|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
10-739 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 1295.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 10 EIKEQRIYQEMGLTDSEYDLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGIVDIGDG 89
Cdd:PRK01213 1 TPDTEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGENAGVVDIGDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 90 LGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKYLVSEVVAGIAGYGNSIGIPTV 169
Cdd:PRK01213 81 QAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 170 GGEIQFDPCYTKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRSAVQVGDPF 249
Cdd:PRK01213 161 GGEVYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGASFASAELSEESEEKRPAVQVGDPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 250 MEKLLLEACLDVIRdhSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKK 329
Cdd:PRK01213 241 MEKLLIEACLELIK--TGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 330 GHVEEIQALFERYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAEDAPVYHKPSKEPARYQAFQeeeafvPVIDDVV 409
Cdd:PRK01213 319 GKEEEVLAIFEKWDLDAAVIGEVTDDGRLRVYHHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQ------ADPEDLK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 410 GVWKELLAQPTIASKRHIYEQYDYQVRTDTAVVPGSDAAIVRVRGTEKAIAMTTDCNSRYLYLDPEVGGAIAVAEAARNI 489
Cdd:PRK01213 393 EALLKLLSSPNIASKEWVYEQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 490 VCSGGKPLAITDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVEDLAHI 569
Cdd:PRK01213 473 AAVGATPLAITDCLNFGNPEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 570 TTQDFKASGDVIFLIGETKAEYSGSELQKIQQGKISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAE 649
Cdd:PRK01213 553 TTSGFKKEGDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 650 ATFKAGLGADVEVPFALS---QLFSESQSRFLVSVKPENEAAFAQLME--LEKVYRLGVVTaDETIRVKHKEDLVtvkTT 724
Cdd:PRK01213 633 MAIAGGLGAEVDLSDGLRpdaLLFSESQGRYVVSVPPENEEAFEALAEaaGVPATRIGVVG-GDALKVKGNDTES---LE 708
|
730
....*....|....*
gi 1071575466 725 ELRSIWEGAIPCLLK 739
Cdd:PRK01213 709 ELREAWEGALPRLLG 723
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
4-739 |
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: 1152.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 4 MEPTTKEIKEQRIYQEMGLTDSEYDLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGI 83
Cdd:COG0046 6 LEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPTEGPRVLSGPGDNAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 84 VDIGDGLGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTP--HAKYLVSEVVAGIAGYG 161
Cdd:COG0046 86 VDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAGIADYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 162 NSIGIPTVGGEIQFDPCYTKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRS 241
Cdd:COG0046 166 NCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSELDRP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 242 AVQVGDPFMEKLLLEACLDVIRDhsDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQE 321
Cdd:COG0046 246 AVQVGDPFMEKRLIEAILELGDT--GLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 322 RMLLCVKKGHVEEIQALFERYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAEDAPVYHKPSKEPARYQAFQeeeaf 401
Cdd:COG0046 324 RMLLVVKPEKLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLD----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 402 VPVIDDVVGVWKELLAQPTIASKRHIYEQYDYQVRTDTAVVPG-SDAAIVRVRGTEKAIAMTTDCNSRYLYLDPEVGGAI 480
Cdd:COG0046 399 LPEPIDLEEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDPGvADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARM 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 481 AVAEAARNIVCSGGKPLAITDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDG--TGIYPTPVIG 558
Cdd:COG0046 479 AVAEAARNLAAVGAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKDgkVAIPPTPVIG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 559 MVGLVEDLAHITTQDFKASGDVIFLIGETKAEYSGSELQKIqQGKISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDL 638
Cdd:COG0046 559 AVGLVDDVRKTVTPDLKKEGDLLYLIGETKNELGGSEYAQV-LGQLGGEPPDVDLEAEKALFEAVQELIREGLILAAHDV 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 639 AEGGFGVALAEATFKAGLGADVEVPF-----ALSQLFSESQSRFLVSVKPENEAAFAQLMELEKV--YRLGVVTADETIR 711
Cdd:COG0046 638 SDGGLAVALAEMAFAGGLGADIDLDAlgdlrPDAALFSESQGRAVVQVAPEDAEAVEALLAEAGLpaHVIGTVTGDDRLV 717
|
730 740
....*....|....*....|....*....
gi 1071575466 712 VKHK-EDLVTVKTTELRSIWEGAIPCLLK 739
Cdd:COG0046 718 IRRGgETLLSLSLAELRDAWEETLPRLRD 746
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
22-738 |
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: 1032.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 22 LTDSEYDLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGIVDIGDGLGVAFKVESHNH 101
Cdd:TIGR01736 1 LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYAVVFKMESHNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 102 PSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTK 181
Cdd:TIGR01736 81 PSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 182 NPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQ-RSAVQVGDPFMEKLLLEACLD 260
Cdd:TIGR01736 161 NPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEELSEEAEEEdRPAVQVGDPFTEKLLIEATLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 261 VIRdhSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFE 340
Cdd:TIGR01736 241 AVD--TGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 341 RYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAeDAPVYHKPSKEPARYQAFQEEEAFVPVIDDVVgvwkELLAQPT 420
Cdd:TIGR01736 319 KYELPASVIGEVTDEGRIRLYYKGEVVADLPIELLA-DAPEYERPSEPPKYPEEEKEPEPPADLEDAFL----KVLSSPN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 421 IASKRHIYEQYDYQVRTDTAVVPGSDAAIVRVRGTEK-AIAMTTDCNSRYLYLDPEVGGAIAVAEAARNIVCSGGKPLAI 499
Cdd:TIGR01736 394 IASKEWVYRQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 500 TDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVEDLAHITTQDFKASGD 579
Cdd:TIGR01736 474 VDCLNFGNPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 580 VIFLIGETKAEYSGSELQKIQQGKISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGAD 659
Cdd:TIGR01736 554 AIYLIGETKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGAE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 660 VEVPFALSQ-----LFSESQSRFLVSVKPENEAAFAQLMELeKVYRLGVVTaDETIRVKHKEDLVTVKTTELRSIWEGAI 734
Cdd:TIGR01736 634 VDIDEIASArpdelLFSESNGRAIVAVPEEKAEEAVKSKGV-PAKVIGKTG-GDRLTIKTGDDTISVSVKELRDAWEEAL 711
|
....
gi 1071575466 735 PCLL 738
Cdd:TIGR01736 712 PEYM 715
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
42-370 |
3.22e-173 |
|
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: 498.54 E-value: 3.22e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 42 ETGLFSVMWSEHCSYKNSKPVLRKFptegkqvlqgpgegagivdigdgLGVAFKVESHNHPSYVEPYQGAATGVGGIIRD 121
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLLKMI-----------------------WAVVFKVETHNHPSAIEPFGGAATGVGGIIRD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 122 VFSMGARPIAMLNSLRFGELDTP--------HAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTKNPLVNAMCVGLI 193
Cdd:cd02203 58 ILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 194 EAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSE-EGEQQRSAVQVGDPFMEKLLLEACLDVIRDhsDILVGI 272
Cdd:cd02203 138 PKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSSKELSEnSSELDRPAVQVGDPFMEKKLQEAILEARET--GLIVGI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 273 QDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQV 352
Cdd:cd02203 216 QDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEV 295
|
330
....*....|....*...
gi 1071575466 353 TDDKMYKIIHHGEVVANV 370
Cdd:cd02203 296 TDDGRLRLYYKGEVVADL 313
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
205-362 |
5.88e-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: 129.77 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 205 GIGNPVMYVGAktgrDGIHGATFASVEFSEEGEQqRSAVQVGDPFMEKLLLEACLDVIRDHSDIlVGIQDMGAAGLVSSS 284
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLEDSG-LAAVQLGDPLLEPTLIYVKLLLAALGGLV-KAMHDITGGGLAGAL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071575466 285 SEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQVTDDKMYKIIH 362
Cdd:pfam02769 75 AEMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
10-739 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 1295.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 10 EIKEQRIYQEMGLTDSEYDLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGIVDIGDG 89
Cdd:PRK01213 1 TPDTEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGENAGVVDIGDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 90 LGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKYLVSEVVAGIAGYGNSIGIPTV 169
Cdd:PRK01213 81 QAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 170 GGEIQFDPCYTKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRSAVQVGDPF 249
Cdd:PRK01213 161 GGEVYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGASFASAELSEESEEKRPAVQVGDPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 250 MEKLLLEACLDVIRdhSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKK 329
Cdd:PRK01213 241 MEKLLIEACLELIK--TGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 330 GHVEEIQALFERYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAEDAPVYHKPSKEPARYQAFQeeeafvPVIDDVV 409
Cdd:PRK01213 319 GKEEEVLAIFEKWDLDAAVIGEVTDDGRLRVYHHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQ------ADPEDLK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 410 GVWKELLAQPTIASKRHIYEQYDYQVRTDTAVVPGSDAAIVRVRGTEKAIAMTTDCNSRYLYLDPEVGGAIAVAEAARNI 489
Cdd:PRK01213 393 EALLKLLSSPNIASKEWVYEQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 490 VCSGGKPLAITDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVEDLAHI 569
Cdd:PRK01213 473 AAVGATPLAITDCLNFGNPEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 570 TTQDFKASGDVIFLIGETKAEYSGSELQKIQQGKISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAE 649
Cdd:PRK01213 553 TTSGFKKEGDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 650 ATFKAGLGADVEVPFALS---QLFSESQSRFLVSVKPENEAAFAQLME--LEKVYRLGVVTaDETIRVKHKEDLVtvkTT 724
Cdd:PRK01213 633 MAIAGGLGAEVDLSDGLRpdaLLFSESQGRYVVSVPPENEEAFEALAEaaGVPATRIGVVG-GDALKVKGNDTES---LE 708
|
730
....*....|....*
gi 1071575466 725 ELRSIWEGAIPCLLK 739
Cdd:PRK01213 709 ELREAWEGALPRLLG 723
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
4-739 |
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: 1152.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 4 MEPTTKEIKEQRIYQEMGLTDSEYDLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGI 83
Cdd:COG0046 6 LEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPTEGPRVLSGPGDNAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 84 VDIGDGLGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTP--HAKYLVSEVVAGIAGYG 161
Cdd:COG0046 86 VDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAGIADYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 162 NSIGIPTVGGEIQFDPCYTKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRS 241
Cdd:COG0046 166 NCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSELDRP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 242 AVQVGDPFMEKLLLEACLDVIRDhsDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQE 321
Cdd:COG0046 246 AVQVGDPFMEKRLIEAILELGDT--GLIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 322 RMLLCVKKGHVEEIQALFERYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAEDAPVYHKPSKEPARYQAFQeeeaf 401
Cdd:COG0046 324 RMLLVVKPEKLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLD----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 402 VPVIDDVVGVWKELLAQPTIASKRHIYEQYDYQVRTDTAVVPG-SDAAIVRVRGTEKAIAMTTDCNSRYLYLDPEVGGAI 480
Cdd:COG0046 399 LPEPIDLEEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDPGvADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARM 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 481 AVAEAARNIVCSGGKPLAITDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDG--TGIYPTPVIG 558
Cdd:COG0046 479 AVAEAARNLAAVGAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKDgkVAIPPTPVIG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 559 MVGLVEDLAHITTQDFKASGDVIFLIGETKAEYSGSELQKIqQGKISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDL 638
Cdd:COG0046 559 AVGLVDDVRKTVTPDLKKEGDLLYLIGETKNELGGSEYAQV-LGQLGGEPPDVDLEAEKALFEAVQELIREGLILAAHDV 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 639 AEGGFGVALAEATFKAGLGADVEVPF-----ALSQLFSESQSRFLVSVKPENEAAFAQLMELEKV--YRLGVVTADETIR 711
Cdd:COG0046 638 SDGGLAVALAEMAFAGGLGADIDLDAlgdlrPDAALFSESQGRAVVQVAPEDAEAVEALLAEAGLpaHVIGTVTGDDRLV 717
|
730 740
....*....|....*....|....*....
