDKMKEeDIVKILFAENPGIVIQISDKHKDEVKKILEDAGV-GYI-KLGKPTDERHI 908
Cdd:TIGR01735 903 DGGLVTTLLEMAFAG-HCGLDVDLDALGD-SLFAVLFNEELGAVIQVAKPDLAAVLELLRAAGLtALIlGIGTPTGHPMI 980
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 909 LVSKDGAT-YQFGIDYMRDVWYSSSYLLDRKQSMNGCAKARFENYKmqpveFAFMPEFKGKLSqYGITPDRRTP---SGI 984
Cdd:TIGR01735 981 RISVNGATlLSEKRSELRDIWEETSFQLQRLRDNPECAEEEFEGLR-----DRDGPGLKLPLT-FDVNEDIAAPfinKGV 1054
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 985 R--AAIIREKGTNGEREMAYSLYLAGFDVKDVTMTDLISGRETLEDVNMIVYCGGFSNSDVLGSAKGWAGGFLFNPKAKE 1062
Cdd:TIGR01735 1055 KpkVAILREQGVNGDREMAAAFDRAGFEAWDVHMSDLLAGRVHLDEFRGLAACGGFSYGDVLGAGKGWAKSILFNPRLRD 1134
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1063 ALDKFYAREDTLSLGICNGCQLMMELGLITPEHKEKGKMLHNDSHKFESTFVGLTIPTNRSVMFGSLSGSKLGIWVAHGE 1142
Cdd:TIGR01735 1135 QFQAFFKRPDTFSLGVCNGCQMLSNLLEWIPGTENWPHFVRNNSERFEARVASVRVGESPSIMLRGMAGSRLPVAVAHGE 1214
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1143 G--KFSLPYDEDKYN----VVAKYSYDE------YPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQNGCYPADrk 1210
Cdd:TIGR01735 1215 GyaAFSSPELQAQADasglAALRYIDDDgnpteaYPLNPNGSPGGIAGITSCDGRVTIMMPHPERVFRAWQNSWRPED-- 1292
|
1290
....*....|....*....
gi 2212149261 1211 nSDQVTPWIEAFVNARKWV 1229
Cdd:TIGR01735 1293 -WDEDTPWLRLFRNARNWL 1310
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
13-1230 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 1017.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 13 IAVESnhQLTPDESNKLCWLFGEAV----MESEENLKGCF----------VGPRREMITPWSTNAVEITQNMGLEGISRI 78
Cdd:PLN03206 26 VGLES--PLSAEKLETLKWLLRETFepenLGTESFLEAKKseglnavvveVGPRLSFTTAWSTNAVSICSACGLTEVTRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 79 E---EYF-----PVKDENAD------YDPMLQRMYkglDQNV--FTTNRQPEPIIYI-------EDLEVYNEKEGLALSK 135
Cdd:PLN03206 104 ErsrRYLlfsssPLDESQINafaamvHDRMTECVY---PQPLtsFESGVVPEPVYTVpvmeegrAALEEINKEMGLAFDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 136 EEMD-YLKKVEKDLGRKLTDSEVFGFAQINSEHCRHKIFGGTFIIDGVEQESSLFQMIKKTTQENPNKIISAYKDNVAFA 214
Cdd:PLN03206 181 QDLDyYTRLFRDDIKRDPTNVELFDIAQSNSEHSRHWFFSGKLVIDGQPMPKTLFQMVKDTLKANPNNSVIGFKDNSSAI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 215 EGPVVEQFAPADHSKPDFFQVKDIKSVISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGGGKGSWPIAGTAVYMTSYPR 294
Cdd:PLN03206 261 RGFVVQPLRPVSPGSPSPLAPVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVAGTAGYCVGNLR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 295 TE-EGREWEEILPVRKWLYQTPEQILIKASNGASDFGNKFGQPLICGSVLTF-EHTENKEVYGYDKVIMLAGGVGYGTQR 372
Cdd:PLN03206 341 IEgSYAPWEDSSFVYPSNLASPLQILIDASNGASDYGNKFGEPLIQGYTRTFgMRLPNGERREWLKPIMFSGGIGQIDHT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 373 DCLKGTPEAGNKVVVIGGDNYRIGLGGGSVSSVDTGRYSSGIELNAVQRANAEMQKRANNVVRALCE-EEVNPVVSIHDH 451
Cdd:PLN03206 421 HLTKGEPDIGMLVVKIGGPAYRIGMGGGAASSMVSGQNDAELDFNAVQRGDAEMSQKLYRVVRACVEmGEDNPIVSIHDQ 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 452 GSAGHVNCLSELVEECGGLIDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHR 531
Cdd:PLN03206 501 GAGGNCNVVKEIIYPKGAEIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPESRDLLQSICDRERCSMAVIGTIDGSGR 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 532 ------------FAFQQADGVRPFDLAVEQMFGSSP-KTYMVDKTVERHYEMPKYELSKLHEYLTNVLQLEAVACKDWLT 598
Cdd:PLN03206 581 vvlvdsaapekcEANGLPPPPPAVDLDLEKVLGDMPqKTFEFKRVANKLEPLDIPPGITVMDALKRVLRLPSVCSKRFLT 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 599 NKVDRSVTGKVARQQCQGELQLPLSDCGVVALDYRGEKGIATSIGHAPQAALADPAAGSILSVSEALTNLVWAPmAEGMD 678
Cdd:PLN03206 661 TKVDRCVTGLVAQQQTVGPLQIPLADVAVIAQTHTGLTGGACAIGEQPIKGLVDPKAMARLAVGEALTNLVWAK-VTALS 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 679 SISLSANWMWPCRsQEGEDARLYTAVKALSDFCCALQINVPTGKDSLSMTQKyPNGEKVISPGTVIVSAGGEVSDVKKVV 758
Cdd:PLN03206 740 DVKASGNWMYAAK-LDGEGADMYDAAVALRDAMIELGVAIDGGKDSLSMAAQ-AGGEVVKAPGNLVISAYVTCPDITKTV 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 759 SPVLVNNEKTTLYHIDFSFDELKLGGSAFAQSLGKVGDEVPCVQDAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTL 838
Cdd:PLN03206 818 TPDLKLGDDGVLLHVDLGKGKRRLGGSALAQAYDQIGDDCPDLDDVAYLKKAFEATQDLIAKRLISAGHDISDGGLVVTL 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 839 LEMCFSnveGGLEISLD-KMKEEDIVKILFAENPGIVIQISDKHKDEVKKILEDAGVGYIKLGKPTDERHILVSKDGATY 917
Cdd:PLN03206 898 LEMAFA---GNCGINVDlPSSGHSAFETLFAEELGLVLEVSRKNLDAVMEKLAAAGVTAEVIGQVTASPLIEVKVDGATC 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 918 QFG-IDYMRDVWYSSSYLLDRKQSMNGCAKARFENYKMQPVEF---AFMPEFkgklsqygiTPDR--RTPSGIRAAIIRE 991
Cdd:PLN03206 975 LSEkTASLRDMWEETSFQLEKLQRLESCVAQEKEGLKSRKAPTwklSFTPAF---------TDKKimNATSKPKVAIIRE 1045
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 992 KGTNGEREMAYSLYLAGFDVKDVTMTDLISGRETLEDVNMIVYCGGFSNSDVLGSAKGWAGGFLFNPKAKEALDKFYARE 1071
Cdd:PLN03206 1046 EGSNGDREMAAAFYAAGFEPWDVTMSDLLNGRISLDDFRGIVFVGGFSYADVLDSAKGWAGSIRFNEPLLQQFQEFYNRP 1125
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1072 DTLSLGICNGCQLMMELGLItPEHKEKG-----------KMLHNDSHKFESTFVGLTIPTNRSVMFGSLSGSKLGIWVAH 1140
Cdd:PLN03206 1126 DTFSLGVCNGCQLMALLGWV-PGPQVGGglgaggdpsqpRFVHNESGRFECRFTSVTIEDSPAIMLKGMEGSTLGVWAAH 1204
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1141 GEGKFSLPYDEDKYNVVAK------YSYD------EYPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQNGCYPAD 1208
Cdd:PLN03206 1205 GEGRAYFPDESVLDEVLKSnlapvrYCDDdgepteQYPFNPNGSPLGIAALCSPDGRHLAMMPHPERCFLMWQFPWYPKE 1284
|
1290 1300
....*....|....*....|...
