|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
11-727 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 1168.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 11 EVKVEKLYRDMGLSDAEFEKVTEILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEHVLMGPGEGAGVVDIGDN 90
Cdd:PRK01213 1 TPDTEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGENAGVVDIGDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 91 QAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELTEKTNRRLLRGVVAGIGGYGNCIGIPTT 170
Cdd:PRK01213 81 QAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 171 AGEIEFDERYDGNPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRPSVQIGDPF 250
Cdd:PRK01213 161 GGEVYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGASFASAELSEESEEKRPAVQVGDPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 251 VGKKLMEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGT 330
Cdd:PRK01213 241 MEKLLIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 331 EQKFLDLFDYHELDSAVIGEVTDTNRFVLTYEGEVFADIPVEPLADEAPVYILEGEPLQHDTAPNRyDDIDVNDVFDRLL 410
Cdd:PRK01213 321 EEEVLAIFEKWDLDAAVIGEVTDDGRLRVYHHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQA-DPEDLKEALLKLL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 411 THPTIASKHYLYDQYDQQVGANTIIKPGLQASVVRVEGTNKAIASTIDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKP 490
Cdd:PRK01213 400 SSPNIASKEWVYEQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 491 LAMTDCLNYGSPEKKHIYQQLTDSTRGMAEACEALATPVVSGNVSLYNETRTSSIFPTPVVGMVGLIENIDF-LKSYQPS 569
Cdd:PRK01213 480 LAITDCLNFGNPEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKrTTSGFKK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 570 IGDTLYVIGETTDSYGGSQIEKLLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSL 649
Cdd:PRK01213 560 EGDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 650 GidAEVNLTN-----AQLFSETQGRYIVAVKAGQTLNIEG--------ATRIGTlTDTDDFKVVAQDSVIerrTSELKRE 716
Cdd:PRK01213 640 G--AEVDLSDglrpdALLFSESQGRYVVSVPPENEEAFEAlaeaagvpATRIGV-VGGDALKVKGNDTES---LEELREA 713
|
730
....*....|.
gi 505960966 717 WEGAIESCMTS 727
Cdd:PRK01213 714 WEGALPRLLGG 724
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
23-725 |
0e+00 |
|
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: 1013.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 23 LSDAEFEKVTEILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEHVLMGPGEGAGVVDIGDNQAVVFKVESHNH 102
Cdd:TIGR01736 1 LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYAVVFKMESHNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 103 PSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELTEKTNRRLLRGVVAGIGGYGNCIGIPTTAGEIEFDERYDG 182
Cdd:TIGR01736 81 PSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 183 NPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEE-LTEESESKRPSVQIGDPFVGKKLMEATLE 261
Cdd:TIGR01736 161 NPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEElSEEAEEEDRPAVQVGDPFTEKLLIEATLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 262 AITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYH 341
Cdd:TIGR01736 241 AVDTGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 342 ELDSAVIGEVTDTNRFVLTYEGEVFADIPVEPLADeAPVYILEGEPLQHDTAPNRYD-DIDVNDVFDRLLTHPTIASKHY 420
Cdd:TIGR01736 321 ELPASVIGEVTDEGRIRLYYKGEVVADLPIELLAD-APEYERPSEPPKYPEEEKEPEpPADLEDAFLKVLSSPNIASKEW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 421 LYDQYDQQVGANTIIKPGLQASVVRVEGTNK-AIASTIDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLNY 499
Cdd:TIGR01736 400 VYRQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 500 GSPEKKHIYQQLTDSTRGMAEACEALATPVVSGNVSLYNETRTSSIFPTPVVGMVGLIENIDFL-KSYQPSIGDTLYVIG 578
Cdd:TIGR01736 480 GNPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLlTSNFKKEGDAIYLIG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 579 ETTDSYGGSQIEKLLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSLGIDAEVN-- 656
Cdd:TIGR01736 560 ETKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGAEVDIDei 639
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960966 657 ---LTNAQLFSETQGRYIVAVKAGQTL-----NIEGATRIGTlTDTDDFKVVAQDSVIERRTSELKREWEGAIESCM 725
Cdd:TIGR01736 640 asaRPDELLFSESNGRAIVAVPEEKAEeavksKGVPAKVIGK-TGGDRLTIKTGDDTISVSVKELRDAWEEALPEYM 715
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
5-727 |
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: 1013.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 5 LEPTAEEVKVEKLYRDMGLSDAEFEKVTEILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEHVLMGPGEGAGV 84
Cdd:COG0046 6 LEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPTEGPRVLSGPGDNAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 85 VDIGDNQAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELT--EKTNRRLLRGVVAGIGGYG 162
Cdd:COG0046 86 VDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDqpPASPRYILIGVVAGIADYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 163 NCIGIPTTAGEIEFDERYDGNPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRP 242
Cdd:COG0046 166 NCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSELDRP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 243 SVQIGDPFVGKKLMEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERM 322
Cdd:COG0046 246 AVQVGDPFMEKRLIEAILELGDTGLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 323 LLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNRFVLTYEGEVFADIPVEPLADEAPVYILEGEPLQHDTAPNRYDDIDV 402
Cdd:COG0046 326 LLVVKPEKLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLDLPEPIDL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 403 NDVFDRLLTHPTIASKHYLYDQYDQQVGANTIIKPGLQ-ASVVRVEGTNKAIASTIDGEARYVFNDPYEGGKMVVAEAYR 481
Cdd:COG0046 406 EEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDPGVAdAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAVAEAAR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 482 NLIAVGAKPLAMTDCLNYGSPEKKHIYQQLTDSTRGMAEACEALATPVVSGNVSLYNETR--TSSIFPTPVVGMVGLIEN 559
Cdd:COG0046 486 NLAAVGAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKdgKVAIPPTPVIGAVGLVDD 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 560 IDFLKSYQ-PSIGDTLYVIGETTDSYGGSQIEKlLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAV 638
Cdd:COG0046 566 VRKTVTPDlKKEGDLLYLIGETKNELGGSEYAQ-VLGQLGGEPPDVDLEAEKALFEAVQELIREGLILAAHDVSDGGLAV 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 639 TLAKISAHYSLGIDAEVNLTN-----AQLFSETQGRYIVAVKAGQTLNIEG--------ATRIGTLTDTDDFKV-VAQDS 704
Cdd:COG0046 645 ALAEMAFAGGLGADIDLDALGdlrpdAALFSESQGRAVVQVAPEDAEAVEAllaeaglpAHVIGTVTGDDRLVIrRGGET 724
|
730 740
....*....|....*....|...