gi 1071575466 712 VKHK-EDLVTVKTTELRSIWEGAIPCLLK 739
Cdd:COG0046 718 IRRGgETLLSLSLAELRDAWEETLPRLRD 746
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
22-738 |
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: 1032.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 22 LTDSEYDLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGIVDIGDGLGVAFKVESHNH 101
Cdd:TIGR01736 1 LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYAVVFKMESHNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 102 PSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTK 181
Cdd:TIGR01736 81 PSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 182 NPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQ-RSAVQVGDPFMEKLLLEACLD 260
Cdd:TIGR01736 161 NPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEELSEEAEEEdRPAVQVGDPFTEKLLIEATLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 261 VIRdhSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFE 340
Cdd:TIGR01736 241 AVD--TGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 341 RYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAeDAPVYHKPSKEPARYQAFQEEEAFVPVIDDVVgvwkELLAQPT 420
Cdd:TIGR01736 319 KYELPASVIGEVTDEGRIRLYYKGEVVADLPIELLA-DAPEYERPSEPPKYPEEEKEPEPPADLEDAFL----KVLSSPN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 421 IASKRHIYEQYDYQVRTDTAVVPGSDAAIVRVRGTEK-AIAMTTDCNSRYLYLDPEVGGAIAVAEAARNIVCSGGKPLAI 499
Cdd:TIGR01736 394 IASKEWVYRQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 500 TDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVEDLAHITTQDFKASGD 579
Cdd:TIGR01736 474 VDCLNFGNPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 580 VIFLIGETKAEYSGSELQKIQQGKISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGAD 659
Cdd:TIGR01736 554 AIYLIGETKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGAE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 660 VEVPFALSQ-----LFSESQSRFLVSVKPENEAAFAQLMELeKVYRLGVVTaDETIRVKHKEDLVTVKTTELRSIWEGAI 734
Cdd:TIGR01736 634 VDIDEIASArpdelLFSESNGRAIVAVPEEKAEEAVKSKGV-PAKVIGKTG-GDRLTIKTGDDTISVSVKELRDAWEEAL 711
|
....
gi 1071575466 735 PCLL 738
Cdd:TIGR01736 712 PEYM 715
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
42-370 |
3.22e-173 |
|
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: 498.54 E-value: 3.22e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 42 ETGLFSVMWSEHCSYKNSKPVLRKFptegkqvlqgpgegagivdigdgLGVAFKVESHNHPSYVEPYQGAATGVGGIIRD 121
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLLKMI-----------------------WAVVFKVETHNHPSAIEPFGGAATGVGGIIRD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 122 VFSMGARPIAMLNSLRFGELDTP--------HAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTKNPLVNAMCVGLI 193
Cdd:cd02203 58 ILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 194 EAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSE-EGEQQRSAVQVGDPFMEKLLLEACLDVIRDhsDILVGI 272
Cdd:cd02203 138 PKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSSKELSEnSSELDRPAVQVGDPFMEKKLQEAILEARET--GLIVGI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 273 QDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQV 352
Cdd:cd02203 216 QDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEV 295
|
330
....*....|....*...