gi 2212149261 1209 -RKNSDQVTPWIEAFVNARKWVE 1230
Cdd:PLN03206 1285 wGVDPAGPSPWLKMFQNAREWCE 1307
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
117-931 |
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: 830.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 117 IYIEDLEVYNEKEGLALSKEEMDYLKKvekDLGRKLTDSEVFGFAQINSEHCRHKIFGGTFiidgveqeSSLfqmikKTT 196
Cdd:COG0046 8 GGREALEEANRELGLALSDDEYDYIVE---ILGRNPTDVELGMFSQMWSEHCSYKSSNALL--------KSL-----PTE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 197 QENpnkIISAYKDNVAFAEGpvveqfapadhskpdffqvkDIKSVISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGgg 276
Cdd:COG0046 72 GPR---VLSGPGDNAGVVDI--------------------GDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFG-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 277 KGSWPIAGTAVYMTSYPRTEEgreweeilpvrkwlyQTPEQILIKASNGASDFGNKFGQPLICGSVLTFEHTEnkevygy 356
Cdd:COG0046 127 MGARPIAGLDSLRFGNLDQPP---------------ASPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYE------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 357 DKVIMLAGGVGYGTQRDCLKG-TPEAGNKVVVIGGDNYRIGLGGGSVSSVDTGRYSSgIELNAVQRANAEMQKRANNVVR 435
Cdd:COG0046 185 GNPLVNAGGVGIIRADHIFKAkAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSE-LDRPAVQVGDPFMEKRLIEAIL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 436 ALCEEevNPVVSIHDHGSAGHVNCLSELVEE--CGGLIDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIA 513
Cdd:COG0046 264 ELGDT--GLIVGIQDMGAGGLSSASSEMAAKggLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLEEFEAIF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 514 ERERAPMYVVGETTGDHRFAFQQaDGVRPFDLAVEQMFGSSPKTYMVDKTVERHYEMPKYELSKLHEYLTNVLQLEAVAC 593
Cdd:COG0046 342 ERWRLPAAVIGEVTDDGRLVVTD-HGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLDLPEPIDLEEALLRLLSSPNVAS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 594 KDWLTNKVDRSVTGKVARQQcqgelqlPLSDCGVVALDyRGEKGIATSIGHAPQAALADPAAGSILSVSEALTNLVWAPm 673
Cdd:COG0046 421 KEWLYRQYDREVGGNTVRDP-------GVADAAVVRVD-GTYKGLAMSTGENPRYALLDPYAGARMAVAEAARNLAAVG- 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 674 AEGMDsISLSANWMWPCRsqEGEDARLYTAVKALSDFCCALQINVPTGKDSLSMTQKypnGEKVISPGTVIVSAGGEVSD 753
Cdd:COG0046 492 AEPLA-ITDCLNWGNPEK--PEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETK---DGKVAIPPTPVIGAVGLVDD 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 754 VKKVVSPVLVnNEKTTLYHIDFSFDElkLGGSAFAQSLGKVGDEVPCVqDAEYFRDAFLAVQELVNKGLILAGHDISAGG 833
Cdd:COG0046 566 VRKTVTPDLK-KEGDLLYLIGETKNE--LGGSEYAQVLGQLGGEPPDV-DLEAEKALFEAVQELIREGLILAAHDVSDGG 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 834 LITTLLEMCFSNvEGGLEISLDKMKEEDIVKILFAENPG-IVIQISDKHKDEVKKILEDAGVGYIKLGKPTDERHILVSK 912
Cdd:COG0046 642 LAVALAEMAFAG-GLGADIDLDALGDLRPDAALFSESQGrAVVQVAPEDAEAVEALLAEAGLPAHVIGTVTGDDRLVIRR 720
|
810 820
....*....|....*....|
gi 2212149261 913 DGAT-YQFGIDYMRDVWYSS 931
Cdd:COG0046 721 GGETlLSLSLAELRDAWEET 740
|
|
| GATase_5 |
pfam13507 |
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
985-1229 |
1.12e-109 |
|
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: 344.48 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 985 RAAIIREKGTNGEREMAYSLYLAGFDVKDVTMTDLISGRETLEDVNMIVYCGGFSNSDVLGSAKGWAGGFLFNPKAKEAL 1064
Cdd:pfam13507 3 RVAILREPGTNGEYEMAAAFERAGFDAVDVHMSDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRDAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1065 DKFYAREDTLSLGICNGCQLMMELGLITPEHKEKG----KMLHNDSHKFESTFVGLTIPTN-RSVMFGSLSGSklGIWVA 1139
Cdd:pfam13507 83 EAFFNRPDTFSLGICNGCQLLSKLGLIPGGEGDLAerwpTLTRNDSGRFESRWVNVKISEKsPSVFLRGMDGS--GLPVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1140 HGEGKFSLPYDE------DKYNVVAKYSYD------EYPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQNGCYPA 1207
Cdd:pfam13507 161 HGEGRFVFRSEEvlarleANGQVALRYVDNagnpteEYPFNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWQWPHWPP 240
|
250 260
....*....|....*....|..
