|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
11-739 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 1323.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 11 QIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDN 90
Cdd:PRK01213 1 TPDTEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGENAGVVDIGDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 91 QAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTV 170
Cdd:PRK01213 81 QAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 171 GGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRPAVQVGDPF 250
Cdd:PRK01213 161 GGEVYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGASFASAELSEESEEKRPAVQVGDPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 251 MEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGR 330
Cdd:PRK01213 241 MEKLLIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 331 EQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKGEKVAEVPADALAEEAPIYHKPSKEAAYFAEFQAMKmetpkvENYKET 410
Cdd:PRK01213 321 EEEVLAIFEKWDLDAAVIGEVTDDGRLRVYHHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQADP------EDLKEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 411 LFALLQQPTIASKEWVYDQYDYQVRTSTVVTPGSDAAVVRVRGTEKGLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVC 490
Cdd:PRK01213 395 LLKLLSSPNIASKEWVYEQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 491 SGGEPLAITDCLNFGNPEKPEIFWQIEKSVDGMSEACRTLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTT 570
Cdd:PRK01213 475 VGATPLAITDCLNFGNPEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 571 QEFKQAGDLVYVIGETKAEFGGSELQKMIHGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAISESA 650
Cdd:PRK01213 555 SGFKKEGDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMA 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 651 IgANGLGATVKLDGE--ATAALFAESQSRFVITVKRENKEAFEKV-----VEAIQVGEVTNtNEVTIHNEENEVLltanv 723
Cdd:PRK01213 635 I-AGGLGAEVDLSDGlrPDALLFSESQGRYVVSVPPENEEAFEALaeaagVPATRIGVVGG-DALKVKGNDTESL----- 707
|
730
....*....|....*.
gi 1121125123 724 DEMRKAWKGAIPCLLK 739
Cdd:PRK01213 708 EELREAWEGALPRLLG 723
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
5-739 |
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: 1179.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 5 LEPNPTQIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGI 84
Cdd:COG0046 6 LEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPTEGPRVLSGPGDNAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 85 VDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSP--RVKYLFEEVVAGIAGYG 162
Cdd:COG0046 86 VDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAGIADYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 163 NCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRP 242
Cdd:COG0046 166 NCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSELDRP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 243 AVQVGDPFMEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERM 322
Cdd:COG0046 246 AVQVGDPFMEKRLIEAILELGDTGLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 323 LIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKGEKVAEVPADALAEEAPIYHKPSKEAAYFAEFqamkmETP 402
Cdd:COG0046 326 LLVVKPEKLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPL-----DLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 403 KVENYKETLFALLQQPTIASKEWVYDQYDYQVRTSTVVTPG-SDAAVVRVRGTEKGLAMTTDCNSRYIYLDPEVGGKIAV 481
Cdd:COG0046 401 EPIDLEEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDPGvADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 482 AEAARNIVCSGGEPLAITDCLNFGNPEKPEIFWQIEKSVDGMSEACRTLQTPVIGGNVSMYNERSGE--AVYPTPTVGMV 559
Cdd:COG0046 481 AEAARNLAAVGAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKDGkvAIPPTPVIGAV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 560 GLVHDLKHVTTQEFKQAGDLVYVIGETKAEFGGSELQKMIhGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAE 639
Cdd:COG0046 561 GLVDDVRKTVTPDLKKEGDLLYLIGETKNELGGSEYAQVL-GQLGGEPPDVDLEAEKALFEAVQELIREGLILAAHDVSD 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 640 GGLAVAISESAIgANGLGATVKLDG----EATAALFAESQSRFVITVKRENKEAFEKV-----VEAIQVGEVTNTNEVTI 710
Cdd:COG0046 640 GGLAVALAEMAF-AGGLGADIDLDAlgdlRPDAALFSESQGRAVVQVAPEDAEAVEALlaeagLPAHVIGTVTGDDRLVI 718
|
730 740
....*....|....*....|....*....
gi 1121125123 711 HNeENEVLLTANVDEMRKAWKGAIPCLLK 739
Cdd:COG0046 719 RR-GGETLLSLSLAELRDAWEETLPRLRD 746
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
23-738 |
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: 1088.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 23 LTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDNQAVVFKMESHNH 102
Cdd:TIGR01736 1 LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYAVVFKMESHNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 103 PSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEG 182
Cdd:TIGR01736 81 PSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 183 NPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEE-LSESSEAKRPAVQVGDPFMEKLLIEACLE 261
Cdd:TIGR01736 161 NPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEElSEEAEEEDRPAVQVGDPFTEKLLIEATLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 262 LIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKY 341
Cdd:TIGR01736 241 AVDTGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 342 GLAAVTMGKVTEDKMLRLFHKGEKVAEVPADALAeEAPIYHKPSKEAAYFAEFQamkmETPKVENYKETLFALLQQPTIA 421
Cdd:TIGR01736 321 ELPASVIGEVTDEGRIRLYYKGEVVADLPIELLA-DAPEYERPSEPPKYPEEEK----EPEPPADLEDAFLKVLSSPNIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 422 SKEWVYDQYDYQVRTSTVVTPGSDAAVVRVRGTEK-GLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITD 500
Cdd:TIGR01736 396 SKEWVYRQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 501 CLNFGNPEKPEIFWQIEKSVDGMSEACRTLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLV 580
Cdd:TIGR01736 476 CLNFGNPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGDAI 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 581 YVIGETKAEFGGSELQKMIHGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAISESAIgANGLGATV 660
Cdd:TIGR01736 556 YLIGETKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAA-ASGIGAEV 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 661 KLDGEATA----ALFAESQSRFVITVKRENKE--AFEKVVEAIQVGEVTNTNeVTIhnEENEVLLTANVDEMRKAWKGAI 734
Cdd:TIGR01736 635 DIDEIASArpdeLLFSESNGRAIVAVPEEKAEeaVKSKGVPAKVIGKTGGDR-LTI--KTGDDTISVSVKELRDAWEEAL 711
|
....
