|
Name |
Accession |
Description |
Interval |
E-value |
| FGAM_synt |
TIGR01735 |
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
2-1276 |
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: 2013.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 2 KKLLWLFGCPLLQDDvareSWLVPGsndlLLEVGPRLNFSTPASTNIVSVCQAAGLRAVDRVETTRRYRLSFAKQPTAEM 81
Cdd:TIGR01735 52 LQLLLLAGSVLEPPQ----SPLGRG----LLEVGPRLGTISPWSSKATSIARNCGLAKVDRIERGRRYYLSGAHPLSEEQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 82 EAISLAALHDRMTEQHYPDPIQSFSPQSIPAPLKDS-INILAEGRPALEKANQELGLALDSWDLDFYTKRFQELQRNPST 160
Cdd:TIGR01735 124 EAQAAALLHDRMTESVLPHEIEAFELFSVPEPLNLTtIDVLGGGRLALEKANQELGLALDEDEIDYLTKRFQELQRNPSD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 161 VEVFDLAQSNSEHSRHWFFKGQLHVDGKKLARSLFESIMSTQSSSNPNNVLKFCDNSSAIQGKEVRFLRPEDSTRPSCFR 240
Cdd:TIGR01735 204 VELMMFAQANSEHCRHKIFNADWIIDGKKQDKSLFQMIKSTHEANPENTVSAYKDNSSVIEGHKVGRLRPDPPTRPEYRQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 241 QQRGLRHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPsFQYPGNFA 320
Cdd:TIGR01735 284 HQEDLVHILMKVETHNHPTAIAPFPGASTGAGGEIRDEGATGRGAKPKAGLTGFCVSNLNIPGLEQPWEDP-FQKPERIA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 321 RPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQ--LPDGQRREWIKPIMFSGGIGSMEAKHVGKEPPEPGMEVVKVGG 398
Cdd:TIGR01735 363 SPLDIMIEAPLGAAAFNNEFGRPNLLGYFRTFELKasLPGGQVRGYHKPIMLAGGIGSIDAEHIQKGEIEPGALLIVLGG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 399 PVYRIGVGGGAASSvQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPGGNPICSLHDQGAGGNGNVLKELSEPA- 477
Cdd:TIGR01735 443 PAMLIGLGGGAASS-MVSGTNTADLDFASVQRGNPEMERRCQEVIDRCWQLGEKNPIISIHDVGAGGLSNALPELIHDGg 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 478 -GAVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDreCLMGKSG 556
Cdd:TIGR01735 522 rGAVIDLRAVPLDDPGLSPLEIWCNESQERYVLLVRAENLEIFTAICERERCPFAVVGTATGDGRLTLVDD--TPVRRNG 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 557 QGDAPPTPP-TPVDLDLDWVLGKMPQKEFFLQRKPPVLQPLALPPDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGLV 635
Cdd:TIGR01735 600 QGDAPSHFPnNPVDLPLEVLLGKMPKMTRFVQRKAPMLQPLDIPPGLDLHEALERVLRLPAVASKRFLITIGDRSVGGLV 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 636 AQQQCVGPLQTPLADVAVVALSHQELVGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWAA 715
Cdd:TIGR01735 680 ARDQMVGPWQTPLADVAVTAASFDTYTGEAMAIGERPPKALLDPKASARLAVGEAITNLAAALVGDLSDVKLSANWMAAA 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 716 KLPGEGAGLADACEAMVTVMAALGVAVDGGKDSLSMAARVG----TETVPAPGSLVISAYAVCPDITATVTPDLKHPGGK 791
Cdd:TIGR01735 760 GHPGEDAALYDAVKAVSELCPALGIAIPVGKDSLSMKTRWQdngeTKSVTAPGSLVISAFAPVPDVRKTVTPDLKHDKGD 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 792 GHLLYVPLSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNC 871
Cdd:TIGR01735 840 SHLLLVDLGPGKNRLGGSALAQVFGQLGGDCPDLDDPERLKAFFAVMQGLVAEGLLLAYHDRSDGGLVTTLLEMAFAGHC 919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 872 GIEVDVPAPGIHALPVLFAEEPGLVLEVQEADVAGVLQRYQSAGLHCLELGHTGEAGpQAMVRVSVNGTVVVEEPVGQLR 951
Cdd:TIGR01735 920 GLDVDLDALGDSLFAVLFNEELGAVIQVAKPDLAAVLELLRAAGLTALILGIGTPTG-HPMIRISVNGATLLSEKRSELR 998
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 952 ALWEETSFQLDLLQAEPRCVTEEKQGLKERIGPSYCLPPTFPVASVPCKPG---GPIPRVAILREEGSNGDREMADAFHL 1028
Cdd:TIGR01735 999 DIWEETSFQLQRLRDNPECAEEEFEGLRDRDGPGLKLPLTFDVNEDIAAPFinkGVKPKVAILREQGVNGDREMAAAFDR 1078
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1029 AGFEVWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCNGCQLLA 1108
Cdd:TIGR01735 1079 AGFEAWDVHMSDLLAGRVHLDEFRGLAACGGFSYGDVLGAGKGWAKSILFNPRLRDQFQAFFKRPDTFSLGVCNGCQMLS 1158
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1109 -LLGWVGSDPNEDQvepdhdsqpaqpglLLRHNlSGRFESRWATVRVEPGPALMLRGMEGSVLPVWSAHGEGYMAFSSPE 1187
Cdd:TIGR01735 1159 nLLEWIPGTENWPH--------------FVRNN-SERFEARVASVRVGESPSIMLRGMAGSRLPVAVAHGEGYAAFSSPE 1223
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1188 LQAKIKAKGLVPLHWADDDGNPTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPERAVRLWQWAWRPSPFDglSTSPWLQ 1267
Cdd:TIGR01735 1224 LQAQADASGLAALRYIDDDGNPTEAYPLNPNGSPGGIAGITSCDGRVTIMMPHPERVFRAWQNSWRPEDWD--EDTPWLR 1301
|
....*....
