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Conserved domains on  [gi|392701623|gb|EIY94780|]
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hypothetical protein HMPREF1079_01255 [Bacteroides fragilis CL05T00C42]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PurM-like super family cl10019
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
29-370 4.34e-77

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.


The actual alignment was detected with superfamily member cd02196:

Pssm-ID: 471963 [Multi-domain]  Cd Length: 297  Bit Score: 240.07  E-value: 4.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  29 IFPQAFCKIIPDILGGDPEYCNIMHADGAGTKSSLAYMYwketgdlSVWKGIAQDALIMNIDDLLCVGAvDNILVSSTIG 108
Cdd:cd02196    1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEM-------GKHDTIGIDLVAMCVNDILCQGA-EPLFFLDYIA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 109 RNKLliPGEVISAIINGTDELLAELremgvGVYATGGETADVGDLVRTIIVDSTVTCRM--KRADVINNANIRPGDVIVG 186
Cdd:cd02196   73 TGKL--DPEVAAEIVKGIAEGCRQA-----GCALLGGETAEMPGVYAEGEYDLAGFAVGvvEKDKIIDGSKIKPGDVLIG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 187 LASHGQAtyekeynggmgSNGLTSARHDVFAKYLAEKYPEsydaavpeelvYSGGLKLtdtvegspidaGKLVLSPTRTY 266
Cdd:cd02196  146 LPSSGLH-----------SNGYSLVRKILFEEGLDYDDPE-----------PGLGKTL-----------GEELLTPTRIY 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 267 APVVKKLLDAlrPEIHGMVHCSGGAQT-KVLHFVGD-VRVVKDNLF-PVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVY 343
Cdd:cd02196  193 VKPILPLLEK--VLVKGMAHITGGGLPeNLPRVLPEgLGAVIDLGSwEIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLI 270
                        330       340
                 ....*....|....*....|....*..
gi 392701623 344 LSPEHAAEVIAISESFGIPAQIVGRIE 370
Cdd:cd02196  271 VSEEDADEVLEILEKLGEKAYVIGEVV 297
 
Name Accession Description Interval E-value
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
29-370 4.34e-77

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: 240.07  E-value: 4.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  29 IFPQAFCKIIPDILGGDPEYCNIMHADGAGTKSSLAYMYwketgdlSVWKGIAQDALIMNIDDLLCVGAvDNILVSSTIG 108
Cdd:cd02196    1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEM-------GKHDTIGIDLVAMCVNDILCQGA-EPLFFLDYIA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 109 RNKLliPGEVISAIINGTDELLAELremgvGVYATGGETADVGDLVRTIIVDSTVTCRM--KRADVINNANIRPGDVIVG 186
Cdd:cd02196   73 TGKL--DPEVAAEIVKGIAEGCRQA-----GCALLGGETAEMPGVYAEGEYDLAGFAVGvvEKDKIIDGSKIKPGDVLIG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 187 LASHGQAtyekeynggmgSNGLTSARHDVFAKYLAEKYPEsydaavpeelvYSGGLKLtdtvegspidaGKLVLSPTRTY 266
Cdd:cd02196  146 LPSSGLH-----------SNGYSLVRKILFEEGLDYDDPE-----------PGLGKTL-----------GEELLTPTRIY 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 267 APVVKKLLDAlrPEIHGMVHCSGGAQT-KVLHFVGD-VRVVKDNLF-PVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVY 343
Cdd:cd02196  193 VKPILPLLEK--VLVKGMAHITGGGLPeNLPRVLPEgLGAVIDLGSwEIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLI 270
                        330       340
                 ....*....|....*....|....*..
gi 392701623 344 LSPEHAAEVIAISESFGIPAQIVGRIE 370
Cdd:cd02196  271 VSEEDADEVLEILEKLGEKAYVIGEVV 297
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
55-379 1.28e-39