gi 505960966 705 VIERRTSELKREWEGAIESCMTS 727
Cdd:COG0046 725 LLSLSLAELRDAWEETLPRLRDN 747
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
43-369 |
3.78e-168 |
|
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: 485.44 E-value: 3.78e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 43 ETGIFSVMWSEHCSYKHSKPFLKQFpttgehvlmgpgegagvvdigdnQAVVFKVESHNHPSAIEPYQGAATGVGGIIRD 122
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLLKMI-----------------------WAVVFKVETHNHPSAIEPFGGAATGVGGIIRD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 123 IVSIGARPINLLNSLRFGELTEK--------TNRRLLRGVVAGIGGYGNCIGIPTTAGEIEFDERYDGNPLVNAMCVGVI 194
Cdd:cd02203 58 ILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 195 DHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFA-SEELTEESESKRPSVQIGDPFVGKKLMEATLEAITYDELVGIQD 273
Cdd:cd02203 138 PKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSsKELSENSSELDRPAVQVGDPFMEKKLQEAILEARETGLIVGIQD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 274 MGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTD 353
Cdd:cd02203 218 LGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTD 297
|
330
....*....|....*.
gi 505960966 354 TNRFVLTYEGEVFADI 369
Cdd:cd02203 298 DGRLRLYYKGEVVADL 313
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
206-361 |
2.34e-35 |
|
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: 130.93 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 206 GVGNSVIYVGLktgrDGIHGATFASEELTEESEsKRPSVQIGDPFVGKKLMEATLEAITYDELV-GIQDMGAAGLTSSSS 284
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLEDS-GLAAVQLGDPLLEPTLIYVKLLLAALGGLVkAMHDITGGGLAGALA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960966 285 EMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNRFVLTY 361
Cdd:pfam02769 76 EMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
11-727 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 1168.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 11 EVKVEKLYRDMGLSDAEFEKVTEILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEHVLMGPGEGAGVVDIGDN 90
Cdd:PRK01213 1 TPDTEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGENAGVVDIGDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 91 QAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELTEKTNRRLLRGVVAGIGGYGNCIGIPTT 170
Cdd:PRK01213 81 QAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 171 AGEIEFDERYDGNPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRPSVQIGDPF 250
Cdd:PRK01213 161 GGEVYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGASFASAELSEESEEKRPAVQVGDPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 251 VGKKLMEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGT 330
Cdd:PRK01213 241 MEKLLIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 331 EQKFLDLFDYHELDSAVIGEVTDTNRFVLTYEGEVFADIPVEPLADEAPVYILEGEPLQHDTAPNRyDDIDVNDVFDRLL 410
Cdd:PRK01213 321 EEEVLAIFEKWDLDAAVIGEVTDDGRLRVYHHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQA-DPEDLKEALLKLL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 411 THPTIASKHYLYDQYDQQVGANTIIKPGLQASVVRVEGTNKAIASTIDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKP 490
Cdd:PRK01213 400 SSPNIASKEWVYEQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 491 LAMTDCLNYGSPEKKHIYQQLTDSTRGMAEACEALATPVVSGNVSLYNETRTSSIFPTPVVGMVGLIENIDF-LKSYQPS 569
Cdd:PRK01213 480 LAITDCLNFGNPEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKrTTSGFKK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 570 IGDTLYVIGETTDSYGGSQIEKLLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSL 649
Cdd:PRK01213 560 EGDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 650 GidAEVNLTN-----AQLFSETQGRYIVAVKAGQTLNIEG--------ATRIGTlTDTDDFKVVAQDSVIerrTSELKRE 716
Cdd:PRK01213 640 G--AEVDLSDglrpdALLFSESQGRYVVSVPPENEEAFEAlaeaagvpATRIGV-VGGDALKVKGNDTES---LEELREA 713
|
730
....*....|.