gi 564372564 1268 LFINARNWT 1276
Cdd:TIGR01735 1302 LFRNARNWL 1310
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
1-1275 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 1770.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1 MKKLLWLFG---CP-LLQDDVARESWLVPGSNDLLLEVGPRLNFSTPASTNIVSVCQAAGLRAVDRVETTRRYRLSFAKQ 76
Cdd:PLN03206 37 LETLKWLLRetfEPeNLGTESFLEAKKSEGLNAVVVEVGPRLSFTTAWSTNAVSICSACGLTEVTRLERSRRYLLFSSSP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 77 PTAEMEAISLAALHDRMTEQHYPDPIQSFSPQSIPAPLKdSINILAEGRPALEKANQELGLALDSWDLDFYTKRFQE-LQ 155
Cdd:PLN03206 117 LDESQINAFAAMVHDRMTECVYPQPLTSFESGVVPEPVY-TVPVMEEGRAALEEINKEMGLAFDEQDLDYYTRLFRDdIK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 156 RNPSTVEVFDLAQSNSEHSRHWFFKGQLHVDGKKLARSLFESIMSTQsSSNPNN-VLKFCDNSSAIQGKEVRFLRPEDST 234
Cdd:PLN03206 196 RDPTNVELFDIAQSNSEHSRHWFFSGKLVIDGQPMPKTLFQMVKDTL-KANPNNsVIGFKDNSSAIRGFVVQPLRPVSPG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 235 RPSCFRQQRGLRHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPSFQ 314
Cdd:PLN03206 275 SPSPLAPVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVAGTAGYCVGNLRIEGSYAPWEDSSFV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 315 YPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEAKHVGKEPPEPGMEVV 394
Cdd:PLN03206 355 YPSNLASPLQILIDASNGASDYGNKFGEPLIQGYTRTFGMRLPNGERREWLKPIMFSGGIGQIDHTHLTKGEPDIGMLVV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 395 KVGGPVYRIGVGGGAASSVqVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPGGNPICSLHDQGAGGNGNVLKELS 474
Cdd:PLN03206 435 KIGGPAYRIGMGGGAASSM-VSGQNDAELDFNAVQRGDAEMSQKLYRVVRACVEMGEDNPIVSIHDQGAGGNCNVVKEII 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 475 EPAGAVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDRECLMGK 554
Cdd:PLN03206 514 YPKGAEIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPESRDLLQSICDRERCSMAVIGTIDGSGRVVLVDSAAPEKCE 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 555 SgqgDAPPTPPTPVDLDLDWVLGKMPQKEFFLQRKPPVLQPLALPPDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGL 634
Cdd:PLN03206 594 A---NGLPPPPPAVDLDLEKVLGDMPQKTFEFKRVANKLEPLDIPPGITVMDALKRVLRLPSVCSKRFLTTKVDRCVTGL 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 635 VAQQQCVGPLQTPLADVAVVALSHQELVGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWA 714
Cdd:PLN03206 671 VAQQQTVGPLQIPLADVAVIAQTHTGLTGGACAIGEQPIKGLVDPKAMARLAVGEALTNLVWAKVTALSDVKASGNWMYA 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 715 AKLPGEGAGLADACEAMVTVMAALGVAVDGGKDSLSMAARVGTETVPAPGSLVISAYAVCPDITATVTPDLKHpGGKGHL 794
Cdd:PLN03206 751 AKLDGEGADMYDAAVALRDAMIELGVAIDGGKDSLSMAAQAGGEVVKAPGNLVISAYVTCPDITKTVTPDLKL-GDDGVL 829
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 795 LYVPLSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIE 874
Cdd:PLN03206 830 LHVDLGKGKRRLGGSALAQAYDQIGDDCPDLDDVAYLKKAFEATQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNCGIN 909
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 875 VDVPAPGIHALPVLFAEEPGLVLEVQEADVAGVLQRYQSAGLHCLELGHTgEAGPqaMVRVSVNGTVVVEEPVGQLRALW 954
Cdd:PLN03206 910 VDLPSSGHSAFETLFAEELGLVLEVSRKNLDAVMEKLAAAGVTAEVIGQV-TASP--LIEVKVDGATCLSEKTASLRDMW 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 955 EETSFQLDLLQAEPRCVTEEKQGLKERIGPSYCLP--PTFPVASVPCKPGGpiPRVAILREEGSNGDREMADAFHLAGFE 1032
Cdd:PLN03206 987 EETSFQLEKLQRLESCVAQEKEGLKSRKAPTWKLSftPAFTDKKIMNATSK--PKVAIIREEGSNGDREMAAAFYAAGFE 1064
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1033 VWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCNGCQLLALLGW 1112
Cdd:PLN03206 1065 PWDVTMSDLLNGRISLDDFRGIVFVGGFSYADVLDSAKGWAGSIRFNEPLLQQFQEFYNRPDTFSLGVCNGCQLMALLGW 1144
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1113 VGSDPNEDQVEPDHDsqPAQPGLLlrHNLSGRFESRWATVRVEPGPALMLRGMEGSVLPVWSAHGEGYMAFSSPELQAKI 1192
Cdd:PLN03206 1145 VPGPQVGGGLGAGGD--PSQPRFV--HNESGRFECRFTSVTIEDSPAIMLKGMEGSTLGVWAAHGEGRAYFPDESVLDEV 1220
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1193 KAKGLVPLHWADDDGNPTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPERAVRLWQWAWRPSPF--DGLSTSPWLQLFI 1270
Cdd:PLN03206 1221 LKSNLAPVRYCDDDGEPTEQYPFNPNGSPLGIAALCSPDGRHLAMMPHPERCFLMWQFPWYPKEWgvDPAGPSPWLKMFQ 1300
|
....*
gi 564372564 1271 NARNW 1275
Cdd:PLN03206 1301 NAREW 1305
|
|
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
11-1275 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 1473.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 11 PLLQDDVARESWL------VPGSNDLLLEVGPRLNFSTPASTNIVSVCQAAGLRAVDRVETTRRYRLSFAKqpTAEMEAI 84
Cdd:PRK05297 45 PLSAEEQAKLERLltygpaEHEPAGRLFLVTPRPGTISPWSSKATDIAHNCGLAGIRRIERGIAYYVEAAL--SAEQRAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 85 SLAALHDRMTEQHYPDPIQS---FSPQSiPAPLKdSINILAEGRPALEKANQELGLALDSWDLDFYTKRFQELQRNPSTV 161
Cdd:PRK05297 123 LAALLHDRMTESVFADLDDAealFSHHE-PKPLT-SVDVLGGGRAALEAANVELGLALAEDEIDYLVEAFTKLGRNPTDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 162 EVFDLAQSNSEHSRHWFFKGQLHVDGKKLARSLFESIMSTqSSSNPNNVLK-FCDNSSAIQGKEVRFLRPEDSTRPSCFR 240
Cdd:PRK05297 201 ELMMFAQANSEHCRHKIFNADWTIDGEEQPKSLFKMIKNT-HETNPDGVLSaYKDNAAVMEGSKVGRFFPDPDTGRYGYH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 241 QQrgLRHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPsFQYPGNFA 320