gi 2212149261 1208 DrkNSDQVTPWIEAFVNARKWV 1229
Cdd:pfam13507 241 G--EWEEVSPWLRLFRNARKWV 260
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
156-532 |
1.23e-97 |
|
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: 314.02 E-value: 1.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 156 EVFGFAQINSEHCRHKIFggtfiidgveqeSSLFQMIkkttqenpnkiisaykDNVAFaegpvveqfapadhskpdffqv 235
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSF------------KSLLKMI----------------WAVVF---------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 236 kdiksvislKAETHNFPTTVEPFNGASTGTGGEIRDRMGGGkgSWPIAGTAVYMTSYPRTEeGREWEEILPVRKwlyqtp 315
Cdd:cd02203 31 ---------KVETHNHPSAIEPFGGAATGVGGIIRDILSMG--ARPIALLDGLRFGDLDIP-GYEPKGKLSPRR------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 316 eqILIKASNGASDFGNKFGQPLICGSVLTFEHTenkevygYDKVIMLAGGVGYGTQRDCLKG-TPEAGNKVVVIGGDNYR 394
Cdd:cd02203 93 --ILDGVVAGISDYGNCIGIPTVGGEVRFDPSY-------YGNPLVNVGCVGIVPKDHIVKSkAPGPGDLVVLVGGRTGR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 395 IGLGGGSVSSVDTGRYSSGIELNAVQRANAEMQKRANNVVRALCEEevNPVVSIHDHGSAGHVNCLSELVE--ECGGLID 472
Cdd:cd02203 164 DGIGGATFSSKELSENSSELDRPAVQVGDPFMEKKLQEAILEARET--GLIVGIQDLGAGGLSSAVSEMAAkgGLGAEID 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 473 MSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRF 532
Cdd:cd02203 242 LDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTDDGRL 301
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
986-1226 |
2.13e-86 |
|
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: 280.27 E-value: 2.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 986 AAIIREKGTNGEREMAYSLYLAGFDVKDVTMTDLISGRETLEDVNMIVYCGGFSNSDVLGSAKGWAggflFNPKAKEALd 1065
Cdd:cd01740 1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFSYGDYLRAGAIAA----ASPLLMEEV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1066 KFYAREDTLSLGICNGCQLMMELGLITPEHKEKGKMLHNDSHKFesTFVGLTIPTNRSVMFGSLS-GSKLGIWVAHGEGK 1144
Cdd:cd01740 76 KEFAERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQN--RFVTLRVENNDSPFTKGYMeGEVLRIPVAHGEGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1145 FSLPYDEDKY----NVVAKYSYD------EYPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQNGcypadrkNSDQ 1214
Cdd:cd01740 154 FYADDETLAEleenGQIAQYVDDdgnvteRYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPWQWE-------RLLG 226
|
250
....*....|..
gi 2212149261 1215 VTPWIEAFVNAR 1226
Cdd:cd01740 227 GSDGLKLFRNAV 238
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
406-1228 |
1.91e-75 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 274.59 E-value: 1.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 406 DTGRY---SSGIELNAVQRANAEMQKrannVVRALCeeevnpVVSIH-DHGSAGHVNCLSELVEECGGLIDMSKLPigDK 481
Cdd:PHA03366 391 DTPPYlyrDSGLEANKILQALKLFYS----LLPGPC------ISGSSrPLGPASVLEHLLALCPPGGLLLFLSALP--ED 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 482 TLSAKEIIANESQERMG----------------LLIKEE--------AIEHVRKIAERERAPMYVVGETT---GDHRFA- 533
Cdd:PHA03366 459 VVSGLKPFSASNRETNEeivkqyflnvycsvvfLVIKNTheggegvtPLDALKRACRLAGCPVHILGRTVplpGIHFVNd 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 534 -FQQADGVRPFD-LAVEQMFGSSPKTYMVDKTVERHYEMPKYE-----LSKLHEYLTNVLQLEAVACKDWLTNKVDRSVT 606
Cdd:PHA03366 539 lGNPVYGELRDDqFKPTFPLQPSRPLSPVSATSEDTRPSPQDEsidwaLFNLNSTLLQILSHPTVGSKEYIVRHIDRCGN 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 607 GKVARQQCQGELQLPLSDCGVVA----LDYRGEK-------------------------------------GIATSIGHA 645
Cdd:PHA03366 619 GRVAQQPGVGPLDLPVSDYSIVVhssvKTRRAIEtpsstedltyqeadelinspltwfdpddesvlhpavpGTCSALGEQ 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 646 PQAALADPAAGSILSVSEALTNLVWAPMAEgMDSISLSANWMWPcrsqEGEDAR--LYTAVKALSDFCCALQINVPTGKD 723
Cdd:PHA03366 699 GYKVQLDPILGAKYAIVEALTNLMLAPVAN-LEDITITLSVTWP----PTDQAAseLYRALAACKEFCRELGVNFTFTSA 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 724 SLSMTQKYPNGEKVISPgTVIVSAGGEVSDVKKVVSPVLVNNEkTTLYHIDFSfDELKLGGSAFAQSLGKVGDEVPCVqD 803
Cdd:PHA03366 774 SSSPRQDQPPQPGPLFN-TIVFTASAPVPSSTPRLTPDLKKPG-SALVHLSIS-PEYTLAGSVFEQIFGLKSGTLPDI-S 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 804 AEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCFSnveGGLEISLDKMKEEDIVKILFAENPGIVIQISDKHKD 883
Cdd:PHA03366 850 PSYLKNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALA---GGRGVTITVPAGEDPLQFLFSETPGVVIEVPPSHLS 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 884 EVKKILEDAGVGYIKLG---KPTDERHILVSKDGAT-YQFGIDYMRDVW---YSSSYLLDR----KQSMN----GCAKAR 948
Cdd:PHA03366 927 AVLTRLRSRNIICYPIGtvgPSGPSNTFSVSHNGTVlFRESLSSLRSTWrsfSDEQFELLRpdltEESMYrkdyGNNEVD 1006
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 949 FENYKM----QPVEFAFMPEFKGKLSQYgITPDRRTPSGIRAAIirekgTNgeremayslylAGFDVKDVTMTDLISGrE 1024
Cdd:PHA03366 1007 LGPLEEglttSPLRLYTCPDKRHRVAVL-LLPGCPGPHALLAAF-----TN-----------AGFDPYPVSIEELKDG-T 1068
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1025 TLEDVNMIVYCGGFSNSDVLGSAKGWAGGFLFNPKAKEALDKFYAREDTLSLGICN-GCQLMMELGLI--------TPEH 1095
Cdd:PHA03366 1069 FLDEFSGLVIGGSSGAEDSYTGARAAVAALLSNPAVRDALLRFLNRPDTFSLGCGElGCQILFALKAVgstapspvPGTE 1148
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1096 KEKGKMLH---NDSHKFESTFVGLTIP-TNRSVMFGSLSGSKLGIWVahgEGK---FSLPYDEDKYNVVAK-------YS 1161