gi 505960966 717 WEGAIESCMTS 727
Cdd:PRK01213 714 WEGALPRLLGG 724
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
23-725 |
0e+00 |
|
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: 1013.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 23 LSDAEFEKVTEILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEHVLMGPGEGAGVVDIGDNQAVVFKVESHNH 102
Cdd:TIGR01736 1 LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYAVVFKMESHNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 103 PSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELTEKTNRRLLRGVVAGIGGYGNCIGIPTTAGEIEFDERYDG 182
Cdd:TIGR01736 81 PSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 183 NPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEE-LTEESESKRPSVQIGDPFVGKKLMEATLE 261
Cdd:TIGR01736 161 NPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEElSEEAEEEDRPAVQVGDPFTEKLLIEATLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 262 AITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYH 341
Cdd:TIGR01736 241 AVDTGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 342 ELDSAVIGEVTDTNRFVLTYEGEVFADIPVEPLADeAPVYILEGEPLQHDTAPNRYD-DIDVNDVFDRLLTHPTIASKHY 420
Cdd:TIGR01736 321 ELPASVIGEVTDEGRIRLYYKGEVVADLPIELLAD-APEYERPSEPPKYPEEEKEPEpPADLEDAFLKVLSSPNIASKEW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 421 LYDQYDQQVGANTIIKPGLQASVVRVEGTNK-AIASTIDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLNY 499
Cdd:TIGR01736 400 VYRQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 500 GSPEKKHIYQQLTDSTRGMAEACEALATPVVSGNVSLYNETRTSSIFPTPVVGMVGLIENIDFL-KSYQPSIGDTLYVIG 578
Cdd:TIGR01736 480 GNPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLlTSNFKKEGDAIYLIG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 579 ETTDSYGGSQIEKLLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSLGIDAEVN-- 656
Cdd:TIGR01736 560 ETKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGAEVDIDei 639
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960966 657 ---LTNAQLFSETQGRYIVAVKAGQTL-----NIEGATRIGTlTDTDDFKVVAQDSVIERRTSELKREWEGAIESCM 725
Cdd:TIGR01736 640 asaRPDELLFSESNGRAIVAVPEEKAEeavksKGVPAKVIGK-TGGDRLTIKTGDDTISVSVKELRDAWEEALPEYM 715
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
5-727 |
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: 1013.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 5 LEPTAEEVKVEKLYRDMGLSDAEFEKVTEILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEHVLMGPGEGAGV 84
Cdd:COG0046 6 LEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPTEGPRVLSGPGDNAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 85 VDIGDNQAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELT--EKTNRRLLRGVVAGIGGYG 162
Cdd:COG0046 86 VDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDqpPASPRYILIGVVAGIADYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 163 NCIGIPTTAGEIEFDERYDGNPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRP 242
Cdd:COG0046 166 NCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSELDRP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 243 SVQIGDPFVGKKLMEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERM 322
Cdd:COG0046 246 AVQVGDPFMEKRLIEAILELGDTGLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 323 LLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNRFVLTYEGEVFADIPVEPLADEAPVYILEGEPLQHDTAPNRYDDIDV 402
Cdd:COG0046 326 LLVVKPEKLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLDLPEPIDL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 403 NDVFDRLLTHPTIASKHYLYDQYDQQVGANTIIKPGLQ-ASVVRVEGTNKAIASTIDGEARYVFNDPYEGGKMVVAEAYR 481
Cdd:COG0046 406 EEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDPGVAdAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAVAEAAR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 482 NLIAVGAKPLAMTDCLNYGSPEKKHIYQQLTDSTRGMAEACEALATPVVSGNVSLYNETR--TSSIFPTPVVGMVGLIEN 559
Cdd:COG0046 486 NLAAVGAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKdgKVAIPPTPVIGAVGLVDD 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 560 IDFLKSYQ-PSIGDTLYVIGETTDSYGGSQIEKlLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAV 638
Cdd:COG0046 566 VRKTVTPDlKKEGDLLYLIGETKNELGGSEYAQ-VLGQLGGEPPDVDLEAEKALFEAVQELIREGLILAAHDVSDGGLAV 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 639 TLAKISAHYSLGIDAEVNLTN-----AQLFSETQGRYIVAVKAGQTLNIEG--------ATRIGTLTDTDDFKV-VAQDS 704
Cdd:COG0046 645 ALAEMAFAGGLGADIDLDALGdlrpdAALFSESQGRAVVQVAPEDAEAVEAllaeaglpAHVIGTVTGDDRLVIrRGGET 724
|
730 740
....*....|....*....|...
gi 505960966 705 VIERRTSELKREWEGAIESCMTS 727
Cdd:COG0046 725 LLSLSLAELRDAWEETLPRLRDN 747
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
43-369 |
3.78e-168 |
|
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: 485.44 E-value: 3.78e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 43 ETGIFSVMWSEHCSYKHSKPFLKQFpttgehvlmgpgegagvvdigdnQAVVFKVESHNHPSAIEPYQGAATGVGGIIRD 122
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLLKMI-----------------------WAVVFKVETHNHPSAIEPFGGAATGVGGIIRD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 123 IVSIGARPINLLNSLRFGELTEK--------TNRRLLRGVVAGIGGYGNCIGIPTTAGEIEFDERYDGNPLVNAMCVGVI 194
Cdd:cd02203 58 ILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 195 DHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFA-SEELTEESESKRPSVQIGDPFVGKKLMEATLEAITYDELVGIQD 273
Cdd:cd02203 138 PKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSsKELSENSSELDRPAVQVGDPFMEKKLQEAILEARETGLIVGIQD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 274 MGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTD 353
Cdd:cd02203 218 LGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTD 297
|
330
....*....|....*.