gi 1071575466 353 TDDKMYKIIHHGEVVANV 370
Cdd:cd02203 296 TDDGRLRLYYKGEVVADL 313
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
28-564 |
1.65e-132 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 405.01 E-value: 1.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 28 DLVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPtegkqvLQGPGEGAGIVDIGDGLGVAFKVESHNHPSYVEP 107
Cdd:PRK14090 5 NILEEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLP------KTGFEGNAGVVNLDDYYSIAFKIESHNHPSAIEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 108 YQGAATGVGGIIRDVFSMGARPIAMLNSLrfgeldtpHAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTKNPLVNA 187
Cdd:PRK14090 79 YNGAATGVGGIIRDVLAMGARPTAIFDSL--------HMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 188 MCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRSaVQVGDPFMEKLLLEACLDVIRDhsD 267
Cdd:PRK14090 151 LAAGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGEKATKLS-IQVGDPFAEKMLIEAFLEMVEE--G 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 268 ILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFERYGLEAV 347
Cdd:PRK14090 228 LVEGAQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 348 VIGQVTDDKMYKIIHHGEVVANVPVDALAEdAPvyhkpskEPARYQAFQEEeafVPVIDDVvgVWKELLAqptiaskRHI 427
Cdd:PRK14090 308 IVAEVIDDPIYRVMYRDDLVMEVPVQLLAN-AP-------EEEIVEYTPGE---IPEFKRV--EFEEVNA-------REV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 428 YEQYDYQVRTDTAVVPGSDAAIVRVRGTEkAIAMTTDCNSRYLYLDPEVGGAIAVAEAARNIVCSGGKPLAITDGLNFGN 507
Cdd:PRK14090 368 FEQYDHMVGTDTVLPPGFGAAVMRIKRDG-GYSLVTHSRADLALQDTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGD 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1071575466 508 PEKPEIfwEIEKAADGISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVE 564
Cdd:PRK14090 447 PDVDPV--GLSAMMTALKDACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLGKVN 501
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
446-704 |
1.16e-112 |
|
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: 341.44 E-value: 1.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 446 DAAIVRVRG-TEKAIAMTTDCNSRYLYLDPEVGGAIAVAEAARNIVCSGGKPLAITDGLNFGNPEKPE-IFWEIEKAADG 523
Cdd:cd02204 1 DAAVLRIPGeTDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEgEMGQLVEAVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 524 ISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVEDLAHITTQDFKASGDVIFLIGETKAEYSGSELQKIQQGK 603
Cdd:cd02204 81 LGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDLLYLIGETKDELGGSEYALAYHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 604 ISGRAPELDLVTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVEVPFALSQ---LFSESQSRFLVS 680
Cdd:cd02204 161 GGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDDAEdelLFSESLGRVLVE 240
|
250 260
....*....|....*....|....
gi 1071575466 681 VKPENEAAFAQLMELEKVYRLGVV 704
Cdd:cd02204 241 VKPENEEVFEAEEAGVPATVIGTV 264
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
91-352 |
3.18e-51 |
|
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: 179.80 E-value: 3.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 91 GVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMG--ARPIAMLNSLRFGELDtPHAKYLVSEVVAGIAGYGNSIGIPT 168
Cdd:cd02193 2 GEAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGidAKPIALSANWMASAGH-PGEDAILYDAVKGVAELCNQLGLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 169 VGGEIQFDPCY-----------TKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGE 237
Cdd:cd02193 81 PVGKDRMSMKTrwqegneqremTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNGLGGTALASVALSYRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 238 QQRSaVQVGDPFMEKLLLEACLDVIRdhSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHMTPYEMLLS 317
Cdd:cd02193 161 GDKS-AQVRDPAQEKGFYEAMQALVA--AGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIALF 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1071575466 318 ESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQV 352
Cdd:cd02193 238 ESQERGVIQVRAEDRDAVEEAQYGLADCVHVLGQA 272
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
205-362 |
5.88e-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: 129.77 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 205 GIGNPVMYVGAktgrDGIHGATFASVEFSEEGEQqRSAVQVGDPFMEKLLLEACLDVIRDHSDIlVGIQDMGAAGLVSSS 284
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLEDSG-LAAVQLGDPLLEPTLIYVKLLLAALGGLV-KAMHDITGGGLAGAL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071575466 285 SEMASKAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQVTDDKMYKIIH 362
Cdd:pfam02769 75 AEMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
95-730 |
2.59e-34 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 141.09 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 95 KVESHNHPSYVEPYQGAATGVGGIIRDVFS--MGARPIA-----MLNSLRFGELDTP-HAKYLVSEVVA----------- 155
Cdd:PRK05297 288 KVETHNHPTAISPFPGAATGSGGEIRDEGAtgRGSKPKAgltgfSVSNLRIPGFEQPwEEDYGKPERIAsaldimiegpl 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 156 GIAGYGNSIGIPTVGG-----EIQFDPC------YTKnPLVNAMCVGLIEAKDIQKGQ-AKG-----IGNPVMyvgaktg 218
Cdd:PRK05297 368 GGAAFNNEFGRPNLLGyfrtfEQKVNSHneevrgYHK-PIMLAGGIGNIRADHVQKGEiPVGaklivLGGPAM------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 219 RDGIHGATFASV---EFSEEGEqqRSAVQVGDPFMEKllleACLDVIR------DHSDIlVGIQDMGAAGLVSSSSEMAS 289
Cdd:PRK05297 440 RIGLGGGAASSMasgQSSEDLD--FASVQRGNPEMER----RCQEVIDrcwqlgDDNPI-LSIHDVGAGGLSNAFPELVN 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 290 KAGAGLELIMDDVPQRELHMTPYEMLLSESQERMLLCVKKGHVEEIQALFERyglE----AVViGQVTDDKMYKII--HH 363
Cdd:PRK05297 513 DGGRGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEAICER---ErcpfAVV-GEATEERHLTLEdsHF 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 364 GEVVANVPVDALAEDAPVYHKPSK-EPARYQAFQEEEAfvpVIDDVVgvwKELLAQPTIASKRHIYEQYDyqvRT----- 437
Cdd:PRK05297 589 DNKPVDLPLDVLLGKPPKMHRDVKtVKAKGPALDYSGI---DLAEAV---ERVLRLPTVASKSFLITIGD---RSvtglv 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 438 --DTAV----VPGSDAAIvrvrgtekaiaMTTDCNSRY-------------LyLDPEVGGAIAVAEAARNIVCSggkPLA 498
Cdd:PRK05297 660 arDQMVgpwqVPVADCAV-----------TAASYDGYAgeamamgertpvaL-LDAAASARMAVGEALTNIAAA---PIG 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 499 ITDGLNF--------GNPEkpeifweiEKAA--DGISAA----CLELD--TPVisGNVSL-----YNETDGTGIYPTP-- 555
Cdd:PRK05297 725 DLKRIKLsanwmaaaGHPG--------EDARlyDAVKAVgmelCPALGitIPV--GKDSLsmktkWQEGGEDKEVTSPls 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 556 -VIGMVGLVEDLAHITTQDFKASGD-VIFLI--GETKAEYSGSELQKIqQGKISGRAPELDLVTEKK-----YQQLllta 626
Cdd:PRK05297 795 lIISAFAPVEDVRKTLTPQLRTDKDtALLLIdlGRGKNRLGGSALAQV-YNQLGDKAPDVDDAEDLKgffnaIQAL---- 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 627 IQEGLVASSHDLAEGGFGVALAEATFKAGLGADVEVPF----ALSQLFSESqsrfL---VSVKPENEAAFAQLME----L 695
Cdd:PRK05297 870 VAEGLLLAYHDRSDGGLLTTLAEMAFAGHCGLDIDLDAlgddALAALFNEE----LgavIQVRAADRDAVEAILAehglS 945
|
730 740 750
....*....|....*....|....*....|....*.