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 144.03  E-value: 1.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  55 DGAGTKSSLAYMywketgdLSVWKGIAQDALIMNIDDLLCVGA-----VDNILVSStigrnklLIPgEVISAIINGtdel 129
Cdd:COG0150   64 DGVGTKLKIAQA-------LDKHDTIGIDLVAMCVNDILVQGAeplffLDYIATGK-------LDP-EVAAAVVKG---- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 130 LAE-LREMGVGVyaTGGETA------DVG--DLVRTI--IVDstvtcrmkRADVINNANIRPGDVIVGLASHGqatyeke 198
Cdd:COG0150  125 IAEgCRQAGCAL--IGGETAempgmyAPGeyDLAGFAvgVVE--------KDKIIDGSRVKAGDVLIGLASSG------- 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 199 ynggMGSNGLTSARHdvfakyLAEKYPESYDAAVPEelvysGGLKLtdtvegspidaGKLVLSPTRTYAPVVKKLLDALR 278
Cdd:COG0150  188 ----LHSNGYSLVRK------ILEVAGLDLDDPVPE-----LGRTL-----------GEALLEPTRIYVKPVLALLKAVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 279 peIHGMVHCSGGAqtkvlhFVGDV-RVVKDNL--------FPVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVYLSPEHA 349
Cdd:COG0150  242 --VHGMAHITGGG------LPENLpRVLPEGLgavidrgsWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDA 313
                        330       340       350
                 ....*....|....*....|....*....|
gi 392701623 350 AEVIAISESFGIPAQIVGRIEESDKKELII 379
Cdd:COG0150  314 DAALALLKAAGETAYVIGEVVAGEGEGVVL 343
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
6-372 4.98e-35

phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273316 [Multi-domain]  Cd Length: 332  Bit Score: 131.30  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623    6 YMMRGVSASKEDvhNAIKNIDKGIFPQAFCKIIPDILG---------GDPEYCNIMHADGAGTKSSLAYMywketgdLSV 76
Cdd:TIGR00878   3 YADAGVDIDAGN--EAVKRIKSLVKKTRRPEVMGGLGGfaglfdlgdKYKEPVLVSGTDGVGTKLLVAEA-------MNK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623   77 WKGIAQDALIMNIDDLLCVGA-----VDNILVsstiGRnkllIPGEVISAIINGtdelLAELREMGvGVYATGGETADVG 151
Cdd:TIGR00878  74 HDTIGIDLVAMNVNDLLVQGAeplffLDYLAV----GK----LDPEVASQIVKG----IAEGCKQA-GCALVGGETAEMP 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  152 DLVRTIIVDSTVTC--RMKRADVINNANIRPGDVIVGLAShgqatyekeynGGMGSNGLTSARhdvfaKYLAEKYPESYD 229
Cdd:TIGR00878 141 GMYRGGHYDLAGTAvgVVEKDEIITGEKVKPGDVLIGLGS-----------SGIHSNGLSLVR-----KVLEDIAGLDYE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  230 AAVPEElvysgglkltdtveGSPIdaGKLVLSPTRTYapvVKKLLDALRP-EIHGMVHCSGGAQTKVLhfvgdVRVVKDN 308
Cdd:TIGR00878 205 DTPEEF--------------GKTL--GEELLEPTRIY---VKPILELIKSvIVHGLAHITGGGLLENI-----PRRLPDG 260
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392701623  309 L--------FPVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVYLSPEHAAEVIAISESFGIPAQIVGRIEES 372
Cdd:TIGR00878 261 LkavidmssWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYGEKAWVIGEVKKG 332
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
55-373 1.60e-20

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 92.18  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  55 DGAGTKSSLAYmywketgDLSVWKGIAQDALIMNIDDLLCVGAVDNILVSS-TIGRNKLLIPGEVISAIINGTDELLAEL 133
Cdd:PLN02557 104 DGVGTKLKLAF-------ETGIHDTIGIDLVAMSVNDIVTSGAKPLFFLDYfATSHLDVDLAEKVIKGIVDGCQQSDCAL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 134 remgvgvyaTGGETADVGDLVRTIIVDST--VTCRMKRADVINNANIRPGDVIVGLAShgqatyekeynGGMGSNGLTSA 211
Cdd:PLN02557 177 ---------LGGETAEMPGFYAEGEYDLSgfAVGSVKKDAVIDGKNIVAGDVLIGLPS-----------SGVHSNGFSLV 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 212 RHdVFAKylaekypesydaavpeelvysGGLKLTDTVEGSPIDAGKLVLSPTRTYapvVKKLLDAL-RPEIHGMVHCSGG 290
Cdd:PLN02557 237 RR-VLAK---------------------SGLSLKDQLPGASVTIGEALMAPTVIY---VKQVLDIIsKGGVKGIAHITGG 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 291 AQTKVLHFV---GDVRVVKDNLFPVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVYLSPEHAAEVIAISESfgiPAQIVG 367
Cdd:PLN02557 292 GFTDNIPRVfpkGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEEGAY---PAYRIG 368

                 ....*.
gi 392701623 368 RIEESD 373
Cdd:PLN02557 369 EVINGE 374
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
179-379 1.95e-13