gi 505960966 354 TNRFVLTYEGEVFADI 369
Cdd:cd02203 298 DGRLRLYYKGEVVADL 313
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
33-603 |
1.58e-139 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 422.73 E-value: 1.58e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 33 EILGRTPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTTGEhvlmgpGEGAGVVDIGDNQAVVFKVESHNHPSAIEPYQGA 112
Cdd:PRK14090 9 EKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGF------EGNAGVVNLDDYYSIAFKIESHNHPSAIEPYNGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 113 ATGVGGIIRDIVSIGARPINLLNSLRFgeltektnRRLLRGVVAGIGGYGNCIGIPTTAGEIEFDERYDGNPLVNAMCVG 192
Cdd:PRK14090 83 ATGVGGIIRDVLAMGARPTAIFDSLHM--------SRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 193 VIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRpSVQIGDPFVGKKLMEATLEAITYDELVGIQ 272
Cdd:PRK14090 155 VVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGEKATKL-SIQVGDPFAEKMLIEAFLEMVEEGLVEGAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 273 DMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVT 352
Cdd:PRK14090 234 DLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVAEVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 353 DTNRFVLTYEGEVFADIPVEPLADEAPVYILEGEPlqhDTAPnRYDDIDVNDVFDRllthptiaskhYLYDQYDQQVGAN 432
Cdd:PRK14090 314 DDPIYRVMYRDDLVMEVPVQLLANAPEEEIVEYTP---GEIP-EFKRVEFEEVNAR-----------EVFEQYDHMVGTD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 433 TIIKPGLQASVVRVEGTNKAIASTiDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLNYGSPEKKHIyqQLT 512
Cdd:PRK14090 379 TVLPPGFGAAVMRIKRDGGYSLVT-HSRADLALQDTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGDPDVDPV--GLS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 513 DSTRGMAEACEALATPVVSGNVSLYNETRTSSIFPTPVVGMVGlieNIDFLKSYQPSIGDtLYVIGETTDSYggsQIEKL 592
Cdd:PRK14090 456 AMMTALKDACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG---KVNPQKVAKPKPSK-VFAVGWNDFEL---EREKE 528
|
570
....*....|.
gi 505960966 593 LYSDVNHEVEK 603
Cdd:PRK14090 529 LWREIRKLSEE 539
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
440-690 |
1.96e-83 |
|
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: 265.17 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 440 QASVVRV-EGTNKAIASTIDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLNYGSPEK-KHIYQQLTDSTRG 517
Cdd:cd02204 1 DAAVLRIpGETDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKpEGEMGQLVEAVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 518 MAEACEALATPVVSGNVSLYNETRTSSIFPTPVVGMVGLIENIDFLKSYQPS-IGDTLYVIGETTDSYGGSQIEKLLYSD 596
Cdd:cd02204 81 LGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKkEGDLLYLIGETKDELGGSEYALAYHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 597 VNHEVEKVDLSQEAAKGEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSLGIDAEVNL---TNAQLFSETQGRYIVA 673
Cdd:cd02204 161 GGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKddaEDELLFSESLGRVLVE 240
|
250 260
....*....|....*....|...
gi 505960966 674 VKAGQTLNIE------GATRIGT 690
Cdd:cd02204 241 VKPENEEVFEaeeagvPATVIGT 263
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
93-351 |
2.37e-53 |
|
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: 185.19 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 93 VVFKVESHNHPSAIEPYQGAATGVGGIIRDIVS--IGARPINLLNSLRFGELtEKTNRRLLRGVVAGIGGYGNCIGIPTT 170
Cdd:cd02193 3 EAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAAtgIDAKPIALSANWMASAG-HPGEDAILYDAVKGVAELCNQLGLPIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 171 AGEIEFDERYDG-----------NPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESES 239
Cdd:cd02193 82 VGKDRMSMKTRWqegneqremthPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNGLGGTALASVALSYRQLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 240 KRPsVQIGDPFVGKKLMEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQ 319
Cdd:cd02193 162 DKS-AQVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIALFESQ 240
|
250 260 270
....*....|....*....|....*....|..