Cdd:PHA03366 1149 TEEQWPITlepNASGLYESRWLNFYIPeTTKSVALRPLRGSVLPCWA---QGThlgFRYPNDGMEYILRNSgqiaatfHG 1225
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2212149261 1162 YD--------EYPGNPNGSdYSIAGLASADGRHLAMM--PHLerAIFPWQngcYPADRKNSD--QVTPWIEAFVNARKW 1228
Cdd:PHA03366 1226 ADvdpgnparHYPRNPTGN-SNVAGLCSADGRHLALLfdPSL--SFHPWQ---WQHVPPENGplKVSPWKLMFQDLHLW 1298
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
624-901 |
5.02e-69 |
|
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: 232.43 E-value: 5.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 624 DCGVVALDYRGEKGIATSIGHAPQAALADPAAGSILSVSEALTNLVWAPmAEGMDsISLSANWMWPCRsQEGEDARLYTA 703
Cdd:cd02204 1 DAAVLRIPGETDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVG-ADPLA-ITDCLNFGNPEK-PEGEMGQLVEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 704 VKALSDFCCALQINVPTGKDSLSMTQKYpngekVISPGTVIVSAGGEVSDVKKVVSPVLvNNEKTTLYHIDFSFDELklG 783
Cdd:cd02204 78 VLGLGDACRALGTPVIGGKDSLYNETEG-----VAIPPTLVIGAVGVVDDVRKIVTLDF-KKEGDLLYLIGETKDEL--G 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 784 GSAFAQSLGKVGDEVPCVQDAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCFSNvEGGLEISLDKMKEEDiv 863
Cdd:cd02204 150 GSEYALAYHGLGGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAG-GLGAEVDLSKDDAED-- 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 2212149261 864 KILFAENPGIVIQISDKHKDEVKKiLEDAGVGYIKLGK 901
Cdd:cd02204 227 ELLFSESLGRVLVEVKPENEEVFE-AEEAGVPATVIGT 263
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
133-931 |
2.78e-66 |
|
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: 238.74 E-value: 2.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 133 LSKEEMdylKKVEKDLGRKLTDSEVFGFAQINSEHCRHKifggtfiidgveqeSSLfQMIKKTTQENPNkIISAYKDNVA 212
Cdd:TIGR01736 1 LSDEEM---ELIREILGREPNDTELAMFSAMWSEHCSYK--------------SSK-KLLKQFPTKGPN-VIQGPGEDAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 213 faegpVVEqfapadhskpdffqVKDiKSVISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGggKGSWPIAGTAVYMTSY 292
Cdd:TIGR01736 62 -----VVD--------------IGD-GYAVVFKMESHNHPSAIEPYNGAATGVGGILRDILS--MGARPIALLDSLRFGP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 293 PRTEEGReweeilpvrkWLYqtpEQILikasNGASDFGNKFGQPLICGSVlTFEHTENkevygyDKVIMLAGGVGYGTQR 372
Cdd:TIGR01736 120 LDDPKNR----------YLF---EGVV----AGISDYGNRIGVPTVGGEV-EFDESYN------GNPLVNVMCVGLVRKD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 373 DCLKGT-PEAGNKVVVIGGDNYRIGLGGGSVSSVDTGRYSSGIELNAVQRANAEMQKRANNVVRALCEEEVnpVVSIHDH 451
Cdd:TIGR01736 176 DIVTGKaKGPGNKLVLVGGKTGRDGIGGATFASEELSEEAEEEDRPAVQVGDPFTEKLLIEATLEAVDTGL--VKGIKDL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 452 GSAGHVNCLSELVEECG-GL-IDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGD 529
Cdd:TIGR01736 254 GAAGLTSASSEMAAKGGlGAeIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVIGEVTDE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 530 HRFAFQQaDGVRPFDLAVEqMFGSSPktymvdkTVERHYEMPKY--------ELSKLHEYLTNVLQLEAVACKDWLTNKV 601
Cdd:TIGR01736 334 GRIRLYY-KGEVVADLPIE-LLADAP-------EYERPSEPPKYpeeekepePPADLEDAFLKVLSSPNIASKEWVYRQY 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 602 DRSVTGKVarqqcqgeLQLPLSDCGVVALDYRGEKGIATSIGHAPQAALADPAAGSILSVSEALTNLVwAPMAEGMdSIS 681
Cdd:TIGR01736 405 DHEVQTRT--------VVKPGEDAAVLRIKETGKLGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLA-AVGAEPL-AAV 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 682 LSANWMWPcrsqegEDARLY----TAVKALSDFCCALQINVPTGKDSLsmtqkYPNGEKV-ISPGTVIVSAgGEVSDVKK 756
Cdd:TIGR01736 475 DCLNFGNP------ERPEVYwqfvEAVKGLGDACRALGTPVVGGNVSL-----YNETNGVpIAPTPTIGMV-GLVEDVEK 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 757 VVsPVLVNNEKTTLYHIDFSFDElkLGGSAFAQSL-GKVGDEVPCVqDAEYFRDAFLAVQELVNKGLILAGHDISAGGLI 835
Cdd:TIGR01736 543 LL-TSNFKKEGDAIYLIGETKDE--LGGSEYLRVIhGIVSGQVPAV-DLEEEKELADAVREAIRAGLVSAAHDVSRGGLA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 836 TTLLEMCF-SNVegGLEISLDKMKEEDIVKILFAENPG-IVIQISDkhkDEVKKILEDAGVGYIKLGKPTDERhILVSKD 913
Cdd:TIGR01736 619 VALAEMAAaSGI--GAEVDIDEIASARPDELLFSESNGrAIVAVPE---EKAEEAVKSKGVPAKVIGKTGGDR-LTIKTG 692
|
810
....*....|....*...
gi 2212149261 914 GATYQFGIDYMRDVWYSS 931
Cdd:TIGR01736 693 DDTISVSVKELRDAWEEA 710
|
|
| PurL2 |
COG0047 |
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
985-1230 |
2.28e-65 |
|
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: 221.09 E-value: 2.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 985 RAAIIREKGTNGEREMAYSLYLAGFDVKDVTMTDLisgRETLEDVNMIVYCGGFSNSDVLGSAKGWAggflFNPkAKEAL 1064
Cdd:COG0047 2 KVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDL---RTDLDDFDGLVLPGGFSYGDYLRAGAIAA----FSP-IMDAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1065 DKFyAREDTLSLGICNGCQLMMELGLItPEHKEKgkMLHNDSHKFESTFVGLTIPTNRSVMFGSLS-GSKLGIWVAHGEG 1143
Cdd:COG0047 74 REF-ARRGGLVLGICNGFQILTELGLL-PGIWPA--LTRNRSLRFICRWVYLRVENNDSPFTSGMEaGEVIPIPIAHGEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1144 KFSLpyDEDKYN-------VVAKYSyDE-----YPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQngcypadrkN 1211
Cdd:COG0047 150 RYVA--DEETLAeleangqVAFRYV-DAdgnvtYPANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLL---------G 217
|
250
....*....|....*....