gi 1071575466 696 EKVYRLGVVTADETIRVKHKEDLVTVKT-TELRSIW 730
Cdd:PRK05297 946 DCVHVIGKPNAGDRIVITRNGKTVFSESrTELRRWW 981
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
91-351 |
5.91e-31 |
|
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: 120.96 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 91 GVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHakyLVSEVVAGIAGYGNSIGIPTVG 170
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVD---ILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 171 GEIQFDPCYTK-NPLVNAMCVGLIEAKDIQKGqakgignpvmyvgaktgrdgihgatfasvefseegeqqrSAVQVGDpf 249
Cdd:cd00396 78 GHTSVSPGTMGhKLSLAVFAIGVVEKDRVIDS---------------------------------------SGARPGD-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 250 meKLLLEACLDVIRDHSDILV-GIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELHM-----TPYEMLLSESQERM 323
Cdd:cd00396 117 --VLILTGVDAVLELVAAGDVhAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRwlcveHIEEALLFNSSGGL 194
|
250 260
....*....|....*....|....*...
gi 1071575466 324 LLCVKKGHVEEIQALFERYGLEAVVIGQ 351
Cdd:cd00396 195 LIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
91-193 |
2.08e-30 |
|
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: 115.24 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 91 GVAFKVESHNHPSYVEPYQG-AATGVGGIIRDVFSMGARPIAMLNSLRFGELdtPHAKYLVSEVVAGIAGYGNSIGIPTV 169
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLALPGG--PEVEWVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....
gi 1071575466 170 GGEIQFDPCYtKNPLVNAMCVGLI 193
Cdd:pfam00586 82 GGDTSFDPEG-GKPTISVTAVGIV 104
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
458-563 |
5.73e-30 |
|
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: 114.08 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 458 AIAMTTDCNSRYLYLDPEVG-GAIAVAEAARNIVCSGGKPLAITDGLNFgnPEKPEIFWEIEKAADGISAACLELDTPVI 536
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLAL--PGGPEVEWVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....*..
gi 1071575466 537 SGNVSLYNEtdgtGIYPTPVIGMVGLV 563
Cdd:pfam00586 82 GGDTSFDPE----GGKPTISVTAVGIV 104
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
14-731 |
1.05e-25 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 114.09 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 14 QRIYQEMGLTDSEYD------LVCSILGREPnyTETGLFSVMWS--EHC------------------------------- 54
Cdd:PLN03206 168 EEINKEMGLAFDEQDldyytrLFRDDIKRDP--TNVELFDIAQSnsEHSrhwffsgklvidgqpmpktlfqmvkdtlkan 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 55 ------SYKNSKPVLRKFPTEGKQVLQgPGEGAGIVDIGDGLGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFS--MG 126
Cdd:PLN03206 246 pnnsviGFKDNSSAIRGFVVQPLRPVS-PGSPSPLAPVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHAtgRG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 127 ARPIA-----MLNSLRFGELDTPH-----------AKYLVSEVVA--GIAGYGNSIGIPTVGGeiqfdpcYTKN------ 182
Cdd:PLN03206 325 SFVVAgtagyCVGNLRIEGSYAPWedssfvypsnlASPLQILIDAsnGASDYGNKFGEPLIQG-------YTRTfgmrlp 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 183 ---------PLVNAMCVGLIEAKDIQKGQAKgIGNPVMYVGAKTGRDGIHGATFAS-VEFSEEGEQQRSAVQVGDPFME- 251
Cdd:PLN03206 398 ngerrewlkPIMFSGGIGQIDHTHLTKGEPD-IGMLVVKIGGPAYRIGMGGGAASSmVSGQNDAELDFNAVQRGDAEMSq 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 252 KL--LLEACLDvIRDHSDIlVGIQDMGAAGLVSSSSEMASKAGAglELIMDDVPQRELHMTPYEMLLSESQERMLLCVKK 329
Cdd:PLN03206 477 KLyrVVRACVE-MGEDNPI-VSIHDQGAGGNCNVVKEIIYPKGA--EIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKP 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 330 GHVEEIQALFERYGLEAVVIGQVTDDKMYKIIH----HGEVVANVPVDALAEDAPVYHKPSKEPAR-----YQAFQEEEA 400
Cdd:PLN03206 553 ESRDLLQSICDRERCSMAVIGTIDGSGRVVLVDsaapEKCEANGLPPPPPAVDLDLEKVLGDMPQKtfefkRVANKLEPL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 401 FVPVIDDVVGVWKELLAQPTIASKRHIYEQYDyqvRTDTAVV-----------PGSDAAIvrvrgtekaIAMT------- 462
Cdd:PLN03206 633 DIPPGITVMDALKRVLRLPSVCSKRFLTTKVD---RCVTGLVaqqqtvgplqiPLADVAV---------IAQThtgltgg 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 463 -TDCNSRYL--YLDPEVGGAIAVAEAARNIVCSggKPLAITDGLNFGNpekpeifW-----------EIEKAADGISAAC 528