gi 505960966 320 ERMLLVVKKGTEQKFLDLFDYHELDSAVIGEV 351
Cdd:cd02193 241 ERGVIQVRAEDRDAVEEAQYGLADCVHVLGQA 272
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
206-361 |
2.34e-35 |
|
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: 130.93 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 206 GVGNSVIYVGLktgrDGIHGATFASEELTEESEsKRPSVQIGDPFVGKKLMEATLEAITYDELV-GIQDMGAAGLTSSSS 284
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLEDS-GLAAVQLGDPLLEPTLIYVKLLLAALGGLVkAMHDITGGGLAGALA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960966 285 EMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNRFVLTY 361
Cdd:pfam02769 76 EMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
92-350 |
2.39e-32 |
|
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: 124.82 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 92 AVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELTEKTnrrLLRGVVAGIGGYGNCIGIPTTA 171
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVD---ILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 172 GEIEFDERYDG-NPLVNAMCVGVIDHDMIQKGTAKGVGNSVIYVGLktgrdgihgatfaseelteeseskrpsvqigdpf 250
Cdd:cd00396 78 GHTSVSPGTMGhKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGV---------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 251 vgkklmEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREKGIS-----PYEMMLSETQERMLLV 325
Cdd:cd00396 124 ------DAVLELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWlcvehIEEALLFNSSGGLLIA 197
|
250 260
....*....|....*....|....*
gi 505960966 326 VKKGTEQKFLDLFDYHELDSAVIGE 350
Cdd:cd00396 198 VPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
89-194 |
5.89e-28 |
|
AIR synthase related protein, N-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 N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 108.30 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 89 DNQAVVFKVESHNHPSAIEPYQG-AATGVGGIIRDIVSIGARPINLLNSLRFGELTEktNRRLLRGVVAGIGGYGNCIGI 167
Cdd:pfam00586 1 DDAAVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPE--VEWVLEEIVEGIAEACREAGV 78
|
90 100
....*....|....*....|....*..
gi 505960966 168 PTTAGEIEFDERYDgNPLVNAMCVGVI 194
Cdd:pfam00586 79 PLVGGDTSFDPEGG-KPTISVTAVGIV 104
|
|
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
96-421 |
8.01e-28 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 120.67 E-value: 8.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 96 KVESHNHPSAIEPYQGAATGVGGIIRD--IVSIGARPI---------NLlNSLRFGELTEKTNRRLLRGVVA------G- 157
Cdd:PRK05297 288 KVETHNHPTAISPFPGAATGSGGEIRDegATGRGSKPKagltgfsvsNL-RIPGFEQPWEEDYGKPERIASAldimieGp 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 158 IGG--YGNCIGIPTTAGEI-EFDERYDGN---------PLVNAMCVGVIDHDMIQKGTAKgVGNSVIYVGlktG---RDG 222
Cdd:PRK05297 367 LGGaaFNNEFGRPNLLGYFrTFEQKVNSHneevrgyhkPIMLAGGIGNIRADHVQKGEIP-VGAKLIVLG---GpamRIG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 223 IHGAT--------------FAseelteeseskrpSVQIGDPfvgkkLMEATL-EAItyD---EL------VGIQDMGAAG 278
Cdd:PRK05297 443 LGGGAassmasgqssedldFA-------------SVQRGNP-----EMERRCqEVI--DrcwQLgddnpiLSIHDVGAGG 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 279 LTSSSSEMAAKGGSGIHLELEKVPVREKGISPYEMMLSETQERMLLVVKkgteQKFLDLFD---------YheldsAVIG 349
Cdd:PRK05297 503 LSNAFPELVNDGGRGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIA----PEDLELFEaicerercpF-----AVVG 573
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505960966 350 EVTDTNRFVLtyEGEVFADIPVE-PLAD---EAPVYILEGEPLQHDTAPNRYDDIDVNDVFDRLLTHPTIASKHYL 421
Cdd:PRK05297 574 EATEERHLTL--EDSHFDNKPVDlPLDVllgKPPKMHRDVKTVKAKGPALDYSGIDLAEAVERVLRLPTVASKSFL 647
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
452-557 |
9.99e-25 |
|
AIR synthase related protein, N-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 N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 99.06 E-value: 9.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 452 AIASTIDGEARYVFNDPYEG-GKMVVAEAYRNLIAVGAKPLAMTDCLNYgsPEKKHIYQQLTDSTRGMAEACEALATPVV 530
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLAL--PGGPEVEWVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....*..