gi 1121125123 735 PCLL 738
Cdd:TIGR01736 712 PEYM 715
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
43-369 |
1.09e-175 |
|
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: 505.08 E-value: 1.09e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 43 ETGLFSVMWSEHCSYKNSKPVLRKFpttgervlqgpgegagivdigdnQAVVFKMESHNHPSAIEPYQGAATGVGGIIRD 122
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLLKMI-----------------------WAVVFKVETHNHPSAIEPFGGAATGVGGIIRD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 123 VFSMGARPVALLNSLRFGELQSP--------RVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLI 194
Cdd:cd02203 58 ILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 195 NHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFA-SEELSESSEAKRPAVQVGDPFMEKLLIEACLELIQSDALVGIQD 273
Cdd:cd02203 138 PKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSsKELSENSSELDRPAVQVGDPFMEKKLQEAILEARETGLIVGIQD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 274 MGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTE 353
Cdd:cd02203 218 LGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTD 297
|
330
....*....|....*.
gi 1121125123 354 DKMLRLFHKGEKVAEV 369
Cdd:cd02203 298 DGRLRLYYKGEVVADL 313
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
30-584 |
4.23e-137 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 416.95 E-value: 4.23e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 30 MVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGErvlqgpGEGAGIVDIGDNQAVVFKMESHNHPSAIEPY 109
Cdd:PRK14090 6 ILEEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGF------EGNAGVVNLDDYYSIAFKIESHNHPSAIEPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 110 QGAATGVGGIIRDVFSMGARPVALLNSLRFGELqsprvkylFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAM 189
Cdd:PRK14090 80 NGAATGVGGIIRDVLAMGARPTAIFDSLHMSRI--------IDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 190 CVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSeAKRPAVQVGDPFMEKLLIEACLELIQSDALV 269
Cdd:PRK14090 152 AAGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGEK-ATKLSIQVGDPFAEKMLIEAFLEMVEEGLVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 270 GIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMG 349
Cdd:PRK14090 231 GAQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 350 KVTEDKMLRLFHKGEKVAEVPADALAeEAPiyhkpsKEAAYfaEFQAMKMetPKvenYKETLFallqQPTIASKewVYDQ 429
Cdd:PRK14090 311 EVIDDPIYRVMYRDDLVMEVPVQLLA-NAP------EEEIV--EYTPGEI--PE---FKRVEF----EEVNARE--VFEQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 430 YDYQVRTSTVVTPGSDAAVVRVRGTEkGLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEK 509
Cdd:PRK14090 371 YDHMVGTDTVLPPGFGAAVMRIKRDG-GYSLVTHSRADLALQDTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGDPDV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1121125123 510 PEIfwQIEKSVDGMSEACRTLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKqagdlVYVIG 584
Cdd:PRK14090 450 DPV--GLSAMMTALKDACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLGKVNPQKVAKPKPSK-----VFAVG 517
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
445-702 |
1.25e-116 |
|
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: 351.84 E-value: 1.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 445 DAAVVRVRG-TEKGLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEKPE-IFWQIEKSVDG 522
Cdd:cd02204 1 DAAVLRIPGeTDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEgEMGQLVEAVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 523 MSEACRTLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLVYVIGETKAEFGGSELQKMIHGK 602
Cdd:cd02204 81 LGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDLLYLIGETKDELGGSEYALAYHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 603 IFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAISESAIgANGLGATVKLD--GEATAALFAESQSRFVI 680
Cdd:cd02204 161 GGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAF-AGGLGAEVDLSkdDAEDELLFSESLGRVLV 239
|
250 260
....*....|....*....|....*
gi 1121125123 681 TVKRENKEAFE---KVVEAIQVGEV 702
Cdd:cd02204 240 EVKPENEEVFEaeeAGVPATVIGTV 264
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
93-327 |
7.49e-52 |
|
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: 181.34 E-value: 7.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 93 VVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMG--ARPVALLNSLRFGELQsPRVKYLFEEVVAGIAGYGNCIGIPTV 170
Cdd:cd02193 3 EAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGidAKPIALSANWMASAGH-PGEDAILYDAVKGVAELCNQLGLPIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 171 GGEVQFDPCYEG-----------NPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEA 239
Cdd:cd02193 82 VGKDRMSMKTRWqegneqremthPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNGLGGTALASVALSYRQLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 240 KRPaVQVGDPFMEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQ 319
Cdd:cd02193 162 DKS-AQVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIALFESQ 240
|
....*...