Cdd:PRK05297 280 QE--PAHILMKVETHNHPTAISPFPGAATGSGGEIRDEGATGRGSKPKAGLTGFSVSNLRIPGFEQPWEED-YGKPERIA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 321 RPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDG--QRREWIKPIMFSGGIGSMEAKHVGKEPPEPGMEVVKVGG 398
Cdd:PRK05297 357 SALDIMIEGPLGGAAFNNEFGRPNLLGYFRTFEQKVNSHneEVRGYHKPIMLAGGIGNIRADHVQKGEIPVGAKLIVLGG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 399 PVYRIGVGGGAASSVqVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPGGNPICSLHDQGAGGNGNVLKELSEPA- 477
Cdd:PRK05297 437 PAMRIGLGGGAASSM-ASGQSSEDLDFASVQRGNPEMERRCQEVIDRCWQLGDDNPILSIHDVGAGGLSNAFPELVNDGg 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 478 -GAVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDReclmgksg 556
Cdd:PRK05297 516 rGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEAICERERCPFAVVGEATEERHLTLEDSH-------- 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 557 qgdappTPPTPVDLDLDWVLGKMPQKEFFLQRKPPVLQPLALPpDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGLVA 636
Cdd:PRK05297 588 ------FDNKPVDLPLDVLLGKPPKMHRDVKTVKAKGPALDYS-GIDLAEAVERVLRLPTVASKSFLITIGDRSVTGLVA 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 637 QQQCVGPLQTPLADVAVVALSHQELVGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWAAK 716
Cdd:PRK05297 661 RDQMVGPWQVPVADCAVTAASYDGYAGEAMAMGERTPVALLDAAASARMAVGEALTNIAAAPIGDLKRIKLSANWMAAAG 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 717 LPGEGAGLADACEAM-VTVMAALGVAVDGGKDSLSMAARV----GTETVPAPGSLVISAYAVCPDITATVTPDLKHPGGk 791
Cdd:PRK05297 741 HPGEDARLYDAVKAVgMELCPALGITIPVGKDSLSMKTKWqeggEDKEVTSPLSLIISAFAPVEDVRKTLTPQLRTDKD- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 792 GHLLYVPLSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNC 871
Cdd:PRK05297 820 TALLLIDLGRGKNRLGGSALAQVYNQLGDKAPDVDDAEDLKGFFNAIQALVAEGLLLAYHDRSDGGLLTTLAEMAFAGHC 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 872 GIEVDVPAPGIHALPVLFAEEPGLVLEVQEADVAGVLQRYQSAGL--HCLELGHTGEAGpqaMVRVSVNGTVVVEEPVGQ 949
Cdd:PRK05297 900 GLDIDLDALGDDALAALFNEELGAVIQVRAADRDAVEAILAEHGLsdCVHVIGKPNAGD---RIVITRNGKTVFSESRTE 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 950 LRALWEETSFQLDLLQAEPRCVTEEKQGLKERIGPSYCLPPTFPVA---SVPCKPGGPIPRVAILREEGSNGDREMADAF 1026
Cdd:PRK05297 977 LRRWWSETSYQMQRLRDNPECADQEFDAILDQADPGLNVKLTFDPNediAAPFIATGARPKVAILREQGVNSHVEMAAAF 1056
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1027 HLAGFEVWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCNGCQL 1106
Cdd:PRK05297 1057 DRAGFDAIDVHMSDLLAGRVTLEDFKGLVACGGFSYGDVLGAGEGWAKSILFNPRLRDQFEAFFARPDTFALGVCNGCQM 1136
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1107 LALLGwvgsdpnedQVEPDHDSQPAqpgllLRHNLSGRFESRWATVRVEPGPALMLRGMEGSVLPVWSAHGEGYMAFSSP 1186
Cdd:PRK05297 1137 MSNLK---------EIIPGAEHWPR-----FVRNRSEQFEARFSLVEVQESPSIFLQGMAGSRLPIAVAHGEGRAEFPDA 1202
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1187 ELQAkIKAKGLVPLHWADDDGNPTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPERAVRLWQWAWRPSPFDGLstSPWL 1266
Cdd:PRK05297 1203 HLAA-LEAKGLVALRYVDNHGQVTETYPANPNGSPNGITGLTTADGRVTIMMPHPERVFRTVQNSWHPEEWGED--SPWM 1279
|
....*....
gi 564372564 1267 QLFINARNW 1275
Cdd:PRK05297 1280 RMFRNARKW 1288
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
121-957 |
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: 679.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 121 LAEGRPALEKANQELGLALDSWDLDFYTKRfqeLQRNPSTVEVFDLAQSNSEHSRHWFFKGQLhvdgkklaRSLfesims 200
Cdd:COG0046 6 LEGGREALEEANRELGLALSDDEYDYIVEI---LGRNPTDVELGMFSQMWSEHCSYKSSNALL--------KSL------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 201 tqSSSNPNNVLKFCDNSSAIQGKEvrflrpedstrpscfrqqrGLrHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQc 280
Cdd:COG0046 69 --PTEGPRVLSGPGDNAGVVDIGD-------------------GL-AVVFKVESHNHPSAIEPYQGAATGVGGIIRDIF- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 281 tGRGAHVVAGTAGYCFGNLHIPGynlpwedpsfqypgnfARPLEVAIEASNGASDYGNKFGEPVLAGFARSlglqlpDGQ 360
Cdd:COG0046 126 -GMGARPIAGLDSLRFGNLDQPP----------------ASPRYILIGVVAGIADYGNCFGVPTVGGEVRF------DES 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 361 RREwiKPIMFSGGIGSMEAKHVGK-EPPEPGMEVVKVGGPVYRIGVGGGAASSVqVQGDNtSDLDFGAVQRGDPEMEQKM 439
Cdd:COG0046 183 YEG--NPLVNAGGVGIIRADHIFKaKAPGVGNKVVYVGGPTGRDGIGGATFASE-ELGED-SELDRPAVQVGDPFMEKRL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 440 NRVIRACVEApggNPICSLHDQGAGGNGNVLKELSEPA--GAVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRD 517
Cdd:COG0046 259 IEAILELGDT---GLIVGIQDMGAGGLSSASSEMAAKGglGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 518 FLSRASARERCPACFVGTITGDKRIVLVDDREclmgksgqgdapptppTPVDLDLDWVLGKMPQKEFFLQRkPPVLQPLA 597
Cdd:COG0046 336 EFEAIFERWRLPAAVIGEVTDDGRLVVTDHGE----------------TVADLPLDFLAGGAPKYHRPAKR-PAYLEPLD 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 598 LPPDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQcvgplqtPLADVAVVALSHQELvGAATALGEQPVKSLL 677
Cdd:COG0046 399 LPEPIDLEEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDP-------GVADAAVVRVDGTYK-GLAMSTGENPRYALL 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 678 DPKAAARLAVSEALTNLVFALVTDLrDVKCSGNWMWAAKlPGEGAGLADACEAMVTVMAALGVAVDGGKDSLSMAARVGt 757