gi 505960966 531 SGNVSLYNEtrtsSIFPTPVVGMVGLI 557
Cdd:pfam00586 82 GGDTSFDPE----GGKPTISVTAVGIV 104
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
15-58 |
3.59e-17 |
|
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: 75.58 E-value: 3.59e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 505960966 15 EKLYRDMGLSDAEFEKVTEI---LGRTPNFTETGIFSVMWSEHCSYK 58
Cdd:pfam18072 4 ANRYLGLALSDDEIDYLVEYfagLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
93-718 |
2.20e-16 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 83.66 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 93 VVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIG-------------------------------ARPINLLNSLRFge 141
Cdd:PLN03206 288 ILLTAETHNFPCAVAPYPGAETGAGGRIRDTHATGrgsfvvagtagycvgnlriegsyapwedssfVYPSNLASPLQI-- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 142 LTEKTNrrllrgvvaGIGGYGNCIGIPTTAG-------EIEFDERYDG-NPLVNAMCVGVIDHDMIQKGTAKgVGNSVIY 213
Cdd:PLN03206 366 LIDASN---------GASDYGNKFGEPLIQGytrtfgmRLPNGERREWlKPIMFSGGIGQIDHTHLTKGEPD-IGMLVVK 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 214 VGLKTGRDGIHG-ATFASEELTEESESKRPSVQIGDPFVGKKL---MEATLEAITYDELVGIQDMGAAGLTSSSSEMA-A 288
Cdd:PLN03206 436 IGGPAYRIGMGGgAASSMVSGQNDAELDFNAVQRGDAEMSQKLyrvVRACVEMGEDNPIVSIHDQGAGGNCNVVKEIIyP 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 289 KGGSgihLELEKVPVREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNRFVLTyEGEVFAD 368
Cdd:PLN03206 516 KGAE---IDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPESRDLLQSICDRERCSMAVIGTIDGSGRVVLV-DSAAPEK 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 369 IPVEPLADEAPVYILEGEPLQHDTAPNRYDD---------------IDVNDVFDRLLTHPTIASKHYLYDQYD------- 426
Cdd:PLN03206 592 CEANGLPPPPPAVDLDLEKVLGDMPQKTFEFkrvanklepldippgITVMDALKRVLRLPSVCSKRFLTTKVDrcvtglv 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 427 ---QQVGAntiikpgLQASVVRVegtnKAIAST---IDGEARYVFNDPYEG-------GKMVVAEAYRNLiaVGAKPLAM 493
Cdd:PLN03206 672 aqqQTVGP-------LQIPLADV----AVIAQThtgLTGGACAIGEQPIKGlvdpkamARLAVGEALTNL--VWAKVTAL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 494 TDCLNYGS--------PEKKHIYqqltDSTRGMAEACEALATPVVSGNVSLY------NETRTSsifPTPVVgMVGLIEN 559
Cdd:PLN03206 739 SDVKASGNwmyaakldGEGADMY----DAAVALRDAMIELGVAIDGGKDSLSmaaqagGEVVKA---PGNLV-ISAYVTC 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 560 IDFLKSYQPSI--GDT---LYV-IGETTDSYGGSQIEKlLYSDVNHEVEKVDLSQEAAKG-EAIRGAIREGVISHTQTVG 632
Cdd:PLN03206 811 PDITKTVTPDLklGDDgvlLHVdLGKGKRRLGGSALAQ-AYDQIGDDCPDLDDVAYLKKAfEATQDLIAKRLISAGHDIS 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 633 KGGIAVTLAKISAHYSLGIDAEVNLTNAQ----LFSETQGrYIVAVKAG------QTLNIEG--ATRIGTLTDTDDFKV- 699
Cdd:PLN03206 890 DGGLVVTLLEMAFAGNCGINVDLPSSGHSafetLFAEELG-LVLEVSRKnldavmEKLAAAGvtAEVIGQVTASPLIEVk 968
|
730
....*....|....*....
gi 505960966 700 VAQDSVIERRTSELKREWE 718
Cdd:PLN03206 969 VDGATCLSEKTASLRDMWE 987
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
452-690 |
4.02e-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: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 452 AIASTIDGEARYVFNDPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLNYGSPEKKHIyqqLTDSTRGMAEACEALATPVVS 531
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDI---LEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 532 GNVSLYneTRTSSIFPTPVVGMVGLIENIDFLKSYQPSIGDTLYVIGettdsyggsqiekllYSDVNHEVEKVDLsqeaa 611
Cdd:cd00396 78 GHTSVS--PGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG---------------VDAVLELVAAGDV----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 612 kgEAIrgairegvishtQTVGKGGIAVTLAKISAHYSLG--IDAE------------VNLTNAQLFSETQGRYIVAVKAG 677
Cdd:cd00396 136 --HAM------------HDITDGGLLGTLPELAQASGVGaeIDLEaipldevvrwlcVEHIEEALLFNSSGGLLIAVPAE 201
|
250 260
....*....|....*....|.
gi 505960966 678 Q------TLNIEG--ATRIGT 690
Cdd:cd00396 202 EadavllLLNGNGidAAVIGR 222
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
467-687 |
1.60e-10 |
|
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: 62.31 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 467 DPYEGGKMVVAEAYRNLIAVG--AKPLAMTDCL--NYGSPEKKHIyqqLTDSTRGMAEACEALATPVVSGNVSLYNETRT 542
Cdd:cd02193 17 DPAAGAATGVGGAIRDIAATGidAKPIALSANWmaSAGHPGEDAI---LYDAVKGVAELCNQLGLPIPVGKDRMSMKTRW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 543 SSIF--------PTPVVGMVGLIENIDFLKSYQPSIGDTLYVIGETT--DSYGGSQI--EKLLYSDVNH-EVEKVDLSQE 609
Cdd:cd02193 94 QEGNeqremthpPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKghNGLGGTALasVALSYRQLGDkSAQVRDPAQE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 610 AAKGEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSLGIDAEVNLTNAQ---------LFSETQGRYIVAVKAGQTL 680
Cdd:cd02193 174 KGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDepdmepleiALFESQERGVIQVRAEDRD 253
|
....*..