gi 1121125123 320 ERMLIVVK 327
Cdd:cd02193 241 ERGVIQVR 248
|
|
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
96-730 |
1.02e-37 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 151.88 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 96 KMESHNHPSAIEPYQGAATGVGGIIRDVFS--MGARPVALLNSLRFGELQSPRVKYLFEEVVA----------------- 156
Cdd:PRK05297 288 KVETHNHPTAISPFPGAATGSGGEIRDEGAtgRGSKPKAGLTGFSVSNLRIPGFEQPWEEDYGkperiasaldimiegpl 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 157 GIAGYGNCIGIPTVGG-----EVQFDpcyEGNPLVNA-----MC---VGLINHEDIKKGQ-AHGA-----GNTVMYVG-- 215
Cdd:PRK05297 368 GGAAFNNEFGRPNLLGyfrtfEQKVN---SHNEEVRGyhkpiMLaggIGNIRADHVQKGEiPVGAklivlGGPAMRIGlg 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 216 ---AS---TGR-----DgihgatFAseelsesseakrpAVQVGDPFMEKL---LIEACLELIQSDALVGIQDMGAAGLTS 281
Cdd:PRK05297 445 ggaASsmaSGQssedlD------FA-------------SVQRGNPEMERRcqeVIDRCWQLGDDNPILSIHDVGAGGLSN 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 282 SSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKkgreQEIVDLF------EKYGLAAVtmGKVTEDK 355
Cdd:PRK05297 506 AFPELVNDGGRGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIA----PEDLELFeaicerERCPFAVV--GEATEER 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 356 MLRLF--HKGEKVAEVPADALAEEAPIYHKPSKEAAyfAEFQAMKMETPKVenyKETLFALLQQPTIASKEW-------- 425
Cdd:PRK05297 580 HLTLEdsHFDNKPVDLPLDVLLGKPPKMHRDVKTVK--AKGPALDYSGIDL---AEAVERVLRLPTVASKSFlitigdrs 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 426 -----VYDQY--DYQVrtstvvtPGSDAAVVRV--RGTEkGLAMTtdcnsryI-------YLDPEVGGKIAVAEAARNIV 489
Cdd:PRK05297 655 vtglvARDQMvgPWQV-------PVADCAVTAAsyDGYA-GEAMA-------MgertpvaLLDAAASARMAVGEALTNIA 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 490 CSggePLA-ITD----------ClnfGNPEKPEIFWQIEKSVdGMsEACRTLQTPVIGGNVSM-----YNErSGEAVYPT 553
Cdd:PRK05297 720 AA---PIGdLKRiklsanwmaaA---GHPGEDARLYDAVKAV-GM-ELCPALGITIPVGKDSLsmktkWQE-GGEDKEVT 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 554 PTVGMV----GLVHDLKHVTTQEFKQAGD--LVYV-IGETKAEFGGSEL-QkmIHGKIFGQSPSIDlDVE-LKRqkqVLA 624
Cdd:PRK05297 791 SPLSLIisafAPVEDVRKTLTPQLRTDKDtaLLLIdLGRGKNRLGGSALaQ--VYNQLGDKAPDVD-DAEdLKG---FFN 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 625 AIQA----GLVQSAHDVAEGGLAVAISESAIgANGLGATVKLD---GEATAALFAEsQSRFVITVKRENKEAFEKVVEA- 696
Cdd:PRK05297 865 AIQAlvaeGLLLAYHDRSDGGLLTTLAEMAF-AGHCGLDIDLDalgDDALAALFNE-ELGAVIQVRAADRDAVEAILAEh 942
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1121125123 697 ------IQVGEVTNTNEVTIHNeENEVLLTANVDEMRKAW 730
Cdd:PRK05297 943 glsdcvHVIGKPNAGDRIVITR-NGKTVFSESRTELRRWW 981
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
206-361 |
3.43e-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: 130.54 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 206 GAGNTVMYVGAstgrDGIHGATFASEELSESSeAKRPAVQVGDPFMEKLLIEACLELIQSDALV-GIQDMGAAGLTSSSA 284
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLED-SGLAAVQLGDPLLEPTLIYVKLLLAALGGLVkAMHDITGGGLAGALA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1121125123 285 EMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFH 361
Cdd:pfam02769 76 EMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
89-194 |
1.30e-33 |
|
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: 124.48 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 89 DNQAVVFKMESHNHPSAIEPYQG-AATGVGGIIRDVFSMGARPVALLNSLRFGElqSPRVKYLFEEVVAGIAGYGNCIGI 167
Cdd:pfam00586 1 DDAAVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLALPG--GPEVEWVLEEIVEGIAEACREAGV 78
|
90 100
....*....|....*....|....*..