gi 2212149261 1212 SDQVTPWIEAFVNARKWVE 1230
Cdd:COG0047 218 PGESTDGLRIFRSAVKYFG 236
|
|
| FGAM-synthase |
TIGR01857 |
phosphoribosylformylglycinamidine synthase, clade II; This model represents a single-molecule ... |
120-1214 |
8.32e-64 |
|
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: 237.82 E-value: 8.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 120 EDLEVYNEKEGLALSKEEMDYLKKVEKDLGRKLTDSEVFGFAQINSEHCRHKIFGGtfIIDGVEQESSLFQ-MIKKTTQE 198
Cdd:TIGR01857 174 EDLAKFKAEQGLAMSLEDLKFIQDYFKSIGRNPTETEIKVLDTYWSDHCRHTTFET--ELKHVTFSDSKFQkQLKKAYED 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 199 NPNKIISAYKDN--VAFAE-GPVVEQFAPADhSKPDFFQVKDIKSVISL-----------------KAETHNFPTTVEPF 258
Cdd:TIGR01857 252 YLAMREELGRSEkpVTLMDmATIFAKYLRKN-GKLDDLEVSEEINACSVeievdvdgvkepwllmfKNETHNHPTEIEPF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 259 NGASTGTGGEIRDRMGGGKGSWP---IAGTAVYMTSYPRTEEGReweeiLPVRKwlyqtpeqILIKASNGASDFGNKFGq 335
Cdd:TIGR01857 331 GGAATCIGGAIRDPLSGRSYVYQamrVTGAGDPTVPISETLKGK-----LPQRK--------ITTTAAHGYSSYGNQIG- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 336 pLICGSVltfehtenKEVY--GYDKVIMLAGGVGYGTQRD-CLKGTPEAGNKVVVIGGDNYRIGLGGGSVSSVDTGRYSS 412
Cdd:TIGR01857 397 -LATGQV--------SEIYhpGYVAKRMEVGAVVAATPKEnVVREKPEPGDVIILLGGKTGRDGIGGATGSSKEHTVESL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 413 GIELNAVQRANAEMQKRANNVVRalceeevNPVVS-----IHDHGSAGHVNCLSELveeCGGL-IDMSKLPIGDKTLSAK 486
Cdd:TIGR01857 468 ELCGAEVQKGNAPEERKIQRLFR-------NGNVTrlikkCNDFGAGGVSVAIGEL---ADGLeIDLNKVPKKYEGLNGT 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 487 EIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRFAFQQaDGVRPFDLAVEQMFGSSPKTYMVDKTVER 566
Cdd:TIGR01857 538 ELAISESQERMAVVVSPEDVDAFLAYCNEENLEATVVATVTEKPRLVMNW-NGKTIVDLSRRFLDTNGVRQVIDAKVVDK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 567 HYEMPKYEL-----SKLHEYLTNVLQLEaVACKDWLTNKVDRSVTGKVARQQCQGELQLPLSDCGVVALD-YRGEKGIAT 640
Cdd:TIGR01857 617 DVKLPEERQktsaeTLEEDWLKVLSDLN-VASQKGLQERFDSSVGAGTVLMPLGGKYQLTPTEASVAKLPvLGGETHTAS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 641 SI--GHAPQAALADPAAGSILSVSEALTNLVwapmAEGMD--SISLSANWMWPCRSQEGED-----ARLYTAVKALSDFc 711
Cdd:TIGR01857 696 AIawGFNPYIAEWSPYHGAAYAVIESLAKLV----AAGADykKARLSFQEYFEKLDKDAERwgkpfAALLGAIKAQIDL- 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 712 calqiNVPT--GKDSLSMTqkypnGEKVISPGTVIvSAGGEVSDVKKVVSPVLvNNEKTTLYHIDFSFDElklggsafaq 789
Cdd:TIGR01857 771 -----GLPAigGKDSMSGT-----FEELTVPPTLI-SFAVTTANSRRVISPEF-KAAGENIYLIPGQALE---------- 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 790 slgkvgDEVPcvqDAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCFSNvEGGLEISlDKMKEEdivkiLFAE 869
Cdd:TIGR01857 829 ------DGTI---DFDLLKENFAQIEELIADHKVVSASAVKYGGVAESLAKMTFGN-RIGAELN-NPELED-----LFTA 892
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 870 NPG-IVIQISDkhkdevkkilEDAGVGYIKLGKPTDERHILVSkdgatyQFGIDymrdvwysssylLDRKQSMngcakar 948
Cdd:TIGR01857 893 QYGsFIFESPE----------ELSIANVEKIGQTTADFVLKVN------GEKLD------------LEELESA------- 937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 949 FENyKMQPVefafmpeFKGKLSQYGIT---PDRRTPSGIRAAIIR-EK---------GTNGEREMAYSLYLAGFDVKDVT 1015
Cdd:TIGR01857 938 WEG-KLEEV-------FPSKFEDKKETvevPAVASEKKVIKAKEKvEKprvvipvfpGTNSEYDSAKAFEKEGAEVNLVI 1009
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1016 MTDL-----ISGRETLED----VNMIVYCGGFSNSDVL-GSAKgWAGGFLFNPKAKEALDKFYAReDTLSLGICNGCQLM 1085
Cdd:TIGR01857 1010 FRNLneealVESVETMVDeidkSQILMLPGGFSAGDEPdGSAK-FIAAILRNPKVRVAIDSFLAR-DGLILGICNGFQAL 1087
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1086 MELGL-----ITPEHKEKGKMLHNDSHKFESTFVGLTIPTNRSVMFGSLS-GSKLGIWVAHGEGKFSLPYDE-----DKY 1154
Cdd:TIGR01857 1088 VKSGLlpygnIEAANETSPTLTYNDINRHVSKIVRTRIASTNSPWLSGVSvGDIHAIPVSHGEGRFVASDEVlaelrENG 1167
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2212149261 1155 NVVAKY------SYDEYPGNPNGSDYSIAGLASADGRHLAMMPHLERaifpWQNGCYPADRKNSDQ 1214
Cdd:TIGR01857 1168 QIATQYvdfngkPSMDSKYNPNGSSLAIEGITSPDGRIFGKMGHSER----YGDGLFKNIPGNKDQ 1229
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
119-931 |
1.43e-57 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 213.04 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 119 IEDLEVYNEkegLALSKEEMDylkKVEKDLGRKLTDSEVFGFAQINSEHCRHKifggtfiidgveqeSS---LfqmiKKT 195
Cdd:PRK01213 2 PDTEELYAE---MGLTDDEYE---RIREILGREPNFTELGMFSVMWSEHCSYK--------------SSkplL----RKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 196 TQENPNkIISAYKDN---VAFAEGPVVeqfapadhskpdffqvkdiksviSLKAETHNFPTTVEPFNGASTGTGGEIRD- 271
Cdd:PRK01213 58 PTKGPR-VLQGPGENagvVDIGDGQAV-----------------------VFKIESHNHPSAVEPYQGAATGVGGILRDi 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 272 -RMGggkgSWPIA-------GTAvymtSYPRTeegreweeilpvrKWLYqtpEQIlIKasnGASDFGNKFGQPLICGSVl 343
Cdd:PRK01213 114 fSMG----ARPIAlldslrfGEL----DHPKT-------------RYLL---EGV-VA---GIGGYGNCIGVPTVGGEV- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 344 TFEHTenkevygYDKVIM-LAGGVGYGTQRDCLKGT-PEAGNKVVVIGGDNYRIGLGGGSVSSVDtgrYSSGIE--LNAV 419
Cdd:PRK01213 165 YFDES-------YNGNPLvNAMCVGLVRHDDIVLAKaSGVGNPVVYVGAKTGRDGIGGASFASAE---LSEESEekRPAV 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 420 QRANAEMQKRannVVRAlCEEEVNP--VVSIHDHGSAGHVNCLSELVEEcGGL---IDMSKLPIGDKTLSAKEIIANESQ 494
Cdd:PRK01213 235 QVGDPFMEKL---LIEA-CLELIKTglVVGIQDMGAAGLTCSSSEMAAK-GGLgieLDLDKVPLREEGMTPYEIMLSESQ 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 495 ERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRFAFQQaDGVRPFDLAVEQMFGSSPkTYmvdktvERHYEMPKY- 573
Cdd:PRK01213 310 ERMLLVVKPGKEEEVLAIFEKWDLDAAVIGEVTDDGRLRVYH-HGEVVADVPAEALADEAP-VY------DRPYKEPAYl 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 574 -----ELSKLHEYLTNVLQLEAVACKDWLTNKVDRSVtgkvarqqcQGE-LQLPLSDCGVVALDyRGEKGIATSIGHAPQ 647
Cdd:PRK01213 382 delqaDPEDLKEALLKLLSSPNIASKEWVYEQYDHEV---------QTNtVVKPGGDAAVLRIR-GGGKGLALTTDCNPR 451
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 648 AALADPAAGSILSVSEALTNLVWA---PMAegmdsISLSANW--------MWpcrsqegedaRLYTAVKALSDFCCALQI 716
Cdd:PRK01213 452 YVYLDPYEGAKLAVAEAARNLAAVgatPLA-----ITDCLNFgnpekpevMW----------QFVEAVRGLADACRALGT 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 717 NVPTGKDSLsmtqkYpN--GEKVISPgTVIVSAGGEVSDVKKVVsPVLVNNEKTTLYHIDFSFDELklGGSAFAQSL-GK 793
Cdd:PRK01213 517 PVVGGNVSL-----Y-NetGGTAIYP-TPVIGMVGLIDDVSKRT-TSGFKKEGDLIYLLGETKDEL--GGSEYLKVIhGH 586
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 794 VGDEVPCVqDAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCF-SNVegGLEISLDKMKEEDIVkiLFAENPG 872
Cdd:PRK01213 587 VGGRPPKV-DLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIaGGL--GAEVDLSDGLRPDAL--LFSESQG 661
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 873 -IVIQISDKHKDEVKKILEDAGVGYIKLGKPTDERHILVSKDGATyqfgIDYMRDVWYSS 931
Cdd:PRK01213 662 rYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDALKVKGNDTES----LEELREAWEGA 717
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
242-525 |
9.64e-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: 148.98 E-value: 9.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 242 ISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGGGKGSWPIAGTAVYMTSYPRTEEGReweeilpvrkwlyqtpeqILIK 321
Cdd:cd02193 3 EAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGIDAKPIALSANWMASAGHPGEDA------------------ILYD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 322 ASNGASDFGNKFGQPLICG----SVLTFEHTENKEVYGYDKVIMLAGGVG-YGTQRDCLKGTPEAGNKVVVIGGDNYRIG 396
Cdd:cd02193 65 AVKGVAELCNQLGLPIPVGkdrmSMKTRWQEGNEQREMTHPPSLVISAFGrVRDDRHTLPQLSTEGNALLLIGGGKGHNG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 397 LGGGSVSSVDTgrysSGIELN--AVQRANAEMQKRANNVVRALCEEevNPVVSIHDHGSAGHVNCLSELVEE--CGGLID 472
Cdd:cd02193 145 LGGTALASVAL----SYRQLGdkSAQVRDPAQEKGFYEAMQALVAA--GKLLAWHDRGAGGLLVALAELVFAghCGVQVD 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2212149261 473 MSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGE 525
Cdd:cd02193 219 LAALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEAQYGLADCVHVLGQ 271
|
|
| PRK01175 |
PRK01175 |
phosphoribosylformylglycinamidine synthase I; Provisional |
984-1216 |
1.30e-38 |
|
phosphoribosylformylglycinamidine synthase I; Provisional
Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 145.29 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 984 IRAAIIREKGTNGEREMAYSLYLAGFDVKDVTMTDLISGRETLEDVNMIVYCGGFSNSDVLGSakgwagGFLFNPKAKEA 1063
Cdd:PRK01175 4 IRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAAERKSVSDYDCLVIPGGFSAGDYIRA------GAIFAARLKAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1064 LDK---FYAREDTLSLGICNGCQLMMELGLIT--PEHKEKGKM--LHNDSHKFESTFVGLTIPTNRSVMFGSLSGSKLGI 1136
Cdd:PRK01175 78 LRKdieEFIDEGYPIIGICNGFQVLVELGLLPgfDEIAEKPEMalTVNESNRFECRPTYLKKENRKCIFTKLLKKDVFQV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1137 WVAHGEGKFSlpYDEDKY--------NVVAKYS-----YDEYPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQng 1203
Cdd:PRK01175 158 PVAHAEGRVV--FSEEEIlerliendQIVFRYVdengnYAGYPWNPNGSIYNIAGITNEKGNVIGLMPHPERAFYGYQ-- 233
|
250
....*....|...