gi 505960966 681 NIEGATR 687
Cdd:cd02193 254 AVEEAQY 260
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
467-706 |
2.89e-09 |
|
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: 59.02 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 467 DPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLNYGSPEKKHIYQQLTDSTRGmaeaceaLATPVVSGnVSLYN-------- 538
Cdd:cd02203 42 EPFGGAATGVGGIIRDILSMGARPIALLDGLRFGDLDIPGYEPKGKLSPRR-------ILDGVVAG-ISDYGncigiptv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 539 --ETRTSSIF---PTPVVGMVGLIENIDFLKSYQPSIGDTLYVIGETT--DSYGG---------SQIEKLLYSDV---NH 599
Cdd:cd02203 114 ggEVRFDPSYygnPLVNVGCVGIVPKDHIVKSKAPGPGDLVVLVGGRTgrDGIGGatfsskelsENSSELDRPAVqvgDP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 600 EVEKVDLsqeaakgEAIRGAIREGVISHTQTVGKGGIAVTLAKISAHYSLGidAEVNLTNAQL-----------FSETQG 668
Cdd:cd02203 194 FMEKKLQ-------EAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLG--AEIDLDKVPLrepgmspweiwISESQE 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 505960966 669 RYIVAVKAGqtlNIE-----------GATRIGTLTDTDDFKVVAQDSVI 706
Cdd:cd02203 265 RMLLVVPPE---DLEeflaickkedlEAAVIGEVTDDGRLRLYYKGEVV 310
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
63-388 |
6.56e-09 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 58.16 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 63 FLKQFpttGEHVLMGpGEGAGVVDIGDnQAVVFKVESHnhpsAIEPYQGAATGVG-----GIIRDIVSIGARPINLLNSL 137
Cdd:COG0309 18 FLPAL---GNEVLVG-GEDAAVLDLGG-GRLAFTTDSF----VVSPIFFPGGDIGklavhGTVNDLAVSGAKPLYLSVSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 138 RfgeLTEKTNRRLLRGVVAGIGGYGNCIGIPTTAGEIEFDERYDGN-PLVNAMCVGVIDHD-MIQKGTAKgVGNSVIyVg 215
Cdd:COG0309 89 I---LEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDgPFINTTGIGVVPKGrLISPSGAR-PGDKII-V- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 216 lkTGRDGIHGAT-FAseelteesesKRPSVQIGDPFVGK-----KLMEATLEAItydeLVGIQDM-----GaaGLTSSSS 284
Cdd:COG0309 163 --TGGIGDHGTAiLA----------AREGLELEGELLSDaaplnDLVSVLLEAA----PGGVHAMrdptrG--GLAGALN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 285 EMAAKGGSGIHLELEKVPVREK--------GISPYEMMlSETqeRMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNR 356
Cdd:COG0309 225 EIAEASGVGIEIDEDAIPVRPEvrgicellGLDPLYLA-NEG--KLVAVVPPEDAEAVLEALRAHGIDAAIIGEVTEGPP 301
|
330 340 350
....*....|....*....|....*....|..
gi 505960966 357 FVLTYEGEVFADIPVEPladeapvyiLEGEPL 388
Cdd:COG0309 302 GRVVLKTAIGGERILDP---------PEGDPL 324
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
571-700 |
2.58e-06 |
|
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: 47.73 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 571 GDTLYVIGE-TTDSYGGSQIEKLLYSDVNHEVEKVDLSQEAAKGEAIRGAIREGV----ISHtqtVGKGGIAVTLAKISA 645
Cdd:pfam02769 3 GDVLILLGSsGLHGAGLSLSRKGLEDSGLAAVQLGDPLLEPTLIYVKLLLAALGGlvkaMHD---ITGGGLAGALAEMAP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505960966 646 HYSLG---------IDAEVNLTNAQLFSETQGRYIVAVKAGQ------TLNIEG--ATRIGTLTDTDDFKVV 700
Cdd:pfam02769 80 ASGVGaeidldkvpIFEELMLPLEMLLSENQGRGLVVVAPEEaeavlaILEKEGleAAVIGEVTAGGRLTVI 151
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
63-351 |
6.47e-05 |
|
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100037 [Multi-domain] Cd Length: 298 Bit Score: 45.67 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 63 FLKQFPTTGEHVLMGPGEG--AGVVDIGDNQAVVfkveshnhpsAIEPYQGAATGVG--GIIR---DIVSIGARPINLLN 135
Cdd:cd06061 14 ILKNLGADRDEVLVGPGGGedAAVVDFGGKVLVV----------STDPITGAGKDAGwlAVHIaanDIATSGARPRWLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 136 SLRfgeLTEKTNRRLLRGVVAGIGGYGNCIGIPTTAGEIEfdeRYDG--NPLVNAMCVGVIDHDMIQKGTAKGVGNSVIY 213
Cdd:cd06061 84 TLL---LPPGTDEEELKAIMREINEAAKELGVSIVGGHTE---VTPGvtRPIISVTAIGKGEKDKLVTPSGAKPGDDIVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 214 vglkTGRDGIHGAtfaseelteeseskrpsVQIGDPF---VGKKLMEATLEAIT--YDELVGIQDMGAA----------- 277
Cdd:cd06061 158 ----TKGAGIEGT-----------------AILANDFeeeLKKRLSEEELREAAklFYKISVVKEALIAaeagvtamhda 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 278 ---GLTSSSSEMAAKGGSGIHLELEKVPVREK--------GISPYEMMLSETqerMLLVVKKGTEQKFLDLFDYHELDSA 346
Cdd:cd06061 217 tegGILGALWEVAEASGVGLRIEKDKIPIRQEtkeicealGIDPLRLISSGT---LLITVPPEKGDELVDALEEAGIPAS 293
|
....*
gi 505960966 347 VIGEV 351
Cdd:cd06061 294 VIGKI 298
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
409-536 |
2.23e-04 |
|
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: 43.74 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 409 LLTHPTIASKH-------YLYDQYDQQVGAntIIKPGLQASVVRVEGTNKAIAstIDG-EARYVFNDPYEGGKMVVAEAY 480
Cdd:cd02192 1 LRAFEGVTRKRdiqdvvaILPDAPFDSLGV--AADLGDDAAAIPDGDGYLLLA--ADGiWPSLVEADPWWAGYCSVLVNV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 505960966 481 RNLIAVGAKPLAMTDCLNYGSPEkkhIYQQLTdstRGMAEACEALATPVVSGNVSL 536
Cdd:cd02192 77 SDIAAMGGRPLAMVDALWSPSAE---AAAQVL---EGMRDAAEKFGVPIVGGHTHP 126
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
291-374 |
4.30e-04 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 43.23 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 291 GSGIHLELEKVPvREKGISPYEMMLSETQERMLLVVKKGTEQKFLDLFDYHELDSAVIGEVTDTNRFVLTYEGE--VFAD 368
Cdd:COG2144 231 GVGATIDLDAIP-RPEGVDLERWLKAFPSFGFLLTVPPENVDEVLARFAARGITAAVIGEVTDSRRLTLRDGGEraTFFD 309
|
....*.