gi 1121125123 168 PTVGGEVQFDPCYeGNPLVNAMCVGLI 194
Cdd:pfam00586 79 PLVGGDTSFDPEG-GKPTISVTAVGIV 104
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
457-562 |
5.12e-31 |
|
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: 116.78 E-value: 5.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 457 GLAMTTDCNSRYIYLDPEVG-GKIAVAEAARNIVCSGGEPLAITDCLNFgnPEKPEIFWQIEKSVDGMSEACRTLQTPVI 535
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLAL--PGGPEVEWVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....*..
gi 1121125123 536 GGNVSMYNERsgeaVYPTPTVGMVGLV 562
Cdd:pfam00586 82 GGDTSFDPEG----GKPTISVTAVGIV 104
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
92-350 |
2.90e-30 |
|
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: 119.04 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 92 AVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSprVKYLfEEVVAGIAGYGNCIGIPTVG 171
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLE--VDIL-EDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 172 GEVQFDPCYEG-NPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGastgrdgihgatfaseelsesseakrpavqvgdpf 250
Cdd:cd00396 78 GHTSVSPGTMGhKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG----------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 251 mekllIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGM-----TPYEMMLSESQERMLIV 325
Cdd:cd00396 123 -----VDAVLELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRwlcveHIEEALLFNSSGGLLIA 197
|
250 260
....*....|....*....|....*
gi 1121125123 326 VKKGREQEIVDLFEKYGLAAVTMGK 350
Cdd:cd00396 198 VPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
57-730 |
3.23e-26 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 115.64 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 57 YKNSKPVLRKFPTTGERVLQgPGEGAGIVDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFS--MGARPVALL 134
Cdd:PLN03206 253 FKDNSSAIRGFVVQPLRPVS-PGSPSPLAPVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHAtgRGSFVVAGT 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 135 NSLRFGELQ---------SPRVKY-------LFEEVVA--GIAGYGNCIGIPTVGGEV----QFDPCYEG----NPLVNA 188
Cdd:PLN03206 332 AGYCVGNLRiegsyapweDSSFVYpsnlaspLQILIDAsnGASDYGNKFGEPLIQGYTrtfgMRLPNGERrewlKPIMFS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 189 MCVGLINHEDIKKGQAHgAGNTVMYVGASTGRDGIHGATfASEELSESSEAKRP--AVQVGDPFME-KL--LIEACLELI 263
Cdd:PLN03206 412 GGIGQIDHTHLTKGEPD-IGMLVVKIGGPAYRIGMGGGA-ASSMVSGQNDAELDfnAVQRGDAEMSqKLyrVVRACVEMG 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 264 QSDALVGIQDMGAAGLTSSSAEMASKAGMGI---EMYLDDvpqrETgMTPYEMMLSESQERMLIVVKKGRE---QEIVDL 337
Cdd:PLN03206 490 EDNPIVSIHDQGAGGNCNVVKEIIYPKGAEIdirAVVVGD----HT-LSVLEIWGAEYQEQDALLIKPESRdllQSICDR 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 338 fEKYGLAAVTM----GKVT--EDKMLRLFHKGEKVAEVPADALAEEAPIYHKPSKEAAY-FAEFQAMKMETPKVENYKET 410
Cdd:PLN03206 565 -ERCSMAVIGTidgsGRVVlvDSAAPEKCEANGLPPPPPAVDLDLEKVLGDMPQKTFEFkRVANKLEPLDIPPGITVMDA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 411 LFALLQQPTIASKEWVYDQYDYQVrTSTVVT---------PGSDAAVVRVRGTE-KGLAmtTDCNSRYI--YLDPEVGGK 478
Cdd:PLN03206 644 LKRVLRLPSVCSKRFLTTKVDRCV-TGLVAQqqtvgplqiPLADVAVIAQTHTGlTGGA--CAIGEQPIkgLVDPKAMAR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 479 IAVAEAARNIVCSggEPLAITDCLNFGNpekpeifWQIEKSVDG----MSEACRTLQTPVI-------GG--NVSMYNER 545
Cdd:PLN03206 721 LAVGEALTNLVWA--KVTALSDVKASGN-------WMYAAKLDGegadMYDAAVALRDAMIelgvaidGGkdSLSMAAQA 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 546 SGEAVYPTPTVGMVGLVH--DLKHVTTQEFKQAGD--LVYV-IGETKAEFGGSELQKmIHGKIFGQSPSIDLDVELKRQ- 619
Cdd:PLN03206 792 GGEVVKAPGNLVISAYVTcpDITKTVTPDLKLGDDgvLLHVdLGKGKRRLGGSALAQ-AYDQIGDDCPDLDDVAYLKKAf 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 620 KQVLAAIQAGLVQSAHDVAEGGLAVAISESAIGAN-GLGATVKLDGE-ATAALFAESQSrFVITVKREN----KEAFEKV 693
Cdd:PLN03206 871 EATQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNcGINVDLPSSGHsAFETLFAEELG-LVLEVSRKNldavMEKLAAA 949
|
730 740 750
....*....|....*....|....*....|....*...