Cdd:PLN03206 701 aCAIGEQPIkgLVDPKAMARLAVGEALTNLVWA--KVTALSDVKASGN-------WmyaakldgegaDMYDAAVALRDAM 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 529 LELDTPVISGNVSLYNETDGTG-IYPTP---VIGMVGLVEDLAHITTQDFKASGDVIFL---IGETKAEYSGSELQKIqQ 601
Cdd:PLN03206 772 IELGVAIDGGKDSLSMAAQAGGeVVKAPgnlVISAYVTCPDITKTVTPDLKLGDDGVLLhvdLGKGKRRLGGSALAQA-Y 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 602 GKISGRAPELDLVTEKK-----YQQLlltaIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVEVPF----ALSQLFSE 672
Cdd:PLN03206 851 DQIGDDCPDLDDVAYLKkafeaTQDL----IAKRLISAGHDISDGGLVVTLLEMAFAGNCGINVDLPSsghsAFETLFAE 926
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071575466 673 SQSrFLVSVKPENEAAFAQLMELEKV--YRLGVVTADETIRVKHKEDL-VTVKTTELRSIWE 731
Cdd:PLN03206 927 ELG-LVLEVSRKNLDAVMEKLAAAGVtaEVIGQVTASPLIEVKVDGATcLSEKTASLRDMWE 987
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
476-719 |
3.26e-23 |
|
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: 101.01 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 476 VGGAIavaeaaRNIVCSGGKPLAITDGLNFGNPEKPEIF--------WEIEKAADGISAACLELDTPVISGNVSLYNETD 547
Cdd:cd02203 51 VGGII------RDILSMGARPIALLDGLRFGDLDIPGYEpkgklsprRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 548 GTGIyptpVIGM-VGLVEDlAHITTQDFKASGDVIFLIG-------------------ETKAEYSGSELQKiqqgkisGR 607
Cdd:cd02203 125 GNPL----VNVGcVGIVPK-DHIVKSKAPGPGDLVVLVGgrtgrdgiggatfsskelsENSSELDRPAVQV-------GD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 608 APeldlvTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVE---VPFA---LSQ---LFSESQSRFL 678
Cdd:cd02203 193 PF-----MEKKLQEAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDldkVPLRepgMSPweiWISESQERML 267
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1071575466 679 VSVKPENEAAFAQLMELEKV--YRLGVVTADETIRVKHKEDLV 719
Cdd:cd02203 268 LVVPPEDLEEFLAICKKEDLeaAVIGEVTDDGRLRLYYKGEVV 310
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
11-57 |
5.58e-20 |
|
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: 83.67 E-value: 5.58e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1071575466 11 IKEQRIYQEMGLTDSEYDLVCSI---LGREPNYTETGLFSVMWSEHCSYK 57
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYfagLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
458-692 |
3.76e-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: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 458 AIAMTTDCNSRYLYLDPEVGGAIAVAEAARNIVCSGGKPLAITDGLNFGNPEKPEIfweIEKAADGISAACLELDTPVIS 537
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDI---LEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 538 GNVSLYneTDGTGIYPTPVIGMVGLVEDLAHITTQDFKAsGDVIFLIGetkaeysgselqkiqqgkisgrapeldlvtek 617
Cdd:cd00396 78 GHTSVS--PGTMGHKLSLAVFAIGVVEKDRVIDSSGARP-GDVLILTG-------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 618 kyQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVE--------------VPFALSQLFSESQSRFLVSVKP 683
Cdd:cd00396 123 --VDAVLELVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDleaipldevvrwlcVEHIEEALLFNSSGGLLIAVPA 200
|
....*....
gi 1071575466 684 ENEAAFAQL 692
Cdd:cd00396 201 EEADAVLLL 209
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
459-692 |
1.38e-15 |
|
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: 77.72 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 459 IAMTTDCNSRYLYLDPEVGGAIAVAEAARNIVCSG--GKPLAITDGL--NFGNPEKPEIFWEIEKaadGISAACLELDTP 534
Cdd:cd02193 3 EAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGidAKPIALSANWmaSAGHPGEDAILYDAVK---GVAELCNQLGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 535 VISGNVSLYNETDGTGIY--------PTPVIGMVGLVEDLAHittQDFKAS--GDVIFLIGETK---AEYSGSELQKIQQ 601
Cdd:cd02193 80 IPVGKDRMSMKTRWQEGNeqremthpPSLVISAFGRVRDDRH---TLPQLSteGNALLLIGGGKghnGLGGTALASVALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 602 GKISGRAP--ELDLVTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVEVPFALSQ---------LF 670
Cdd:cd02193 157 YRQLGDKSaqVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDepdmepleiAL 236
|
250 260
....*....|....*....|..