gi 2212149261 1204 cYPADRKNSDQVT 1216
Cdd:PRK01175 234 -HPYWEKEEDYGD 245
|
|
| FGAM_synth_I |
TIGR01737 |
phosphoribosylformylglycinamidine synthase I; In some species, ... |
984-1203 |
9.58e-34 |
|
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: 129.81 E-value: 9.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 984 IRAAIIREKGTNGEREMAYSLYLAGFDVKDVTMTDLIsgretLEDVNMIVYCGGFSNSDVLGSAKGWAggflFNPKAKEA 1063
Cdd:TIGR01737 1 MKVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGS-----LPDYDGVVLPGGFSYGDYLRAGAIAA----ASPIMQEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1064 LDKfyAREDTLSLGICNGCQLMMELGLItpehkeKGKMLHNDSHKFESTFVGLTIPTNRSVMFGSLS-GSKLGIWVAHGE 1142
Cdd:TIGR01737 72 REF--AEKGVPVLGICNGFQILVEAGLL------PGALLPNDSLRFICRWVYLRVENADTIFTKNYKkGEVIRIPIAHGE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1143 GKFSLPYD-----EDKYNVVAKY----SYDEYPGNPNGSDYSIAGLASADGRHLAMMPHLERAIFPWQNG 1203
Cdd:TIGR01737 144 GRYYADDEtlarlESNDQVVFRYcdedGDVAEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGG 213
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
985-1199 |
6.52e-32 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 124.46 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 985 RAAIIREKGTNGEREMAYSL-YLAGFDVKDVTMTDlisgrETLEDVNMIVYCGGFSNSDVL--GS-AKgwaggflFNPkA 1060
Cdd:PRK03619 2 KVAVIVFPGSNCDRDMARALrDLLGAEPEYVWHKE-----TDLDGVDAVVLPGGFSYGDYLrcGAiAA-------FSP-I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1061 KEALDKFyAREDTLSLGICNGCQLMMELGLItpehkeKGKMLHNDSHKFESTFVGLTIPTNRSvMFGSL--SGSKLGIWV 1138
Cdd:PRK03619 69 MKAVKEF-AEKGKPVLGICNGFQILTEAGLL------PGALTRNASLKFICRDVHLRVENNDT-PFTSGyeKGEVIRIPI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2212149261 1139 AHGEGKF-----SLPYDEDKYNVVAKYSYDeypgNPNGSDYSIAGLASADGRHLAMMPHLERAIFP 1199
Cdd:PRK03619 141 AHGEGNYyadeeTLKRLEGNGQVVFRYCDE----NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEP 202
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
637-888 |
4.81e-25 |
|
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: 106.23 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 637 GIATSIG-HAPQAALaDPAAGSILSVSEALTNLvwAPMAEGMDSISLSANWMwPCRSQEGEDARLYTAVKALSDFCCALQ 715
Cdd:cd02193 2 GEAMKIEeHNHPAAI-DPAAGAATGVGGAIRDI--AATGIDAKPIALSANWM-ASAGHPGEDAILYDAVKGVAELCNQLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 716 INVPTGKDSLSM-TQKYPNGE--KVISPGTVIVSAGGEVSDVKKVVSPVLVNNEKTTLyhIDFSFDELKLGGSAFAQ--- 789
Cdd:cd02193 78 LPIPVGKDRMSMkTRWQEGNEqrEMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLL--IGGGKGHNGLGGTALASval 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 790 SLGKVGDEVPCVQDAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCFSNVEGGL----EISLDKMKEEDIVKI 865
Cdd:cd02193 156 SYRQLGDKSAQVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQvdlaALGDDEPDMEPLEIA 235
|
250 260
....*....|....*....|...
gi 2212149261 866 LFAENPGIVIQISDKHKDEVKKI 888
Cdd:cd02193 236 LFESQERGVIQVRAEDRDAVEEA 258
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
380-535 |
3.19e-23 |
|
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: 97.03 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 380 EAGNKVVVIGGDnyriGLGGGSVSSVDTGRYSSGieLNAVQRANAEMQKRANNVVRALCEEEvNPVVSIHDHGSAGHVNC 459
Cdd:pfam02769 1 KPGDVLILLGSS----GLHGAGLSLSRKGLEDSG--LAAVQLGDPLLEPTLIYVKLLLAALG-GLVKAMHDITGGGLAGA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212149261 460 LSELVE--ECGGLIDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRFAFQ 535
Cdd:pfam02769 74 LAEMAPasGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVI 151
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
122-171 |
3.60e-21 |
|
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: 87.52 E-value: 3.60e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2212149261 122 LEVYNEKEGLALSKEEMDYLKKVEKDLGRKLTDSEVFGFAQINSEHCRHK 171
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYFAGLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
138-760 |
3.45e-20 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 96.46 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 138 MDYLKKVEKDLGRKLTDSEVFGFAQINSEHCrhkifggtfiidGVEQESSLFQMIKKTTQENPNKIISAykdnvafaegp 217
Cdd:PRK14090 1 MRYLNILEEKLGREPTFVELQAFSVMWSEHC------------GYSHTKKYIRRLPKTGFEGNAGVVNL----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 218 vveqfapadhskpdffqvkDIKSVISLKAETHNFPTTVEPFNGASTGTGGEIRDRMGggKGSWPiagTAVYMTSYPrtee 297
Cdd:PRK14090 58 -------------------DDYYSIAFKIESHNHPSAIEPYNGAATGVGGIIRDVLA--MGARP---TAIFDSLHM---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 298 greweeilpvrkwlyqtpEQILIKASNGASDFGNKFGQPLICGSVLTfehtenKEVYGYDKVI-MLAGGVGYGTQRDCLK 376
Cdd:PRK14090 110 ------------------SRIIDGIIEGIADYGNSIGVPTVGGELRI------SSLYAHNPLVnVLAAGVVRNDMLVDSK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 377 GTpEAGNKVVVIGGDNYRIGLGGGSVSSVD-TGRYSSGIelnAVQRANAEMQKRANNVVRALCEEEVnpVVSIHDHGSAG 455
Cdd:PRK14090 166 AS-RPGQVIVIFGGATGRDGIHGASFASEDlTGEKATKL---SIQVGDPFAEKMLIEAFLEMVEEGL--VEGAQDLGAGG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 456 HVNCLSELVEE--CGGLIDMSKLPIGDKTLSAKEIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGETTGDHRFA 533
Cdd:PRK14090 240 VLSATSELVAKggLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVAEVIDDPIYR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 534 FQQADgvrpfDLAVE---QMFGSSPKTYMVDKTVErhyEMPKYelsklheyltnvlqleavackDWLT-NKVDRSVTGKV 609
Cdd:PRK14090 320 VMYRD-----DLVMEvpvQLLANAPEEEIVEYTPG---EIPEF---------------------KRVEfEEVNAREVFEQ 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 610 ARQQCQGELQLPlSDCGVVALDYRGEKGIATSIGHAPQAALADPAAGSILSVSEAltnlVWAPMAEGMDSISLS--ANWM 687
Cdd:PRK14090 371 YDHMVGTDTVLP-PGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTFIAVLES----VRKTLSVGAEPLAITncVNYG 445
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2212149261 688 WPcrsqEGEDARLYTAVKALSDFCCALQINVPTGKDSLSMTQKypngeKVISPGTVIVSAGGEVsDVKKVVSP 760
Cdd:PRK14090 446 DP----DVDPVGLSAMMTALKDACEFSGVPVASGNASLYNTYQ-----GKPIPPTLVVGMLGKV-NPQKVAKP 508
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
782-908 |
2.75e-14 |
|
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: 71.61 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 782 LGGSAFAQSLGKVGDE-VPCVQ--DAEYFRDAFLAVQELV-NKGLILAGHDISAGGLITTLLEMCF-SNVegGLEISLDK 856
Cdd:pfam02769 14 LHGAGLSLSRKGLEDSgLAAVQlgDPLLEPTLIYVKLLLAaLGGLVKAMHDITGGGLAGALAEMAPaSGV--GAEIDLDK 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2212149261 857 MK----EEDIVKILFAENPGI-VIQISDKHKDEVKKILEDAGVGYIKLGKPTDERHI 908
Cdd:pfam02769 92 VPifeeLMLPLEMLLSENQGRgLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRL 148
|
|
| FGAR-AT_N |
pfam18076 |
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain ... |
15-79 |
8.77e-11 |
|
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: 60.18 E-value: 8.77e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2212149261 15 VESNHQLTPDESNKLCWLF--GEAVMESEENLKGCFVGPRREMITPWSTNAVEITQNMGLEGISRIE 79
Cdd:pfam18076 6 VELEAPLSAAERARLEQLLtyGPPLEEPEPEGELLLVTPRLGTISPWSSKATDIAHNCGLDAVRRIE 72
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
637-901 |
9.91e-11 |
|
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: 63.18 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 637 GIATSI-GHAPQAALaDPAAGSILSVSEALTNLVwapmAEGMDSISLSANWMWPcrsQEGEDARLYTAVKALSDFCCALQ 715
Cdd:cd00396 1 SLAMSTdGINPPLAI-NPWAGGRLAVGGAVNDIA----AMGARPIALLASLSLS---NGLEVDILEDVVDGVAEACNQLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 716 INVPTGKDSLSMTQKYPNgekvisPGTViVSAGGEVSDvkkvvspvlvnnekttlyhidfsfDELKLGGSAfaqslgKVG 795
Cdd:cd00396 73 VPIVGGHTSVSPGTMGHK------LSLA-VFAIGVVEK------------------------DRVIDSSGA------RPG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 796 DEVpcvqdaeyFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCF-SNVegGLEISLDK-MKEEDIVKI-------- 865
Cdd:cd00396 116 DVL--------ILTGVDAVLELVAAGDVHAMHDITDGGLLGTLPELAQaSGV--GAEIDLEAiPLDEVVRWLcvehieea 185
|
250 260 270
....*....|....*....|....*....|....*..