Cdd:COG0046 471 DPYAGARMAVAEAARNLAAVGAEPL-AITDCLNWGNPEK-PEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKDG- 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 758 eTVPAPGSLVISAYAVCPDITATVTPDLKHPggkGHLLYVpLSPGQHRLGGTALAQCFSQLGEHPPDLDlPENLVRAFHI 837
Cdd:COG0046 548 -KVAIPPTPVIGAVGLVDDVRKTVTPDLKKE---GDLLYL-IGETKNELGGSEYAQVLGQLGGEPPDVD-LEAEKALFEA 621
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 838 TQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPA-PGIHALPVLFAEEPG-LVLEVQEADVAGVLQRYQSAG 915
Cdd:COG0046 622 VQELIREGLILAAHDVSDGGLAVALAEMAFAGGLGADIDLDAlGDLRPDAALFSESQGrAVVQVAPEDAEAVEALLAEAG 701
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 564372564 916 LHCLELGHTGEAGpqaMVRVSVNGTVVVEEPVGQLRALWEET 957
Cdd:COG0046 702 LPAHVIGTVTGDD---RLVIRRGGETLLSLSLAELRDAWEET 740
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
470-1276 |
1.89e-142 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 466.42 E-value: 1.89e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 470 LKELSEPAGAVIYTSRfqLGDPTLNALEIWGAEYQESN--------------ALLLRPSDR----------DFLSRASAR 525
Cdd:PHA03366 439 LLALCPPGGLLLFLSA--LPEDVVSGLKPFSASNRETNeeivkqyflnvycsVVFLVIKNTheggegvtplDALKRACRL 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 526 ERCPACFVGTITGDKRIVLVDDReclmgksgqgdAPPTPPTPVDLD------LDWVLGKMPQKEFFlQRKPPVLQPLALP 599
Cdd:PHA03366 517 AGCPVHILGRTVPLPGIHFVNDL-----------GNPVYGELRDDQfkptfpLQPSRPLSPVSATS-EDTRPSPQDESID 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 600 -PDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALS--------------------- 657
Cdd:PHA03366 585 wALFNLNSTLLQILSHPTVGSKEYIVRHIDRCGNGRVAQQPGVGPLDLPVSDYSIVVHSsvktrraietpsstedltyqe 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 658 HQELV--------------------GAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWaakl 717
Cdd:PHA03366 665 ADELInspltwfdpddesvlhpavpGTCSALGEQGYKVQLDPILGAKYAIVEALTNLMLAPVANLEDITITLSVTW---- 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 718 pgeGAGLADACEAMVTVMAA------LGVAVdggkdSLSMAA---RVGTETVPAPG--SLVISAYAVCPDITATVTPDLK 786
Cdd:PHA03366 741 ---PPTDQAASELYRALAACkefcreLGVNF-----TFTSASsspRQDQPPQPGPLfnTIVFTASAPVPSSTPRLTPDLK 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 787 HPGGkgHLLYVPLSPGQHrLGGTALAQCFSQLGEHPPDLDlPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMA 866
Cdd:PHA03366 813 KPGS--ALVHLSISPEYT-LAGSVFEQIFGLKSGTLPDIS-PSYLKNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 867 FAGNCGIEVDVPApGIHALPVLFAEEPGLVLEVQEADVAGVLQRYQSAGLHCLELGHTGEAGPQAMVRVSVNGTVVVEEP 946
Cdd:PHA03366 889 LAGGRGVTITVPA-GEDPLQFLFSETPGVVIEVPPSHLSAVLTRLRSRNIICYPIGTVGPSGPSNTFSVSHNGTVLFRES 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 947 VGQLRALWeeTSFQLDLLQAEPRCVTEEKQGLKERIGPSYCLPP------TFPVASV--PCKPggpiPRVAILREEGSNG 1018
Cdd:PHA03366 968 LSSLRSTW--RSFSDEQFELLRPDLTEESMYRKDYGNNEVDLGPleegltTSPLRLYtcPDKR----HRVAVLLLPGCPG 1041
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1019 DREMADAFHLAGFEVWDVTMQDLCSGAVrLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSL 1098
Cdd:PHA03366 1042 PHALLAAFTNAGFDPYPVSIEELKDGTF-LDEFSGLVIGGSSGAEDSYTGARAAVAALLSNPAVRDALLRFLNRPDTFSL 1120
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1099 GVCN-GCQLLALLGWVGSdpNEDQVEPDHDSQPAQPGLLLRhNLSGRFESRWATVRV-EPGPALMLRGMEGSVLPVWsAH 1176
Cdd:PHA03366 1121 GCGElGCQILFALKAVGS--TAPSPVPGTETEEQWPITLEP-NASGLYESRWLNFYIpETTKSVALRPLRGSVLPCW-AQ 1196
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1177 GEgYMAFS--SPELQAKIKAKGLVPLHWAD---DDGNPTEQYPLNPNGSpGGIAGICSPDGRHLALMPHPERAVRLWQWA 1251
Cdd:PHA03366 1197 GT-HLGFRypNDGMEYILRNSGQIAATFHGadvDPGNPARHYPRNPTGN-SNVAGLCSADGRHLALLFDPSLSFHPWQWQ 1274
|
890 900
....*....|....*....|....*
gi 564372564 1252 WRPSPFDGLSTSPWLQLFINARNWT 1276
Cdd:PHA03366 1275 HVPPENGPLKVSPWKLMFQDLHLWC 1299
|
|
| GATase_5 |
pfam13507 |
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
1006-1275 |
4.70e-141 |
|
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: 428.84 E-value: 4.70e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1006 PRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREE 1085
Cdd:pfam13507 2 PRVAILREPGTNGEYEMAAAFERAGFDAVDVHMSDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1086 LGRFRRRPDTFSLGVCNGCQLLALLGWVGSDPNEDQvepdhDSQPAqpgllLRHNLSGRFESRWATVRV-EPGPALMLRG 1164
Cdd:pfam13507 82 FEAFFNRPDTFSLGICNGCQLLSKLGLIPGGEGDLA-----ERWPT-----LTRNDSGRFESRWVNVKIsEKSPSVFLRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1165 MEGSVLPVwsAHGEGYMAFSSPELQAKIKAKGLVPLHWADDDGNPTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPERA 1244
Cdd:pfam13507 152 MDGSGLPV--AHGEGRFVFRSEEVLARLEANGQVALRYVDNAGNPTEEYPFNPNGSPLGIAGICSPDGRVLGLMPHPERV 229
|
250 260 270
....*....|....*....|....*....|.
gi 564372564 1245 VRLWQWAWRPsPFDGLSTSPWLQLFINARNW 1275
Cdd:pfam13507 230 FRPWQWPHWP-PGEWEEVSPWLRLFRNARKW 259
|
|
| tegu_FGAM_synt |
TIGR01739 |
herpesvirus tegument protein/v-FGAM-synthase; This model describes a family of large proteins ... |
341-1276 |
3.59e-125 |
|
herpesvirus tegument protein/v-FGAM-synthase; This model describes a family of large proteins of herpesvirues. The protein is described variably as tegument protein or phosphoribosylformylglycinamidine synthase (FGAM-synthase). Most of the length of the protein shows homology to eukaryotic FGAM-synthase. Functional characterizations were not verified during construction of this model.
