NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039736975|ref|XP_017169994|]
View 

RING finger protein 112 isoform X9 [Mus musculus]

Protein Classification

GBP domain-containing protein( domain architecture ID 10111037)

GBP domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 50-248 1.14e-46

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


:

Pssm-ID: 206650  Cd Length: 224  Bit Score: 162.11  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975  50 LARDTPVCLLAVLGEQHSGKSFLLDHLLSGLPSLESGDSGRPraegslpgirwgangLTRGIWMWSHPFLLGKeGKKVAV 129
Cdd:cd01851     1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQ---------------TTKGIWMWSDPFKDTD-GKKHAV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 130 FLVDTGDVMSPELS-KETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVH----VAEVMGKHYGMVPIQHLDLLVR 204
Cdd:cd01851    65 LLLDTEGTDGRERGeFENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFVVR 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039736975 205 DSSHHNKSGQGHVGDILQKLSGKYPKVQELL--LGKRARCYLLPAP 248
Cdd:cd01851   145 DFTGPTPLEGLDVTEKSETLIEELNKIWSSIrkPFTPITCFVLPHP 190
 
Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 50-248 1.14e-46

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 162.11  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975  50 LARDTPVCLLAVLGEQHSGKSFLLDHLLSGLPSLESGDSGRPraegslpgirwgangLTRGIWMWSHPFLLGKeGKKVAV 129
Cdd:cd01851     1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQ---------------TTKGIWMWSDPFKDTD-GKKHAV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 130 FLVDTGDVMSPELS-KETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVH----VAEVMGKHYGMVPIQHLDLLVR 204
Cdd:cd01851    65 LLLDTEGTDGRERGeFENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFVVR 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039736975 205 DSSHHNKSGQGHVGDILQKLSGKYPKVQELL--LGKRARCYLLPAP 248
Cdd:cd01851   145 DFTGPTPLEGLDVTEKSETLIEELNKIWSSIrkPFTPITCFVLPHP 190
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 51-273 4.10e-18

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460516  Cd Length: 260  Bit Score: 83.96  E-value: 4.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975  51 ARDTPVCLLAVLGEQHSGKSFLLDHLLsglpslesgdsgrpraeGSLPGIRWGAN--GLTRGIWMWSHPFllgKEGKKVA 128
Cdd:pfam02263  16 AITQPVVVVAIAGLYRTGKSFLMNFLA-----------------GKLTGFSLGGTveSETKGIWMWCVPH---PNKPKHT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 129 VFLVDT---GDVmspelSKETrVKLC----ALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMV------- 194
Cdd:pfam02263  76 LVLLDTeglGDV-----EKSD-NKNDawifALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRVadsadfv 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 195 -PIQHLDLLVRDSSHHNKSGQGHVG------DILQKLSGKYPKVQELLLGKRA--------RCYLLPAPerqwVNKDQAS 259
Cdd:pfam02263 150 sFFPDFVWTVRDFSLPLEADGGPITgdeyleNRLKLSQGQHEELQNFNLPRLCirsffpkrKCFLFDRP----GLKKALN 225

                         250
                  ....*....|....*.
gi 1039736975 260 PR--GNTEDDFSHHFR 273
Cdd:pfam02263 226 PQfeGLREDELDPEFQ 241
 
Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 50-248 1.14e-46

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 162.11  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975  50 LARDTPVCLLAVLGEQHSGKSFLLDHLLSGLPSLESGDSGRPraegslpgirwgangLTRGIWMWSHPFLLGKeGKKVAV 129
Cdd:cd01851     1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQ---------------TTKGIWMWSDPFKDTD-GKKHAV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 130 FLVDTGDVMSPELS-KETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVH----VAEVMGKHYGMVPIQHLDLLVR 204
Cdd:cd01851    65 LLLDTEGTDGRERGeFENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFVVR 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039736975 205 DSSHHNKSGQGHVGDILQKLSGKYPKVQELL--LGKRARCYLLPAP 248
Cdd:cd01851   145 DFTGPTPLEGLDVTEKSETLIEELNKIWSSIrkPFTPITCFVLPHP 190
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 51-273 4.10e-18

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460516  Cd Length: 260  Bit Score: 83.96  E-value: 4.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975  51 ARDTPVCLLAVLGEQHSGKSFLLDHLLsglpslesgdsgrpraeGSLPGIRWGAN--GLTRGIWMWSHPFllgKEGKKVA 128
Cdd:pfam02263  16 AITQPVVVVAIAGLYRTGKSFLMNFLA-----------------GKLTGFSLGGTveSETKGIWMWCVPH---PNKPKHT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 129 VFLVDT---GDVmspelSKETrVKLC----ALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMV------- 194
Cdd:pfam02263  76 LVLLDTeglGDV-----EKSD-NKNDawifALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRVadsadfv 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039736975 195 -PIQHLDLLVRDSSHHNKSGQGHVG------DILQKLSGKYPKVQELLLGKRA--------RCYLLPAPerqwVNKDQAS 259
Cdd:pfam02263 150 sFFPDFVWTVRDFSLPLEADGGPITgdeyleNRLKLSQGQHEELQNFNLPRLCirsffpkrKCFLFDRP----GLKKALN 225

                         250
                  ....*....|....*.
gi 1039736975 260 PR--GNTEDDFSHHFR 273
Cdd:pfam02263 226 PQfeGLREDELDPEFQ 241
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH