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Conserved domains on  [gi|392887466|ref|NP_493240|]
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Gamma-interferon-inducible lysosomal thiol reductase [Caenorhabditis elegans]

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

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List of domain hits

 Name Accession Description Interval E-value
GILT pfam03227
Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two ...
 40-139 4.78e-23

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: 88.93  E-value: 4.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887466   40 EVFGISRCPDTSKFIHNQLVPFYQNykgNLSDglKLDFHAVPTGGHQV---DGKYVNRCLHGALECALNKLQMCSKKHIK 116
Cdd:pfam03227   1 TVYYESLCPDSRRFITQQLLPTYRL---KLQD--IMDLTLVPFGKAKVnssGSGWGFTCQHGPEECLGNKLQACAIKLLP 75

                          90       100
                  ....*....|....*....|....*.
gi 392887466  117 Q--DWLVTAGCIQG-KTAYSAGLKCL 139
Cdd:pfam03227  76 DqdQALPFIACMESsNDPDEAAEKCA 101
 
Name Accession Description Interval E-value
GILT pfam03227
Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two ...
 40-139 4.78e-23

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: 88.93  E-value: 4.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887466   40 EVFGISRCPDTSKFIHNQLVPFYQNykgNLSDglKLDFHAVPTGGHQV---DGKYVNRCLHGALECALNKLQMCSKKHIK 116
Cdd:pfam03227   1 TVYYESLCPDSRRFITQQLLPTYRL---KLQD--IMDLTLVPFGKAKVnssGSGWGFTCQHGPEECLGNKLQACAIKLLP 75

                          90       100
                  ....*....|....*....|....*.
gi 392887466  117 Q--DWLVTAGCIQG-KTAYSAGLKCL 139
Cdd:pfam03227  76 DqdQALPFIACMESsNDPDEAAEKCA 101
 
Name Accession Description Interval E-value
GILT pfam03227
Gamma interferon inducible lysosomal thiol reductase (GILT); This family includes the two ...
 40-139 4.78e-23

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: 88.93  E-value: 4.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887466   40 EVFGISRCPDTSKFIHNQLVPFYQNykgNLSDglKLDFHAVPTGGHQV---DGKYVNRCLHGALECALNKLQMCSKKHIK 116
Cdd:pfam03227   1 TVYYESLCPDSRRFITQQLLPTYRL---KLQD--IMDLTLVPFGKAKVnssGSGWGFTCQHGPEECLGNKLQACAIKLLP 75

                          90       100
                  ....*....|....*....|....*.
gi 392887466  117 Q--DWLVTAGCIQG-KTAYSAGLKCL 139
Cdd:pfam03227  76 DqdQALPFIACMESsNDPDEAAEKCA 101
 
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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