gi 505960966 369 IPVEPL 374
Cdd:COG2144 310 FSKEPL 315
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
254-351 |
4.56e-04 |
|
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100033 [Multi-domain] Cd Length: 293 Bit Score: 42.82 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 254 KLMEATLEAitYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLELEKVPVREK--------GISPYEMMlSETqeRMLLV 325
Cdd:cd02197 191 GLVEALLEA--GPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEAIPVREEvrgacemlGLDPLYLA-NEG--KFVAI 265
|
90 100
....*....|....*....|....*...
gi 505960966 326 VKKGTEQKFLDLFDYHEL--DSAVIGEV 351
Cdd:cd02197 266 VPPEDAEEVLEALRSHPLgkEAAIIGEV 293
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
467-706 |
2.14e-03 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 41.38 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 467 DPYEGGKMVVAEAYRNLIAVGAKPLAMTDCLnygspekkHIYQQLTDSTRGMAEACEALATPVVSGnvslynETRTSSIF 546
Cdd:PRK14090 77 EPYNGAATGVGGIIRDVLAMGARPTAIFDSL--------HMSRIIDGIIEGIADYGNSIGVPTVGG------ELRISSLY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 547 ---PTPVVGMVGLIENIDFLKSYQPSIGDTLYVIGETTDS---YGGSQIEKLLYSD--VNHEVEKVDLSQEAAKGEAIRG 618
Cdd:PRK14090 143 ahnPLVNVLAAGVVRNDMLVDSKASRPGQVIVIFGGATGRdgiHGASFASEDLTGEkaTKLSIQVGDPFAEKMLIEAFLE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 619 AIREGVISHTQTVGKGGIAVTLAKISAHYSLGidAEVNLTNAQ-----------LFSETQGRYIVAV---KAGQTLNIE- 683
Cdd:PRK14090 223 MVEEGLVEGAQDLGAGGVLSATSELVAKGGLG--AIVHLDRVPlrepdmepweiLISESQERMAVVTspeKASRILEIAk 300
|
250 260
....*....|....*....|....*...
gi 505960966 684 -----GATrIGTLTDTDDFKVVAQDSVI 706
Cdd:PRK14090 301 khllfGDI-VAEVIDDPIYRVMYRDDLV 327
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
399-532 |
2.84e-03 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 40.53 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 399 DIDVNDVFDRLLTHPTIASKHYLYD---QYDQQVGANTIIKPGLQASVVRVEGTNKAIAstIDG-EARYVFNDPYEGGK- 473
Cdd:COG2144 1 MMDLAALAAELRNFPGVTRKRDIADvvrALGLASSGGTAAAFGDDAAAIPDGDGYLLLA--AEGiWPKFVEADPWFAGYc 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505960966 474 --MVvaeayrNL--I-AVGAKPLAMTDCLNYGSPEkkhIYQQLTdstRGMAEACEALATPVVSG 532
Cdd:COG2144 79 svLV------NVsdIaAMGGRPLAVVDALWSSDEE---AAAPVL---AGMRAASRKFGVPIVGG 130
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
253-365 |
2.99e-03 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 41.16 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960966 253 KKLMEATLEAITYDELVGIQDMGAAGLTSSSSEMAAKGGSGIHLElekVPVrekGISPYEMMLSETQERMLLVVKKGTE- 331
Cdd:PHA03366 854 KNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALAGGRGVTIT---VPA---GEDPLQFLFSETPGVVIEVPPSHLSa 927
|
90 100 110
....*....|....*....|....*....|....*...
gi 505960966 332 -QKFLDLFDyheLDSAVIGEV---TDTNRFVLTYEGEV 365
Cdd:PHA03366 928 vLTRLRSRN---IICYPIGTVgpsGPSNTFSVSHNGTV 962
|
|
| |