gi 1121125123 694 -VEAIQVGEVTNTNEVTIHNEENEVlLTANVDEMRKAW 730
Cdd:PLN03206 950 gVTAEVIGQVTASPLIEVKVDGATC-LSEKTASLRDMW 986
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
475-717 |
6.06e-21 |
|
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: 94.08 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 475 VGGKIavaeaaRNIVCSGGEPLAITDCLNFGNPEKPEIFWQIEKSVdgmseacRTLQTPVIGGnVSMYNERSGEAV---- 550
Cdd:cd02203 51 VGGII------RDILSMGARPIALLDGLRFGDLDIPGYEPKGKLSP-------RRILDGVVAG-ISDYGNCIGIPTvgge 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 551 ---------YPTPTVGMVGLVhDLKHVTTQEFKQAGDLVYVIGETKAEFGgselqkmIHGKIFGQSPSIDLDVELKR--- 618
Cdd:cd02203 117 vrfdpsyygNPLVNVGCVGIV-PKDHIVKSKAPGPGDLVVLVGGRTGRDG-------IGGATFSSKELSENSSELDRpav 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 619 -----------QKQVLAAIQAGLVQSAHDVAEGGLAVAISESAiGANGLGATVKLD----GEATAA----LFAESQSRFV 679
Cdd:cd02203 189 qvgdpfmekklQEAILEARETGLIVGIQDLGAGGLSSAVSEMA-AKGGLGAEIDLDkvplREPGMSpweiWISESQERML 267
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1121125123 680 ITVKRENKEAFEKV-----VEAIQVGEVTNTNEVTIHNEENEV 717
Cdd:cd02203 268 LVVPPEDLEEFLAIckkedLEAAVIGEVTDDGRLRLYYKGEVV 310
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
12-58 |
1.66e-19 |
|
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: 82.13 E-value: 1.66e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1121125123 12 IKEERIYAEMGLTDEEFAMVEKI---LGRLPNYTETGLFSVMWSEHCSYK 58
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYfagLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
457-691 |
3.52e-18 |
|
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: 83.98 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 457 GLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEKPEIfwqIEKSVDGMSEACRTLQTPVIG 536
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDI---LEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 537 GNVSMYNERSGEavYPTPTVGMVGLVHDLKHVTTQEfKQAGDLVYVIGetkaefggselqkmihgkifgqspsidldvel 616
Cdd:cd00396 78 GHTSVSPGTMGH--KLSLAVFAIGVVEKDRVIDSSG-ARPGDVLILTG-------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 617 krQKQVLAAIQAGLVQSAHDVAEGGLAVAISESAiGANGLGATVKLD-------------GEATAALFAESQSRFVITVK 683
Cdd:cd00396 123 --VDAVLELVAAGDVHAMHDITDGGLLGTLPELA-QASGVGAEIDLEaipldevvrwlcvEHIEEALLFNSSGGLLIAVP 199
|
....*...
gi 1121125123 684 RENKEAFE 691
Cdd:cd00396 200 AEEADAVL 207
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
575-710 |
6.33e-16 |
|
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: 75.46 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 575 QAGDLVYVIGEtkAEFGGSEL---QKMIHGKIFGQSPSIDLDVELKRQKQVLAAIQA-GLVQSAHDVAEGGLAVAISESA 650
Cdd:pfam02769 1 KPGDVLILLGS--SGLHGAGLslsRKGLEDSGLAAVQLGDPLLEPTLIYVKLLLAALgGLVKAMHDITGGGLAGALAEMA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121125123 651 IgANGLGATVKLD--------GEATAALFAESQSRFVITVKRENKEAFEKV-----VEAIQVGEVTNTNEVTI 710
Cdd:pfam02769 79 P-ASGVGAEIDLDkvpifeelMLPLEMLLSENQGRGLVVVAPEEAEAVLAIlekegLEAAVIGEVTAGGRLTV 150
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
104-351 |
2.29e-14 |
|
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: 73.72 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 104 SAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKY-LFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEG 182
Cdd:cd02204 26 SLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEGEMgQLVEAVLGLGDACRALGTPVIGGKDSLYNETEG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 183 ---NPLVNAMCVGLInhEDIKK---GQAHGAGNTVMYVGASTGRDGIHGATFASEELSESseakrpAVQVGDPFMEKLLI 256
Cdd:cd02204 106 vaiPPTLVIGAVGVV--DDVRKivtLDFKKEGDLLYLIGETKDELGGSEYALAYHGLGGG------APPLVDLEREKALF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 257 EACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPqretgmTPYEMMLSESQERMLIVVKKgrEQEIVD 336
Cdd:cd02204 178 DAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDD------AEDELLFSESLGRVLVEVKP--ENEEVF 249
|
250
....*....|....*
gi 1121125123 337 LFEKYGLAAVTMGKV 351
Cdd:cd02204 250 EAEEAGVPATVIGTV 264
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
457-693 |
2.21e-13 |
|
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: 71.17 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 457 GLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSG--GEPLAITDCLNFGNPeKPEIFWQIEKSVDGMSEACRTLQTPV 534
Cdd:cd02193 2 GEAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGidAKPIALSANWMASAG-HPGEDAILYDAVKGVAELCNQLGLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 535 IGGNVSMY--------NERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLVYVIGET--KAEFGGSELQKMIHGKIF 604
Cdd:cd02193 81 PVGKDRMSmktrwqegNEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKghNGLGGTALASVALSYRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 605 GQSPSIDLDVELKR--QKQVLAAIQAGLVQSAHDVAEGGLAVAISESAiGANGLGATVKL--------DGEATAALFAES 674
Cdd:cd02193 161 GDKSAQVRDPAQEKgfYEAMQALVAAGKLLAWHDRGAGGLLVALAELV-FAGHCGVQVDLaalgddepDMEPLEIALFES 239
|
250
....*....|....*....