Pssm-ID: 273784 [Multi-domain] Cd Length: 1202 Bit Score: 416.79 E-value: 3.59e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 341 GEPVLAGFAR---SLGLQLPDGQRrewikPIMFSGGIGSMEAKHVGKEPPEPGMEVVKVG--GPVYRigvgggaaSSVQV 415
Cdd:TIGR01739 237 GVPTCGGFIRlisKNKLSLPTPYT-----PTYNTSILDRLCHVTINTADEPPGQDIVALGqfEPSLL--------PDTPP 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 416 QGDNTSDLDFGAVQrgdpemeQKMNRVIRacvEAPGGNPICSLHDQGAGGNGNVLKELSEPAGAVIYTSrfQLGDPTLNA 495
Cdd:TIGR01739 304 LLYADSPLDVNKIL-------TALALLTD---DVKTPCIVGSIRPLGPCSVKEHLTALLPPCGAELDLS--NLPDEVVAA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 496 LEIWGAEYQESNALLLR----------------------------PSDRdfLSRASARERCPACFVGTITGDKRIVLVDD 547
Cdd:TIGR01739 372 LARSSPANRVENEKMVKqyflnvvcsvvfltvkntphntgtegvtPLER--LKTACRMFGCPVKVLGKLVPLPGLHIVSD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 548 reclmgksgQGDAPPTPPTpvdldLDWVLGKMPQKEFFLQRKPPV--LQPLALPP-----DLSVGQALERVLRLPAVASK 620
Cdd:TIGR01739 450 ---------LFNPVPTYPT-----FDFTSFTPTSPLLPLGGPEPVsrTRPMFLDEslnwqTLNLRSTILKILSHPTVGSK 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 621 RYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALS-----------HQELV-------------------------GA 664
Cdd:TIGR01739 516 EFIVRHIDRCGNGRVAQQQGVGPLDLPVSDYSLVLHNlsrptdttevtYSENAmdlildpdswlyswenevlenpalsCV 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 665 ATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAgLADACEAMVTVMAALGVAVdg 744
Cdd:TIGR01739 596 CSALGEQTYKVQADPKRGATYAITEALLNLSLSPWNTLEDVIITLSVTWSPTDHVYSL-LKDALRACKDFCEELGVSF-- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 745 gkdSLSMAARVGTETVPAPG--SLVISAYAVCPDITATVTPDLKHPGGkgHLLYVPLSPgQHRLGGTALAQCFSQLGEHP 822
Cdd:TIGR01739 673 ---TVTSAASSPTQDSGSAPfmSIVFSASCPVLLSAKKITPDLKSHGS--HLIWLSLHP-SYTLAGSIFEQILGLSFIRL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 823 PDLDlPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPApGIHALPVLFAEEPGLVLEVQEA 902
Cdd:TIGR01739 747 PALS-PVSLKKLLSALQTLVKEGVIVSGHDVSDGGLVACVAEMALSGGKGVRITLPH-GTDPLEFLCSETPGVVIEVDPS 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 903 DVAGVLQRYQSAGLHCLELGHTGEAGPQAMVRVSVNGTVVVEEPVGQLRALWEETSFQLDLLQA---EPRCVTEEKQGLK 979
Cdd:TIGR01739 825 SMYAVLQFLRSEGLVFQVIGRVGESGPSPTFSVVHNSTVLFQEPLSLLQGTWRSFSDEENTLLCpnlEPREMHVLDYGYN 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 980 E---RIGPSYClpPTFPVASVPCKPggPIPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAVrLDTFRGVAF 1056
Cdd:TIGR01739 905 EmdfGGVPKGL--PLSPLRFFTCPD--PRHQVAVLLLPGQSVPHGLLAALTNAGFDPRIVSITELKKTDF-LDTFSGLII 979
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1057 VGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCN-GCQLLALLGWVGSDPNEDQVepdHDSQPAQPGL 1135
Cdd:TIGR01739 980 GGASGTLDSEVGARALAAALLRNQAFLRDLLTFLNRPDTFSLGFGElGCQLLLALNIVGYTQSSPFI---TVPTEVQEPP 1056
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1136 LLRHNLSGRFESRWATVRV-EPGPALMLRGMEGSVLPVWsAHGEgYMAF--SSPELQAKIKAKGLVPLHWAD---DDGNP 1209
Cdd:TIGR01739 1057 RLEKNASGLYESRWLNFYIpETTKSVFLRPLRGSVLPCW-AQGT-HLGLyhPDDGVEEELENSGQIASTFHGnspSSGLP 1134
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372564 1210 TEQYPLNPNGSpGGIAGICSPDGRHLALMPHPERAVRLWQWAWRPSPFDGLSTSPWLQLFINARNWT 1276
Cdd:TIGR01739 1135 ATNYPRNPSGG-SNVAGLCSADGRHLALLIDPSLSFFPWQWQHVPPNNPPLQVSPWKLMFQRLHLWS 1200
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
162-552 |
7.93e-125 |
|
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: 387.98 E-value: 7.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 162 EVFDLAQSNSEHSRHWFFKGQLhvdgkklarslfesimstqsssnpnnvlkfcdnssaiqgkevrflrpedstrpscfrq 241
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLL---------------------------------------------------------- 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 242 qRGLRHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGrgAHVVAGTAGYCFGNLHIPGYnlpwedpsfqYPGNFAR 321
Cdd:cd02203 23 -KMIWAVVFKVETHNHPSAIEPFGGAATGVGGIIRDILSMG--ARPIALLDGLRFGDLDIPGY----------EPKGKLS 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 322 PLEVAIEASNGASDYGNKFGEPVLAGFARSlglqlpDGQRreWIKPIMFSGGIGSMEAKHVGK-EPPEPGMEVVKVGGPV 400
Cdd:cd02203 90 PRRILDGVVAGISDYGNCIGIPTVGGEVRF------DPSY--YGNPLVNVGCVGIVPKDHIVKsKAPGPGDLVVLVGGRT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 401 YRIGVGGGAASSVQVqGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEApggNPICSLHDQGAGGNGNVLKELSE--PAG 478
Cdd:cd02203 162 GRDGIGGATFSSKEL-SENSSELDRPAVQVGDPFMEKKLQEAILEARET---GLIVGIQDLGAGGLSSAVSEMAAkgGLG 237
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372564 479 AVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDRECLM 552
Cdd:cd02203 238 AEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTDDGRLRLYYKGEVVA 311
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
1008-1273 |
6.46e-100 |
|
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: 317.63 E-value: 6.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1008 VAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAvtfnPQAREELG 1087
Cdd:cd01740 1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFSYGDYLRAGAIAAAS----PLLMEEVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1088 RFRRRpDTFSLGVCNGCQLLALLGWVgsdpnedqvepdhdsqpaqPGLLLRhNLSGRF----ESRWATVRVEPGPALMLR 1163
Cdd:cd01740 77 EFAER-GGLVLGICNGFQILVELGLL-------------------PGALIR-NKGLKFicrwQNRFVTLRVENNDSPFTK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1164 G-MEGSVLPVWSAHGEGYMAFSSPELQAKIKAKGLVplHWADDDGNPTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPE 1242
Cdd:cd01740 136 GyMEGEVLRIPVAHGEGRFYADDETLAELEENGQIA--QYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPE 213
|
250 260 270
....*....|....*....|....*....|.
gi 564372564 1243 RAVRLWQWAWRpspfdgLSTSPWLQLFINAR 1273
Cdd:cd01740 214 RAVEPWQWERL------LGGSDGLKLFRNAV 238
|
|
| PurL2 |
COG0047 |
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1006-1275 |
1.64e-84 |
|
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: 275.40 E-value: 1.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1006 PRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLcsgAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAvtfnpQAREE 1085
Cdd:COG0047 1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDL---RTDLDDFDGLVLPGGFSYGDYLRAGAIAAFS-----PIMDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1086 LGRFRRRpDTFSLGVCNGCQLLALLGWVgsdpnedqvepdhdsqpaqPGLL--LRHNLSGRFESRWATVRVEPGPALMLR 1163
Cdd:COG0047 73 VREFARR-GGLVLGICNGFQILTELGLL-------------------PGIWpaLTRNRSLRFICRWVYLRVENNDSPFTS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1164 GME-GSVLPVWSAHGEGYmAFSSPELQAKIKAKGLVPLHWADDDGNPTeqYPLNPNGSPGGIAGICSPDGRHLALMPHPE 1242
Cdd:COG0047 133 GMEaGEVIPIPIAHGEGR-YVADEETLAELEANGQVAFRYVDADGNVT--YPANPNGSLNNIAGITNEDGNVLGMMPHPE 209
|
250 260 270
....*....|....*....|....*....|...