gi 1071575466 671 SESQSRFLVSVKPENEAAFAQL 692
Cdd:cd02193 237 FESQERGVIQVRAEDRDAVEEA 258
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
578-714 |
1.91e-14 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 71.22 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 578 GDVIFLIGEtkaeySG------SELQKIQQGKISGRAPELDLVTEKKYQQLLLTAIQ-EGLVASSHDLAEGGFGVALAEA 650
Cdd:pfam02769 3 GDVLILLGS-----SGlhgaglSLSRKGLEDSGLAAVQLGDPLLEPTLIYVKLLLAAlGGLVKAMHDITGGGLAGALAEM 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1071575466 651 TFKAGLGADVEVP---------FALSQLFSESQSRFLVSVKPENEAAFAQLMELE--KVYRLGVVTADETIRVKH 714
Cdd:pfam02769 78 APASGVGAEIDLDkvpifeelmLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEglEAAVIGEVTAGGRLTVIV 152
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
81-352 |
3.09e-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: 73.34 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 81 AGIVDI--GDGLGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKY--LVsEVVAG 156
Cdd:cd02204 2 AAVLRIpgETDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEGEMgqLV-EAVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 157 IAGYGNSIGIPTVGGEIQFdpcYTKNPLVNAM------CVGLIEAKDIQKGQA-KGIGNPVMYVGAKTGRDGihGATFAS 229
Cdd:cd02204 81 LGDACRALGTPVIGGKDSL---YNETEGVAIPptlvigAVGVVDDVRKIVTLDfKKEGDLLYLIGETKDELG--GSEYAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 230 VEFSEEGEqqrsAVQVGDPFMEKLLLEACLDVIRDHsdILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPqrelhm 309
Cdd:cd02204 156 AYHGLGGG----APPLVDLEREKALFDAVQELIKEG--LVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDD------ 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1071575466 310 TPYEMLLSESQERMLLCVKKGHVEEIQAlfERYGLEAVVIGQV 352
Cdd:cd02204 224 AEDELLFSESLGRVLVEVKPENEEVFEA--EEAGVPATVIGTV 264
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
472-730 |
1.27e-12 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 71.59 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 472 LDPEVGGAIAVAEAARNIVCSGGKPLA-ITDGLNFGNPEKPEIFWEIEKAADGISAACLELdtpvisgNVSLY------N 544
Cdd:PHA03366 704 LDPILGAKYAIVEALTNLMLAPVANLEdITITLSVTWPPTDQAASELYRALAACKEFCREL-------GVNFTftsassS 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 545 ETDGTGIYPTPVIGMV-----GLVEDLAHITTQDFKASGDVIFLIG-ETKAEYSGSELQKIQqGKISGRAPELDLVTEKK 618
Cdd:PHA03366 777 PRQDQPPQPGPLFNTIvftasAPVPSSTPRLTPDLKKPGSALVHLSiSPEYTLAGSVFEQIF-GLKSGTLPDISPSYLKN 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 619 YQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVEVPF---ALSQLFSESQSrFLVSVKPENEAA---FAQL 692
Cdd:PHA03366 856 LFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALAGGRGVTITVPAgedPLQFLFSETPG-VVIEVPPSHLSAvltRLRS 934
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1071575466 693 MELEkVYRLGVV---TADETIRVKHK-EDLVTVKTTELRSIW 730
Cdd:PHA03366 935 RNII-CYPIGTVgpsGPSNTFSVSHNgTVLFRESLSSLRSTW 975
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
444-661 |
3.58e-09 |
|
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: 58.76 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 444 GSDAAIVRVrgTEKAIAMTTDCnsryLYLDPEVGGAIAVAEAARNIVCSGGKPLAITDGLNF--GNPEKpeifwEIEKAA 521
Cdd:cd06061 32 GEDAAVVDF--GGKVLVVSTDP----ITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLppGTDEE-----ELKAIM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 522 DGISAACLELDTPVISGNvslynetdgTGIYPT---PVIG--MVGLVEDLAHITTQDFKAsGDVIFLIGETKAEYSGSeL 596
Cdd:cd06061 101 REINEAAKELGVSIVGGH---------TEVTPGvtrPIISvtAIGKGEKDKLVTPSGAKP-GDDIVMTKGAGIEGTAI-L 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1071575466 597 QKIQQGKISGRAPELDLVTEKKYQqLLLTAIQEGLVA------SSHDLAEGGFGVALAEATFKAGLGADVE 661
Cdd:cd06061 170 ANDFEEELKKRLSEEELREAAKLF-YKISVVKEALIAaeagvtAMHDATEGGILGALWEVAEASGVGLRIE 239
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
472-719 |
4.60e-07 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 53.32 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 472 LDPEVGGAIAVAEAARNIVCSGGKPLAITDGLNFGNPekpeifweIEKAADGISAACLELDTPVISGNVSLyneTDGTGI 551
Cdd:PRK14090 76 IEPYNGAATGVGGIIRDVLAMGARPTAIFDSLHMSRI--------IDGIIEGIADYGNSIGVPTVGGELRI---SSLYAH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 552 YPTPVIGMVGLVEDlAHITTQDFKASGDVIFLIGETK-------AEYSGSELQKIQQGKISGRAPelDLVTEKKYQQLLL 624
Cdd:PRK14090 145 NPLVNVLAAGVVRN-DMLVDSKASRPGQVIVIFGGATgrdgihgASFASEDLTGEKATKLSIQVG--DPFAEKMLIEAFL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 625 TAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVE---VPF------ALSQLFSESQSRFLVSVKPENEAAFAQLMEL 695
Cdd:PRK14090 222 EMVEEGLVEGAQDLGAGGVLSATSELVAKGGLGAIVHldrVPLrepdmePWEILISESQERMAVVTSPEKASRILEIAKK 301
|
250 260
....*....|....*....|....*.