gi 1121125123 675 QSRFVITVKRENKEAFEKV 693
Cdd:cd02193 240 QERGVIQVRAEDRDAVEEA 258
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
435-663 |
6.50e-12 |
|
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: 66.85 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 435 RTSTVVTPGSDAAVVRVRGTEKGLAMTTDCnsryIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNF--GNPEKpei 512
Cdd:cd06061 22 RDEVLVGPGGGEDAAVVDFGGKVLVVSTDP----ITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLppGTDEE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 513 fwQIEKSVDGMSEACRTLQTPVIGGNVsmynERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKqAGDLVYV-----IGETK 587
Cdd:cd06061 95 --ELKAIMREINEAAKELGVSIVGGHT----EVTPGVTRPIISVTAIGKGEKDKLVTPSGAK-PGDDIVMtkgagIEGTA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1121125123 588 --AEFGGSELQKMIHGKIFGQSPSIDLDVELkrQKQVLAAIQAGlVQSAHDVAEGGLAVAISESAIgANGLGATVKLD 663
Cdd:cd06061 168 ilANDFEEELKKRLSEEELREAAKLFYKISV--VKEALIAAEAG-VTAMHDATEGGILGALWEVAE-ASGVGLRIEKD 241
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
439-707 |
4.56e-11 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 64.71 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 439 VVTPGSDAAVVRVRGTEkgLAMTTDCNSryiyLDPEVG-----GKIAVAEAARNIVCSGGEPLAITDCLNFgnPE--KPE 511
Cdd:COG0309 26 VLVGGEDAAVLDLGGGR--LAFTTDSFV----VSPIFFpggdiGKLAVHGTVNDLAVSGAKPLYLSVSLIL--EEgfPLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 512 IFWQIeksVDGMSEACRTLQTPVIGGNVSMYnERsGEAVYPTPTVGMVGLVHDLKHVTTQEFKqAGDLVYV---IGetka 588
Cdd:COG0309 98 DLERI---VESMAEAAREAGVSIVTGDTKVV-ER-GGVDGPFINTTGIGVVPKGRLISPSGAR-PGDKIIVtggIG---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 589 efggselqkmIHG-KIFGQSPSIDLDVELKRQ-----KQVLAAIQAGL--VQSAHDVAEGGLAVAISESAiGANGLGATV 660
Cdd:COG0309 168 ----------DHGtAILAAREGLELEGELLSDaaplnDLVSVLLEAAPggVHAMRDPTRGGLAGALNEIA-EASGVGIEI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1121125123 661 KLD----GEATAA---------LFAESQSRFVITVKRENKEAfekVVEAIQ--------VGEVTNTNE 707
Cdd:COG0309 237 DEDaipvRPEVRGicellgldpLYLANEGKLVAVVPPEDAEA---VLEALRahgidaaiIGEVTEGPP 301
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
471-730 |
9.91e-11 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 65.43 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 471 LDPEVGGKIAVAEAARNIVCSGG---EPLAITdcLNFGNPEKPEIFWQIEKSVDGMSEACRTLqtpviggNVS-MYNERS 546
Cdd:PHA03366 704 LDPILGAKYAIVEALTNLMLAPVanlEDITIT--LSVTWPPTDQAASELYRALAACKEFCREL-------GVNfTFTSAS 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 547 GEAVYPTPTVGMVGL----------VHDLKHVTTQEFKQAGD-LVYVIGETKAEFGGSELQKmihgkIFGQSPSIDLDVE 615
Cdd:PHA03366 775 SSPRQDQPPQPGPLFntivftasapVPSSTPRLTPDLKKPGSaLVHLSISPEYTLAGSVFEQ-----IFGLKSGTLPDIS 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 616 LKRQKQVLAAIQA----GLVQSAHDVAEGGLAVAISESAIgANGLGATVKL-DGEATAA-LFAESQSrFVITVKREN--- 686
Cdd:PHA03366 850 PSYLKNLFRAVQHliseGLVVSGHDVSDGGLIACLAEMAL-AGGRGVTITVpAGEDPLQfLFSETPG-VVIEVPPSHlsa 927
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1121125123 687 --KEAFEKVVEAIQVGEVTN---TNEVTI-HNeeNEVLLTANVDEMRKAW 730
Cdd:PHA03366 928 vlTRLRSRNIICYPIGTVGPsgpSNTFSVsHN--GTVLFRESLSSLRSTW 975
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
437-703 |
1.77e-08 |
|
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).