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: 67.37  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  179 RPGDVIVGLASHGqatyekeynggMGSNGLTSARHDVFakylaekypESYDAAVPEelvysgglkltdtvegspidaGKL 258
Cdd:pfam02769   1 KPGDVLILLGSSG-----------LHGAGLSLSRKGLE---------DSGLAAVQL---------------------GDP 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  259 VLSPTRTYapvVKKLLDALRPEIHGMVHCSGGAQTKVLH---FVGDVRVVKDnlFPVPPLFRTIQEQSgtdwaEMYKVFN 335
Cdd:pfam02769  40 LLEPTLIY---VKLLLAALGGLVKAMHDITGGGLAGALAemaPASGVGAEID--LDKVPIFEELMLPL-----EMLLSEN 109
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392701623  336 MGhRLEVYLSPEHAAEVIAISESFGIPAQIVGRIEESDKKELII 379
Cdd:pfam02769 110 QG-RGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
 
Name Accession Description Interval E-value
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
29-370 4.34e-77

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: 240.07  E-value: 4.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  29 IFPQAFCKIIPDILGGDPEYCNIMHADGAGTKSSLAYMYwketgdlSVWKGIAQDALIMNIDDLLCVGAvDNILVSSTIG 108
Cdd:cd02196    1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEM-------GKHDTIGIDLVAMCVNDILCQGA-EPLFFLDYIA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 109 RNKLliPGEVISAIINGTDELLAELremgvGVYATGGETADVGDLVRTIIVDSTVTCRM--KRADVINNANIRPGDVIVG 186
Cdd:cd02196   73 TGKL--DPEVAAEIVKGIAEGCRQA-----GCALLGGETAEMPGVYAEGEYDLAGFAVGvvEKDKIIDGSKIKPGDVLIG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 187 LASHGQAtyekeynggmgSNGLTSARHDVFAKYLAEKYPEsydaavpeelvYSGGLKLtdtvegspidaGKLVLSPTRTY 266
Cdd:cd02196  146 LPSSGLH-----------SNGYSLVRKILFEEGLDYDDPE-----------PGLGKTL-----------GEELLTPTRIY 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 267 APVVKKLLDAlrPEIHGMVHCSGGAQT-KVLHFVGD-VRVVKDNLF-PVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVY 343
Cdd:cd02196  193 VKPILPLLEK--VLVKGMAHITGGGLPeNLPRVLPEgLGAVIDLGSwEIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLI 270
                        330       340
                 ....*....|....*....|....*..
gi 392701623 344 LSPEHAAEVIAISESFGIPAQIVGRIE 370
Cdd:cd02196  271 VSEEDADEVLEILEKLGEKAYVIGEVV 297
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
55-379 1.28e-39

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 144.03  E-value: 1.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  55 DGAGTKSSLAYMywketgdLSVWKGIAQDALIMNIDDLLCVGA-----VDNILVSStigrnklLIPgEVISAIINGtdel 129
Cdd:COG0150   64 DGVGTKLKIAQA-------LDKHDTIGIDLVAMCVNDILVQGAeplffLDYIATGK-------LDP-EVAAAVVKG---- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 130 LAE-LREMGVGVyaTGGETA------DVG--DLVRTI--IVDstvtcrmkRADVINNANIRPGDVIVGLASHGqatyeke 198
Cdd:COG0150  125 IAEgCRQAGCAL--IGGETAempgmyAPGeyDLAGFAvgVVE--------KDKIIDGSRVKAGDVLIGLASSG------- 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 199 ynggMGSNGLTSARHdvfakyLAEKYPESYDAAVPEelvysGGLKLtdtvegspidaGKLVLSPTRTYAPVVKKLLDALR 278
Cdd:COG0150  188 ----LHSNGYSLVRK------ILEVAGLDLDDPVPE-----LGRTL-----------GEALLEPTRIYVKPVLALLKAVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 279 peIHGMVHCSGGAqtkvlhFVGDV-RVVKDNL--------FPVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVYLSPEHA 349
Cdd:COG0150  242 --VHGMAHITGGG------LPENLpRVLPEGLgavidrgsWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDA 313
                        330       340       350
                 ....*....|....*....|....*....|
gi 392701623 350 AEVIAISESFGIPAQIVGRIEESDKKELII 379
Cdd:COG0150  314 DAALALLKAAGETAYVIGEVVAGEGEGVVL 343
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
6-372 4.98e-35

phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273316 [Multi-domain]  Cd Length: 332  Bit Score: 131.30  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623    6 YMMRGVSASKEDvhNAIKNIDKGIFPQAFCKIIPDILG---------GDPEYCNIMHADGAGTKSSLAYMywketgdLSV 76
Cdd:TIGR00878   3 YADAGVDIDAGN--EAVKRIKSLVKKTRRPEVMGGLGGfaglfdlgdKYKEPVLVSGTDGVGTKLLVAEA-------MNK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623   77 WKGIAQDALIMNIDDLLCVGA-----VDNILVsstiGRnkllIPGEVISAIINGtdelLAELREMGvGVYATGGETADVG 151
Cdd:TIGR00878  74 HDTIGIDLVAMNVNDLLVQGAeplffLDYLAV----GK----LDPEVASQIVKG----IAEGCKQA-GCALVGGETAEMP 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  152 DLVRTIIVDSTVTC--RMKRADVINNANIRPGDVIVGLAShgqatyekeynGGMGSNGLTSARhdvfaKYLAEKYPESYD 229
Cdd:TIGR00878 141 GMYRGGHYDLAGTAvgVVEKDEIITGEKVKPGDVLIGLGS-----------SGIHSNGLSLVR-----KVLEDIAGLDYE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  230 AAVPEElvysgglkltdtveGSPIdaGKLVLSPTRTYapvVKKLLDALRP-EIHGMVHCSGGAQTKVLhfvgdVRVVKDN 308
Cdd:TIGR00878 205 DTPEEF--------------GKTL--GEELLEPTRIY---VKPILELIKSvIVHGLAHITGGGLLENI-----PRRLPDG 260
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392701623  309 L--------FPVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVYLSPEHAAEVIAISESFGIPAQIVGRIEES 372
Cdd:TIGR00878 261 LkavidmssWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYGEKAWVIGEVKKG 332
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
55-373 1.60e-20

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 92.18  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  55 DGAGTKSSLAYmywketgDLSVWKGIAQDALIMNIDDLLCVGAVDNILVSS-TIGRNKLLIPGEVISAIINGTDELLAEL 133
Cdd:PLN02557 104 DGVGTKLKLAF-------ETGIHDTIGIDLVAMSVNDIVTSGAKPLFFLDYfATSHLDVDLAEKVIKGIVDGCQQSDCAL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 134 remgvgvyaTGGETADVGDLVRTIIVDST--VTCRMKRADVINNANIRPGDVIVGLAShgqatyekeynGGMGSNGLTSA 211
Cdd:PLN02557 177 ---------LGGETAEMPGFYAEGEYDLSgfAVGSVKKDAVIDGKNIVAGDVLIGLPS-----------SGVHSNGFSLV 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 212 RHdVFAKylaekypesydaavpeelvysGGLKLTDTVEGSPIDAGKLVLSPTRTYapvVKKLLDAL-RPEIHGMVHCSGG 290
Cdd:PLN02557 237 RR-VLAK---------------------SGLSLKDQLPGASVTIGEALMAPTVIY---VKQVLDIIsKGGVKGIAHITGG 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623 291 AQTKVLHFV---GDVRVVKDNLFPVPPLFRTIQEQSGTDWAEMYKVFNMGHRLEVYLSPEHAAEVIAISESfgiPAQIVG 367
Cdd:PLN02557 292 GFTDNIPRVfpkGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEEGAY---PAYRIG 368

                 ....*.
gi 392701623 368 RIEESD 373
Cdd:PLN02557 369 EVINGE 374
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
179-379 1.95e-13

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: 67.37  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  179 RPGDVIVGLASHGqatyekeynggMGSNGLTSARHDVFakylaekypESYDAAVPEelvysgglkltdtvegspidaGKL 258
Cdd:pfam02769   1 KPGDVLILLGSSG-----------LHGAGLSLSRKGLE---------DSGLAAVQL---------------------GDP 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392701623  259 VLSPTRTYapvVKKLLDALRPEIHGMVHCSGGAQTKVLH---FVGDVRVVKDnlFPVPPLFRTIQEQSgtdwaEMYKVFN 335
Cdd:pfam02769  40 LLEPTLIY---VKLLLAALGGLVKAMHDITGGGLAGALAemaPASGVGAEID--LDKVPIFEELMLPL-----EMLLSEN 109
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392701623  336 MGhRLEVYLSPEHAAEVIAISESFGIPAQIVGRIEESDKKELII 379
Cdd:pfam02769 110 QG-RGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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