NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|125628657|ref|NP_075552|]
View 

gamma-interferon-inducible lysosomal thiol reductase precursor [Mus musculus]

Protein Classification

GILT family protein( domain architecture ID 10505223)

gamma interferon inducible lysosomal thiol reductase (GILT) family protein similar to Homo sapiens GILT that is a lysosomal thiol reductase which can reduce protein disulfide bonds

EC:  1.8.-.-
Gene Ontology:  GO:0016671
PubMed:  10852914

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
GILT pfam03227
Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two ...
62-161 6.19e-38

Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two characterized human gamma-interferon-inducible lysosomal thiol reductase (GILT) sequences: Swiss:P13284 and Swiss:Q9UL08. It also contains several other eukaryotic putative proteins with similarity to GILT. The aligned region contains three conserved cysteine residues. In addition, the two GILT sequences possess a C-X(2)-C motif that is shared by some of the other sequences in the family. This motif is thought to be associated with disulphide bond reduction.


:

Pssm-ID: 460853  Cd Length: 102  Bit Score: 128.22  E-value: 6.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628657   62 SLYYESLCGACRYFLVRDLFPTW-LMVMEIMNITLVPYGNAQERNVSGTWEFTCQHGELECRLNMVEACLLDKLEK-EAA 139
Cdd:pfam03227   1 TVYYESLCPDSRRFITQQLLPTYrLKLQDIMDLTLVPFGKAKVNSSGSGWGFTCQHGPEECLGNKLQACAIKLLPDqDQA 80
                          90       100
                  ....*....|....*....|..
gi 125628657  140 FLTIVCMEEMDDMEKKLGPCLQ 161
Cdd:pfam03227  81 LPFIACMESSNDPDEAAEKCAE 102
 
Name Accession Description Interval E-value
GILT pfam03227
Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two ...
62-161 6.19e-38

Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two characterized human gamma-interferon-inducible lysosomal thiol reductase (GILT) sequences: Swiss:P13284 and Swiss:Q9UL08. It also contains several other eukaryotic putative proteins with similarity to GILT. The aligned region contains three conserved cysteine residues. In addition, the two GILT sequences possess a C-X(2)-C motif that is shared by some of the other sequences in the family. This motif is thought to be associated with disulphide bond reduction.


Pssm-ID: 460853  Cd Length: 102  Bit Score: 128.22  E-value: 6.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628657   62 SLYYESLCGACRYFLVRDLFPTW-LMVMEIMNITLVPYGNAQERNVSGTWEFTCQHGELECRLNMVEACLLDKLEK-EAA 139
Cdd:pfam03227   1 TVYYESLCPDSRRFITQQLLPTYrLKLQDIMDLTLVPFGKAKVNSSGSGWGFTCQHGPEECLGNKLQACAIKLLPDqDQA 80
                          90       100
                  ....*....|....*....|..
gi 125628657  140 FLTIVCMEEMDDMEKKLGPCLQ 161
Cdd:pfam03227  81 LPFIACMESSNDPDEAAEKCAE 102
 
Name Accession Description Interval E-value
GILT pfam03227
Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two ...
62-161 6.19e-38

Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two characterized human gamma-interferon-inducible lysosomal thiol reductase (GILT) sequences: Swiss:P13284 and Swiss:Q9UL08. It also contains several other eukaryotic putative proteins with similarity to GILT. The aligned region contains three conserved cysteine residues. In addition, the two GILT sequences possess a C-X(2)-C motif that is shared by some of the other sequences in the family. This motif is thought to be associated with disulphide bond reduction.


Pssm-ID: 460853  Cd Length: 102  Bit Score: 128.22  E-value: 6.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628657   62 SLYYESLCGACRYFLVRDLFPTW-LMVMEIMNITLVPYGNAQERNVSGTWEFTCQHGELECRLNMVEACLLDKLEK-EAA 139
Cdd:pfam03227   1 TVYYESLCPDSRRFITQQLLPTYrLKLQDIMDLTLVPFGKAKVNSSGSGWGFTCQHGPEECLGNKLQACAIKLLPDqDQA 80
                          90       100
                  ....*....|....*....|..
gi 125628657  140 FLTIVCMEEMDDMEKKLGPCLQ 161
Cdd:pfam03227  81 LPFIACMESSNDPDEAAEKCAE 102
 
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