Pssm-ID: 100030 [Multi-domain] Cd Length: 291 Bit Score: 56.41 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 437 STVVTPGSDAAVVRVRGteKGLAMTTDC-------NSRYiylDPE-VGGKiAVAEAARNIVCSGGEPLAITdcLNFGNPE 508
Cdd:cd02194 18 GVLLGIGDDAAVLKPPG--GRLVVTTDTlvegvhfPPDT---TPEdIGWK-ALAVNLSDLAAMGARPLGFL--LSLGLPP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 509 KPEIFWqIEKSVDGMSEACRTLQTPVIGGNVSmyneRSGEAVYptpTVGMVGLVHDLKHVtTQEFKQAGDLVYVIGetka 588
Cdd:cd02194 90 DTDEEW-LEEFYRGLAEAADRYGVPLVGGDTT----SGSELVI---SVTALGEVEKGKPL-RRSGAKPGDLLYVTG---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 589 EFGGSE--LQKMIHGKifgQSPSIDLDVELKRQKQ------VLAAIQAGLVQSAHDVAEgGLAVAISESAiGANGLGATV 660
Cdd:cd02194 157 TLGDAAagLALLLGGL---KLPEELYEELIERHLRpeprleLGRALAEGLATAMIDISD-GLLADLGHIA-EASGVGAVI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 661 KLD-----GEATAALFAESQSRF----------VITVKRENKEAFEKV--VEAIQVGEVT 703
Cdd:cd02194 232 DLDklplsPALRAAELGEDALELalsggedyelLFTVPPENAEAAAAKlgVPVTVIGRVT 291
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
70-371 |
1.32e-07 |
|
AIR synthase (PurM) related protein, archaeal subgroup 2 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: 100036 Cd Length: 346 Bit Score: 54.32 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 70 TGERVLQGPGEGAGIVDIGDNQAVVFKMESHNHPSAIePYQGAATGVGGIIRDVFSMGARPVALLNSLRFGElqSPRVKY 149
Cdd:cd02691 27 TGEVSIVAQDDDAGVDAADVEYIVVAIDGIHSRLSDF-PFLAGFHATRAALRDVMVMGARPVALLSDIHLAD--DGDVGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 150 LFeEVVAGIAGYGNCIGIPTVGG---EVQFDPCYeGNPLVNAM-CVGLINHEDIKKGQAHGAGNTVMYVGAStgrdgihG 225
Cdd:cd02691 104 LF-DFTAGVTAVSEATGVPLVAGstlRIGGDMVL-GDRLVGGVgAVGRSKSDPSRRKNAEPGDLILMTEGAG-------G 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 226 ATFASEelsesseakrpAVQVGDPFMEKL-----LIEACLELIQSDALVGIQ---DMGAAGLTSSSAEMASKAGMGIEMY 297
Cdd:cd02691 175 GTITTT-----------AIYHGMPDVVEEtlnvdFIKACEALRDSGLVSKVHsmtDVTNGGIRGDALEISKTAGVSLVFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 298 LDDVpqrETGMTP--YEMM-------LSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKGEKVAE 368
Cdd:cd02691 244 EEKV---RSLINPkvLKMLeelgidpLGVSLDSLMIIAPEEDAVDIIRTLREAGVRADEVGRVEEGRGVPLVVTGEGREL 320
|
...
gi 1121125123 369 VPA 371
Cdd:cd02691 321 KPA 323
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
255-370 |
5.39e-07 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 53.49 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 255 LIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYlddVPQREtgmTPYEMMLSESQErMLIVVKKGREQEI 334
Cdd:PHA03366 856 LFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALAGGRGVTIT---VPAGE---DPLQFLFSETPG-VVIEVPPSHLSAV 928
|
90 100 110
....*....|....*....|....*....|....*....
gi 1121125123 335 VDLFEKYGLAAVTMGKV---TEDKMLRLFHKGEKVAEVP 370
Cdd:PHA03366 929 LTRLRSRNIICYPIGTVgpsGPSNTFSVSHNGTVLFRES 967
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
471-704 |
1.09e-05 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 48.70 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 471 LDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPekpeifwqIEKSVDGMSEACRTLQTPVIGGNVSMYNERSGEav 550
Cdd:PRK14090 76 IEPYNGAATGVGGIIRDVLAMGARPTAIFDSLHMSRI--------IDGIIEGIADYGNSIGVPTVGGELRISSLYAHN-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 551 yPTPTVGMVGLVHDlKHVTTQEFKQAGDLVYVigetkaeFGGSELQKMIHGKIFGqspSIDLDVE--LKRQKQV------ 622
Cdd:PRK14090 146 -PLVNVLAAGVVRN-DMLVDSKASRPGQVIVI-------FGGATGRDGIHGASFA---SEDLTGEkaTKLSIQVgdpfae 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 623 -------LAAIQAGLVQSAHDVAEGGLAVAISEsAIGANGLGATVKL--------DGEATAALFAESQSRF-VITVKREN 686
Cdd:PRK14090 214 kmlieafLEMVEEGLVEGAQDLGAGGVLSATSE-LVAKGGLGAIVHLdrvplrepDMEPWEILISESQERMaVVTSPEKA 292
|
250 260
....*....|....*....|..