gi 564372564 1243 RAVRLWQwawrpSPFDGlstSPWLQLFINARNW 1275
Cdd:COG0047 210 RAVEPLL-----GPGES---TDGLRIFRSAVKY 234
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
650-924 |
8.76e-81 |
|
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: 265.94 E-value: 8.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 650 DVAVVALSHQELVGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLrDVKCSGNWMWAAKLPGEGAGLADACE 729
Cdd:cd02204 1 DAAVLRIPGETDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPL-AITDCLNFGNPEKPEGEMGQLVEAVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 730 AMVTVMAALGVAVDGGKDSLSMAarvgTETVPAPGSLVISAYAVCPDITATVTPDLKHPGGKghLLYVPLSPGQHRLGGT 809
Cdd:cd02204 80 GLGDACRALGTPVIGGKDSLYNE----TEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDL--LYLIGETKDELGGSEY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 810 ALAqcFSQLGEHPPDLDLPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPAPGiHALPVLF 889
Cdd:cd02204 154 ALA--YHGLGGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDD-AEDELLF 230
|
250 260 270
....*....|....*....|....*....|....*
gi 564372564 890 AEEPGLVLEVQEADVAGVLqRYQSAGLHCLELGHT 924
Cdd:cd02204 231 SESLGRVLVEVKPENEEVF-EAEEAGVPATVIGTV 264
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
248-956 |
9.71e-61 |
|
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: 222.56 E-value: 9.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 248 VVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGrgAHVVAGTAGYCFGNLHIPgynlpwedpsfqypgnfaRPLEVAI 327
Cdd:TIGR01736 71 VVFKMESHNHPSAIEPYNGAATGVGGILRDILSMG--ARPIALLDSLRFGPLDDP------------------KNRYLFE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 328 EASNGASDYGNKFGEPVLAG---FARSLglqlpDGQrrewikPIMFSGGIGSMEAKHV--GKEPpEPGMEVVKVGGPVYR 402
Cdd:TIGR01736 131 GVVAGISDYGNRIGVPTVGGeveFDESY-----NGN------PLVNVMCVGLVRKDDIvtGKAK-GPGNKLVLVGGKTGR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 403 IGVGGGAASSVQVqGDNTSDLDFGAVQRGDPEMEQKMnrvIRACVEAPGGNPICSLHDQGAGGNGNVLKELSEPA--GAV 480
Cdd:TIGR01736 199 DGIGGATFASEEL-SEEAEEEDRPAVQVGDPFTEKLL---IEATLEAVDTGLVKGIKDLGAAGLTSASSEMAAKGglGAE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 481 IYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDRECLmgksgqgda 560
Cdd:TIGR01736 275 IYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVIGEVTDEGRIRLYYKGEVV--------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 561 pptpptpVDLDLDwVLGKMP--QKEfflQRKPPVLQPLALP-PDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGlvaq 637
Cdd:TIGR01736 346 -------ADLPIE-LLADAPeyERP---SEPPKYPEEEKEPePPADLEDAFLKVLSSPNIASKEWVYRQYDHEVQT---- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 638 qqcvGPLQTPLADVAVVALSHQELVGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKC--SGN----- 710
Cdd:TIGR01736 411 ----RTVVKPGEDAAVLRIKETGKLGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDClnFGNperpe 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 711 --WMWAAKLpgegAGLADACEamvtvmaALGVAVDGGKDSLSMAarvgTETVPAPGSLVISAYAVCPDITATVTPDLKhp 788
Cdd:TIGR01736 487 vyWQFVEAV----KGLGDACR-------ALGTPVVGGNVSLYNE----TNGVPIAPTPTIGMVGLVEDVEKLLTSNFK-- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 789 gGKGHLLYVplsPGQHR--LGGTALAQCFSQLGEH-PPDLDLpENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEM 865
Cdd:TIGR01736 550 -KEGDAIYL---IGETKdeLGGSEYLRVIHGIVSGqVPAVDL-EEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEM 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 866 AFAGNCGIEVDVPA-PGIHALPVLFAEEPG-LVLEVQEADVAGVLqryQSAGLHCLELGHTGeaGPQamVRVSVNGTVVV 943
Cdd:TIGR01736 625 AAASGIGAEVDIDEiASARPDELLFSESNGrAIVAVPEEKAEEAV---KSKGVPAKVIGKTG--GDR--LTIKTGDDTIS 697
|
730
....*....|...
gi 564372564 944 EEpVGQLRALWEE 956
Cdd:TIGR01736 698 VS-VKELRDAWEE 709
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
248-957 |
6.94e-54 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 202.26 E-value: 6.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 248 VVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGrgAHVVAGTAGYCFGNLhipgynlpwEDPSFQY--PGnfarplEV 325
Cdd:PRK01213 83 VVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMG--ARPIALLDSLRFGEL---------DHPKTRYllEG------VV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 326 AieasnGASDYGNKFGEPVLAG---FARSLglqlpDGQrrewikPIMFSGGIGSMEAKHVGK-EPPEPGMEVVKVGGPVY 401
Cdd:PRK01213 146 A-----GIGGYGNCIGVPTVGGevyFDESY-----NGN------PLVNAMCVGLVRHDDIVLaKASGVGNPVVYVGAKTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 402 RIGVGGGAASSVQVQGDNTSDLdfGAVQRGDPEMEQkmnRVIRACVEAPGGNPICSLHDQGAGGNGNVLKELSEPA--GA 479
Cdd:PRK01213 210 RDGIGGASFASAELSEESEEKR--PAVQVGDPFMEK---LLIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKGglGI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 480 VIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDflsraSARERC-----PACFVGTITGDKRIVLVDDRECLmgk 554
Cdd:PRK01213 285 ELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEE-----EVLAIFekwdlDAAVIGEVTDDGRLRVYHHGEVV--- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 555 sgqgdapptpptpVDLDLDWVLGKMPqkEFFLQRKPPVLQPLALPPDLSVGQALERVLRLPAVASKRYLTNKVDRSVGG- 633
Cdd:PRK01213 357 -------------ADVPAEALADEAP--VYDRPYKEPAYLDELQADPEDLKEALLKLLSSPNIASKEWVYEQYDHEVQTn 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 634 -LVAqqqcvgplqtPLADVAVVALSHQELvGAATALGEQPVKSLLDPKAAARLAVSEALTNLVfalvtdlrdvkCSG--- 709
Cdd:PRK01213 422 tVVK----------PGGDAAVLRIRGGGK-GLALTTDCNPRYVYLDPYEGAKLAVAEAARNLA-----------AVGatp 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 710 -------NW--------MW----AAKlpgegaGLADACEamvtvmaALGVAVDGGKDSLSmaarvgTETV-----PAPgs 765
Cdd:PRK01213 480 laitdclNFgnpekpevMWqfveAVR------GLADACR-------ALGTPVVGGNVSLY------NETGgtaiyPTP-- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 766 lVISAYAVCPDITATVTPDLKHPggkGHLLYVpLSPGQHRLGGTALAQCF-SQLGEHPPDLDLPE-----NLVRAfHITQ 839
Cdd:PRK01213 539 -VIGMVGLIDDVSKRTTSGFKKE---GDLIYL-LGETKDELGGSEYLKVIhGHVGGRPPKVDLEAekrlqELVRE-AIRE 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 840 GLLKdrrlcSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPApGIHALPVLFAEEPG-LVLEVQEADVAGVLQRYQSAGLHC 918
Cdd:PRK01213 613 GLVT-----SAHDVSEGGLAVALAEMAIAGGLGAEVDLSD-GLRPDALLFSESQGrYVVSVPPENEEAFEALAEAAGVPA 686
|
730 740 750
....*....|....*....|....*....|....*....