gi 1071575466 696 EKVYR--LGVVTADETIRVKHKEDLV 719
Cdd:PRK14090 302 HLLFGdiVAEVIDDPIYRVMYRDDLV 327
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
266-377 |
6.03e-07 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 53.10 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 266 SDILVGIQDMGAAGLVSSSSEMASKAGAGLELimdDVPQRElhmTPYEMLLSESQErMLLCVKKGHVEEIQALFERYGLE 345
Cdd:PHA03366 866 EGLVVSGHDVSDGGLIACLAEMALAGGRGVTI---TVPAGE---DPLQFLFSETPG-VVIEVPPSHLSAVLTRLRSRNII 938
|
90 100 110
....*....|....*....|....*....|....*
gi 1071575466 346 AVVIGQV---TDDKMYKIIHHGEVVANVPVDALAE 377
Cdd:PHA03366 939 CYPIGTVgpsGPSNTFSVSHNGTVLFRESLSSLRS 973
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
73-352 |
1.35e-06 |
|
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: 50.60 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 73 VLQGPGEGAGIVDIGDGLGVafkVESHNH-PSYVE-PY-QG--AATGVggiIRDVFSMGARPIAMLNSLRFGELDTPHAK 147
Cdd:cd02195 36 VGLGTGDDAAVYRLPGGLAL---VQTTDFfPPIVDdPYlFGriAAANA---LSDIYAMGAKPLSALAIVTLPRKLPALQE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 148 YLVSEVVAGiagyGNSI----GIPTVGG------EIQFdpcytknplvnAMCV-GLIEAKDI------QKGQA----KGI 206
Cdd:cd02195 110 EVLREILAG----GKDKlreaGAVLVGGhtiegpEPKY-----------GLSVtGLVHPNKIlrnsgaKPGDVliltKPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 207 GNPVMYVGAKTGRdgIHGATFASVefSEEGEQ-QRSAVQvgdpFMEKLLLEACLDVirdhsdilVGIqdmgaaGLVSSSS 285
Cdd:cd02195 175 GTGILFAAEMAGL--ARGEDIDAA--LESMARlNRAAAE----LLRKYGAHACTDV--------TGF------GLLGHLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1071575466 286 EMASKAGAGLELIMDDVPqreLHMT--PyemllsesqerMLLCVKKGHVEEIQALFERYGLEAVVIGQV 352
Cdd:cd02195 233 EMARASGVSAEIDLDKLP---LLQTsgG-----------LLAAVPPEDAAALLALLKAGGPPAAIIGEV 287
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
101-350 |
7.53e-06 |
|
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: 48.36 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 101 HPSYVE--PYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGelDTPHAKylvsEVVAGIAGYGNSIGIPTVGGEIQFDPC 178
Cdd:cd02192 56 WPSLVEadPWWAGYCSVLVNVSDIAAMGGRPLAMVDALWSP--SAEAAA----QVLEGMRDAAEKFGVPIVGGHTHPDSP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 179 YtknplvNAMCVGLIeakdiqkGQAKGignPVMYV-GAKTGrDGIHGATFASVEFSEEGEQQRSAVQVGDPfmeklllea 257
Cdd:cd02192 130 Y------NALSVAIL-------GRARK---DLLISfGAKPG-DRLILAIDLDGRVHPSPPPNWDATTMKSP--------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 258 clDVIRDHSDILVGI---------QDMGAAGLVSSSSEMASKAGAGLELIMDDVP-------QRELHMTP-YEMLLSesq 320
Cdd:cd02192 184 --ALLRRQIALLPELaerglvhaaKDISNPGIIGTLGMLLEASGVGAEIDLDAIPrpegvdlERWLKCFPgFGFLLT--- 258
|
250 260 270
....*....|....*....|....*....|
gi 1071575466 321 ermllcVKKGHVEEIQALFERYGLEAVVIG 350
Cdd:cd02192 259 ------ARPENADEVVAVFAAVGITAAVIG 282
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
72-371 |
2.69e-04 |
|
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: 43.92 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 72 QVLQGPGEGAGIVDIGDGLGVAFKVES--------HNHPSYVePYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGElDT 143
Cdd:cd02691 22 ELIGKTGEVSIVAQDDDAGVDAADVEYivvaidgiHSRLSDF-PFLAGFHATRAALRDVMVMGARPVALLSDIHLAD-DG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 144 PHAKYLvsEVVAGIAGYGNSIGIPTVGG---EIQFDpCYTKNPLVNAM-CVGLIEAKDIQKGQAKGIGNPVMYVGAKTGR 219
Cdd:cd02691 100 DVGKLF--DFTAGVTAVSEATGVPLVAGstlRIGGD-MVLGDRLVGGVgAVGRSKSDPSRRKNAEPGDLILMTEGAGGGT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 220 DGIHGATFASVEFSEEgeqqrsAVQVGDpfmekllLEACLDVIRDHSDILV-GIQDMGAAGLVSSSSEMASKAGAGLELI 298
Cdd:cd02691 177 ITTTAIYHGMPDVVEE------TLNVDF-------IKACEALRDSGLVSKVhSMTDVTNGGIRGDALEISKTAGVSLVFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575466 299 MDDVpQRELHMTPYEML-------LSESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQVTDDKMYKIIHHGEVVANVP 371
Cdd:cd02691 244 EEKV-RSLINPKVLKMLeelgidpLGVSLDSLMIIAPEEDAVDIIRTLREAGVRADEVGRVEEGRGVPLVVTGEGRELKP 322
|
|
| |