gi 1121125123 687 KEAFEKVVEAIQ----VGEVTN 704
Cdd:PRK14090 293 SRILEIAKKHLLfgdiVAEVID 314
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
431-663 |
1.27e-05 |
|
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100028 [Multi-domain] Cd Length: 283 Bit Score: 47.59 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 431 DYQVRTSTVVTPGSDAAVVRVRGTEKGLAmttdCN---SRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNP 507
Cdd:cd02192 23 APFDSLGVAADLGDDAAAIPDGDGYLLLA----ADgiwPSLVEADPWWAGYCSVLVNVSDIAAMGGRPLAMVDALWSPSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 508 EKPEIFWQieksvdGMSEACRTLQTPVIGGNVSMynersgEAVYPTPTVGMVGLVHdlKHVTTQEFKQAGDLVYVIGETK 587
Cdd:cd02192 99 EAAAQVLE------GMRDAAEKFGVPIVGGHTHP------DSPYNALSVAILGRAR--KDLLISFGAKPGDRLILAIDLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 588 AEFGGSElqkmihgKIFGQSPSIDLDVELKRQKQVLAAI-QAGLVQSAHDVAEGGL---AVAISEsaigANGLGATVKLD 663
Cdd:cd02192 165 GRVHPSP-------PPNWDATTMKSPALLRRQIALLPELaERGLVHAAKDISNPGIigtLGMLLE----ASGVGAEIDLD 233
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
442-578 |
8.37e-05 |
|
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100031 [Multi-domain] Cd Length: 287 Bit Score: 45.20 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 442 PGSDAAVVRVRGtEKGLAMTTDcnsrYIY---LDPEVGGKIAVAEAARNIVCSGGEP---LAITdCLNFGNPEKP-EIFW 514
Cdd:cd02195 40 TGDDAAVYRLPG-GLALVQTTD----FFPpivDDPYLFGRIAAANALSDIYAMGAKPlsaLAIV-TLPRKLPALQeEVLR 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1121125123 515 QIeksVDGMSEACRTLQTPVIGGNvSMYNersgeavyPTPTVGMV--GLVHDlKHVTTQEFKQAGD 578
Cdd:cd02195 114 EI---LAGGKDKLREAGAVLVGGH-TIEG--------PEPKYGLSvtGLVHP-NKILRNSGAKPGD 166
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
63-351 |
1.61e-04 |
|
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100037 [Multi-domain] Cd Length: 298 Bit Score: 44.12 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 63 VLRKFPTTGERVLQGPGEG--AGIVDIGDNQAVVfkmeshnhpsAIEPYQGAATGVG--GIIR---DVFSMGARPVALLN 135
Cdd:cd06061 14 ILKNLGADRDEVLVGPGGGedAAVVDFGGKVLVV----------STDPITGAGKDAGwlAVHIaanDIATSGARPRWLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 136 SLRFGELQSPRvkyLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCyEGNPLVNAMCVGLINHEDIKKGQAHGAGNT-VMyv 214
Cdd:cd06061 84 TLLLPPGTDEE---ELKAIMREINEAAKELGVSIVGGHTEVTPG-VTRPIISVTAIGKGEKDKLVTPSGAKPGDDiVM-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 215 gasTGRDGIHGATFAseelsesseAKRPAVQVGDPFMEKLLIEAC----LELIQSDALVGIQD----MGAA---GLTSSS 283
Cdd:cd06061 158 ---TKGAGIEGTAIL---------ANDFEEELKKRLSEEELREAAklfyKISVVKEALIAAEAgvtaMHDAtegGILGAL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1121125123 284 AEMASKAGMGIEMYLDDVPQRE--------TGMTPYEMMLSESqerMLIVVKKGREQEIVDLFEKYGLAAVTMGKV 351
Cdd:cd06061 226 WEVAEASGVGLRIEKDKIPIRQetkeiceaLGIDPLRLISSGT---LLITVPPEKGDELVDALEEAGIPASVIGKI 298
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
458-537 |
2.60e-04 |
|
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 43.62 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125123 458 LAMTTDcnsryiyldpEVGGKIAVAEAARN---------------IVCSGGEPLAITDCLNFGNPEkPEIFWQIeksVDG 522
Cdd:cd02196 22 LVSGTD----------GVGTKLKLAQEMGKhdtigidlvamcvndILCQGAEPLFFLDYIATGKLD-PEVAAEI---VKG 87
|
90
....*....|....*
gi 1121125123 523 MSEACRTLQTPVIGG 537
Cdd:cd02196 88 IAEGCRQAGCALLGG 102
|
|
| |