gi 564372564 919 LELGHTGEAGpqamVRVSVNGTVVVEEpvgqLRALWEET 957
Cdd:PRK01213 687 TRIGVVGGDA----LKVKGNDTESLEE----LREAWEGA 717
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
247-534 |
4.77e-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: 149.75 E-value: 4.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 247 HVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPgynlpwedpsfqypgnfarPLEVA 326
Cdd:cd02193 2 GEAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGIDAKPIALSANWMASAGHPG-------------------EDAIL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 327 IEASNGASDYGNKFGEPVLAGFARSLGL---QLPDGQRREWIKPIMFSGGIGSMEAKHVGK-EPPEPGMEVVKVGGPVYR 402
Cdd:cd02193 63 YDAVKGVAELCNQLGLPIPVGKDRMSMKtrwQEGNEQREMTHPPSLVISAFGRVRDDRHTLpQLSTEGNALLLIGGGKGH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 403 IGVGGGAASSVQVQGDntsDLDFGAVQRGDPEMEQKMNRVIRACVEApggNPICSLHDQGAGGNGNVLKELSEPA--GAV 480
Cdd:cd02193 143 NGLGGTALASVALSYR---QLGDKSAQVRDPAQEKGFYEAMQALVAA---GKLLAWHDRGAGGLLVALAELVFAGhcGVQ 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564372564 481 IYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVG 534
Cdd:cd02193 217 VDLAALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEAQYGLADCVHVLG 270
|
|
| FGAM_synth_I |
TIGR01737 |
phosphoribosylformylglycinamidine synthase I; In some species, ... |
1007-1245 |
6.92e-37 |
|
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: 139.05 E-value: 6.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1007 RVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLcsgavRLDTFRGVAFVGGFSYADVLGSakGWAAAVTFNPQAREEL 1086
Cdd:TIGR01737 2 KVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDG-----SLPDYDGVVLPGGFSYGDYLRA--GAIAAASPIMQEVREF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1087 GRfRRRPdtfSLGVCNGCQLLALLGwvgsdpnedqvepdhdsqpAQPGLLLrHNLSGRFESRWATVRVEPGPALMLRGM- 1165
Cdd:TIGR01737 75 AE-KGVP---VLGICNGFQILVEAG-------------------LLPGALL-PNDSLRFICRWVYLRVENADTIFTKNYk 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1166 EGSVLPVWSAHGEGYMAFSSPELqAKIKAKGLVPLHWADDDGNPTEQYplNPNGSPGGIAGICSPDGRHLALMPHPERAV 1245
Cdd:TIGR01737 131 KGEVIRIPIAHGEGRYYADDETL-ARLESNDQVVFRYCDEDGDVAEEA--NPNGSVGNIAGIVNERGNVLGMMPHPERAS 207
|
|
| PRK01175 |
PRK01175 |
phosphoribosylformylglycinamidine synthase I; Provisional |
1006-1259 |
8.86e-36 |
|
phosphoribosylformylglycinamidine synthase I; Provisional
Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 137.20 E-value: 8.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1006 PRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAVtfNPQAREE 1085
Cdd:PRK01175 4 IRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAAERKSVSDYDCLVIPGGFSAGDYIRAGAIFAARL--KAVLRKD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1086 LGRFRRRpDTFSLGVCNGCQLLALLGwvgsdpnedqVEPDHDSQPAQPGLLLRHNLSGRFESRWATVRVEPGPALMLRGM 1165
Cdd:PRK01175 82 IEEFIDE-GYPIIGICNGFQVLVELG----------LLPGFDEIAEKPEMALTVNESNRFECRPTYLKKENRKCIFTKLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1166 EGSVLPVWSAHGEGYMAFSSPELQAKIKAKGLVPLHWADDDGNpTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPERAV 1245
Cdd:PRK01175 151 KKDVFQVPVAHAEGRVVFSEEEILERLIENDQIVFRYVDENGN-YAGYPWNPNGSIYNIAGITNEKGNVIGLMPHPERAF 229
|
250
....*....|....*..
gi 564372564 1246 RLWQ---WAWRPSPFDG 1259
Cdd:PRK01175 230 YGYQhpyWEKEEDYGDG 246
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
1007-1245 |
2.63e-28 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 114.06 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1007 RVAILREEGSNGDREMADAF-HLAGFE---VWdvtmqdlcSGAVRLDTFRGVAFVGGFSYADVLGSakGWAAAvtFNPqA 1082
Cdd:PRK03619 2 KVAVIVFPGSNCDRDMARALrDLLGAEpeyVW--------HKETDLDGVDAVVLPGGFSYGDYLRC--GAIAA--FSP-I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1083 REELGRFRRRpDTFSLGVCNGCQLLA---LLgwvgsdpnedqvepdhdsqpaqPGLLLRhNLSGRFESRWATVRVEPGPA 1159
Cdd:PRK03619 69 MKAVKEFAEK-GKPVLGICNGFQILTeagLL----------------------PGALTR-NASLKFICRDVHLRVENNDT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1160 LMLRGME-GSVL--PVwsAHGEG-YmaFSSPELQAKIKAKGLVPLHWADDdgnpteqyplNPNGSPGGIAGICSPDGRHL 1235
Cdd:PRK03619 125 PFTSGYEkGEVIriPI--AHGEGnY--YADEETLKRLEGNGQVVFRYCDE----------NPNGSVNDIAGIVNEKGNVL 190
|
250
....*....|
gi 564372564 1236 ALMPHPERAV 1245
Cdd:PRK03619 191 GMMPHPERAV 200
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
388-546 |
2.01e-26 |
|
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: 106.28 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 388 EPGMEVVKVGGpvyrIGVGGGAASSVQVQGDNTSDldfGAVQRGDPEMEQKMNRVIRACVEApgGNPICSLHDQGAGGNG 467
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLEDSGL---AAVQLGDPLLEPTLIYVKLLLAAL--GGLVKAMHDITGGGLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 468 NVLKELSEPA--GAVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLV 545
Cdd:pfam02769 72 GALAEMAPASgvGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVI 151
|
.