gi 2212149261 866 -LFAENPGIVIQISDKHKDEVKKILEDAGVGYIKLGK 901
Cdd:cd00396 186 lLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
241-525 |
1.27e-10 |
|
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: 62.80 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 241 VISLKAETHNFPTTVEPFNGASTGTGGEIRD-RMGGGKgswPIAGTAVYMTSYPRTEEGreweeilpvrkwLYQTPEQIl 319
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDiAAMGAR---PIALLASLSLSNGLEVDI------------LEDVVDGV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 320 ikasngaSDFGNKFGQPLICGsvltfeHTENKEVYGYDKVIMLAGGVGYgTQRDCLK--GTPEAGNKVVVIGGDnyrigl 397
Cdd:cd00396 65 -------AEACNQLGVPIVGG------HTSVSPGTMGHKLSLAVFAIGV-VEKDRVIdsSGARPGDVLILTGVD------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 398 gggsvssvdtgryssgielnAVQRANAEmqkrannvvralceeevNPVVSIHDHGSAGHVNCLSELVEE--CGGLIDMSK 475
Cdd:cd00396 125 --------------------AVLELVAA-----------------GDVHAMHDITDGGLLGTLPELAQAsgVGAEIDLEA 167
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2212149261 476 LP--IGDKTLSAK---EIIANESQERMGLLIKEEAIEHVRKIAERERAPMYVVGE 525
Cdd:cd00396 168 IPldEVVRWLCVEhieEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
782-914 |
9.77e-08 |
|
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: 55.17 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 782 LGGSAFA---QSLGKVGDEVPCVQ--DAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMCfSNVEGGLEISLDK 856
Cdd:cd02203 166 IGGATFSskeLSENSSELDRPAVQvgDPFMEKKLQEAILEARETGLIVGIQDLGAGGLSSAVSEMA-AKGGLGAEIDLDK 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212149261 857 --MKEEDIV--KILFAENpgiviQ------ISDKHKDEVKKILEDAGVGYIKLGKPTDERHILVSKDG 914
Cdd:cd02203 245 vpLREPGMSpwEIWISES-----QermllvVPPEDLEEFLAICKKEDLEAAVIGEVTDDGRLRLYYKG 307
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
803-894 |
6.93e-05 |
|
AIR synthase (PurM) related protein, subgroup 3 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: 100028 [Multi-domain] Cd Length: 283 Bit Score: 46.05 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 803 DAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMC-FSNVegGLEISLDK------MKEEDIVKI------LFAE 869
Cdd:cd02192 182 SPALLRRQIALLPELAERGLVHAAKDISNPGIIGTLGMLLeASGV--GAEIDLDAiprpegVDLERWLKCfpgfgfLLTA 259
|
90 100
....*....|....*....|....*
gi 2212149261 870 NPGIViqisdkhkDEVKKILEDAGV 894
Cdd:cd02192 260 RPENA--------DEVVAVFAAVGI 276
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
987-1085 |
1.93e-04 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 42.20 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 987 AIIREKGTNGE--REMAYSLYLAGFDVKDVTMT-DLISGRETLEDVNMIVYCGGFSNSDVLgsakgwaggfLFNPKAKEA 1063
Cdd:cd01653 2 AVLLFPGFEELelASPLDALREAGAEVDVVSPDgGPVESDVDLDDYDGLILPGGPGTPDDL----------ARDEALLAL 71
|
90 100
....*....|....*....|..
gi 2212149261 1064 LDKFYAReDTLSLGICNGCQLM 1085
Cdd:cd01653 72 LREAAAA-GKPILGICLGAQLL 92
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
803-916 |
2.02e-04 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 44.77 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 803 DAEYFRDAFLAVQELVNKGLILAGHDISAGGLITTLLEMC-FSNVegGLEISLDKM---KEEDIVKILFAeNP--GIVIQ 876
Cdd:COG2144 188 PPERLRAQLELLPELAEAGLVTAAKDISNPGIIGTLGMLLeCSGV--GATIDLDAIprpEGVDLERWLKA-FPsfGFLLT 264
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2212149261 877 ISDKHKDEVKKILEDAGVGYIKLGKPTDERHILVSKDGAT 916
Cdd:COG2144 265 VPPENVDEVLARFAARGITAAVIGEVTDSRRLTLRDGGER 304
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| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
1004-1085 |
4.30e-04 |
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Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 40.65 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 1004 LYLAGFDVKDVTMT-DLISGRETLEDVNMIVYCGGFSNSDVLgsakgwaggfLFNPKAKEALDKFYAReDTLSLGICNGC 1082
Cdd:cd03128 21 LREAGAEVDVVSPDgGPVESDVDLDDYDGLILPGGPGTPDDL----------AWDEALLALLREAAAA-GKPVLGICLGA 89
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...
gi 2212149261 1083 QLM 1085
Cdd:cd03128 90 QLL 92
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| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
778-901 |
2.90e-03 |
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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: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212149261 778 DELK-LGGSAFAQSLGKVGDEVPCVQDAEyfrdafLAVQELVNkglilAGHDISAGGLITTLLEMCF-SNVegGLEISLD 855
Cdd:cd06061 175 EELKkRLSEEELREAAKLFYKISVVKEAL------IAAEAGVT-----AMHDATEGGILGALWEVAEaSGV--GLRIEKD 241
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2212149261 856 KMK-EEDIVKI--LFAENP------GIVIQISDKHK-DEVKKILEDAGVGYIKLGK 901
Cdd:cd06061 242 KIPiRQETKEIceALGIDPlrlissGTLLITVPPEKgDELVDALEEAGIPASVIGK 297
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