gi 564372564 546 D 546
Cdd:pfam02769 152 V 152
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
663-909 |
2.20e-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: 107.38 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 663 GAATALGEQPVKSLLDPKAAARLAVSEALTNlVFALVTDLRDVKCSGNWMWAAKLPGEGAGLADACEAMVTVMAALGVAV 742
Cdd:cd02193 2 GEAMKIEEHNHPAAIDPAAGAATGVGGAIRD-IAATGIDAKPIALSANWMASAGHPGEDAILYDAVKGVAELCNQLGLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 743 DGGKDSLSMAAR--VGTETVPA--PGSLVISAYAVCPDITATVtPDLKHPGGKghLLYVPLSPGQHRLGGTALAQ---CF 815
Cdd:cd02193 81 PVGKDRMSMKTRwqEGNEQREMthPPSLVISAFGRVRDDRHTL-PQLSTEGNA--LLLIGGGKGHNGLGGTALASvalSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 816 SQLGEHPPDLDLPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPA-----PGIHALPV-LF 889
Cdd:cd02193 158 RQLGDKSAQVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAAlgddePDMEPLEIaLF 237
|
250 260
....*....|....*....|
gi 564372564 890 AEEPGLVLEVQEADVAGVLQ 909
Cdd:cd02193 238 ESQERGVIQVRAEDRDAVEE 257
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
248-513 |
2.00e-15 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 81.05 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 248 VVFTAETHNFPTGVAPFSGATTGTGGRIRDVqcTGRGAHVVAgtagyCFGNLHIpgynlpwedpsfqypgnfARPLEVAI 327
Cdd:PRK14090 63 IAFKIESHNHPSAIEPYNGAATGVGGIIRDV--LAMGARPTA-----IFDSLHM------------------SRIIDGII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 328 EasnGASDYGNKFGEPVLAGfarslGLQLPDGQRREWIKPIMfSGGIGSMEaKHVGKEPPEPGMEVVKVGGPVYRIGVGG 407
Cdd:PRK14090 118 E---GIADYGNSIGVPTVGG-----ELRISSLYAHNPLVNVL-AAGVVRND-MLVDSKASRPGQVIVIFGGATGRDGIHG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 408 GAASSVQVQGDNTSDLdfgAVQRGDPEMEQKMnrvIRACVEAPGGNPICSLHDQGAGGngnVLKELSEPA-----GAVIY 482
Cdd:PRK14090 188 ASFASEDLTGEKATKL---SIQVGDPFAEKML---IEAFLEMVEEGLVEGAQDLGAGG---VLSATSELVakgglGAIVH 258
|
250 260 270
....*....|....*....|....*....|.
gi 564372564 483 TSRFQLGDPTLNALEIWGAEYQESNALLLRP 513
Cdd:PRK14090 259 LDRVPLREPDMEPWEILISESQERMAVVTSP 289
|
|
| FGAR-AT_N |
pfam18076 |
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain ... |
12-105 |
8.97e-14 |
|
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: 69.04 E-value: 8.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 12 LLQddvARESWLVPGSNDLLLEVGPRLNFSTP-AS--TNIVSVCqaaGLRAVDRVETTRRYRLSFAKQPTAEMEAIsLAA 88
Cdd:pfam18076 23 LLT---YGPPLEEPEPEGELLLVTPRLGTISPwSSkaTDIAHNC---GLDAVRRIERGIAYYLTGKPLSAAELAAL-AAL 95
|
90 100
....*....|....*....|
gi 564372564 89 LHDRMTEQ---HYPDPIQSF 105
Cdd:pfam18076 96 LHDRMTESvltDLEDAAALF 115
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
128-176 |
1.84e-10 |
|
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: 57.09 E-value: 1.84e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564372564 128 LEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEVFDLAQSNSEHSRH 176
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYFAGLGRNPTDVELGMFAQMWSEHCRH 49
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
849-928 |
7.35e-10 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 58.90 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 849 SGHDVSDGGLVTCLLEMAFAGNCGIEVDVPAP-----GIHALPVLFAEEPG-LVLEVQEADVAGVLQRYQSAGLHCLELG 922
Cdd:pfam02769 61 AMHDITGGGLAGALAEMAPASGVGAEIDLDKVpifeeLMLPLEMLLSENQGrGLVVVAPEEAEAVLAILEKEGLEAAVIG 140
|
....*.
gi 564372564 923 HTGEAG 928
Cdd:pfam02769 141 EVTAGG 146
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
665-922 |
4.87e-08 |
|
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: 55.09 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 665 ATALGEQPVKSLLDPKAAARLAVSEALTNLVfalVTDLRDVKCSGNWMWAAklPGEGAGLADACEAMVTVMAALGVAVDG 744
Cdd:cd00396 3 AMSTDGINPPLAINPWAGGRLAVGGAVNDIA---AMGARPIALLASLSLSN--GLEVDILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 745 GKDSLSMAarvgtetvpapgslvisaYAVCPDITATvtpdlkhpGGKGHLLYVPLSPGQHRLGGTALaqcfsqlgehppd 824
Cdd:cd00396 78 GHTSVSPG------------------TMGHKLSLAV--------FAIGVVEKDRVIDSSGARPGDVL------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 825 ldlpenLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVD---VPAP--------GIHALPVLFAEEP 893
Cdd:cd00396 119 ------ILTGVDAVLELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDleaIPLDevvrwlcvEHIEEALLFNSSG 192
|
250 260
....*....|....*....|....*....
gi 564372564 894 GLVLEVQEADVAGVLQRYQSAGLHCLELG 922
Cdd:cd00396 193 GLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
1008-1109 |
6.99e-05 |
|
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: 43.36 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1008 VAILREEGSNGD--REMADAFHLAGFEVWDVTMQ-DLCSGAVRLDTFRGVAFVGGFSYADVLgsakgwaaavTFNPQARE 1084
Cdd:cd01653 1 VAVLLFPGFEELelASPLDALREAGAEVDVVSPDgGPVESDVDLDDYDGLILPGGPGTPDDL----------ARDEALLA 70
|
90 100
....*....|....*....|....*
gi 564372564 1085 ELGRFRRRpDTFSLGVCNGCQLLAL 1109
Cdd:cd01653 71 LLREAAAA-GKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
1008-1107 |
4.65e-04 |
|
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: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 1008 VAILREEGSNGD--REMADAFHLAGFEVWDVTMQ-DLCSGAVRLDTFRGVAFVGGFSYADVLgsakgwaaavTFNPQARE 1084
Cdd:cd03128 1 VAVLLFGGSEELelASPLDALREAGAEVDVVSPDgGPVESDVDLDDYDGLILPGGPGTPDDL----------AWDEALLA 70
|
90 100
....*....|....*....|...
gi 564372564 1085 ELGRFRRRpDTFSLGVCNGCQLL 1107
Cdd:cd03128 71 LLREAAAA-GKPVLGICLGAQLL 92
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
851-948 |
8.33e-03 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 40.06 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372564 851 HDVSDGGLVTCLLEMAFAGNCGIEVD---VP-APGIHAL-------PVLFAEEPGLVLEVQEADVAGVLQRYQSAGLHCL 919
Cdd:COG0309 212 RDPTRGGLAGALNEIAEASGVGIEIDedaIPvRPEVRGIcellgldPLYLANEGKLVAVVPPEDAEAVLEALRAHGIDAA 291
|
90 100 110
....*....|....*....|....*....|.
gi 564372564 920 ELGHTgEAGPQAMVRV--SVNGTVVVEEPVG 948
Cdd:COG0309 292 IIGEV-TEGPPGRVVLktAIGGERILDPPEG 321
|
|
| |
