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Conserved domains on  [gi|1395777166|ref|NP_001351012|]
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HLA class II histocompatibility antigen gamma chain isoform d [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MHC2-interact pfam09307
CLIP, MHC2 interacting; Members of this family are found in class II invariant ...
 17-126 7.81e-49

CLIP, MHC2 interacting; Members of this family are found in class II invariant chain-associated peptide (CLIP), and are required for association with class II major histocompatibility complex (MHC) in the MHC class II processing pathway.


:

Pssm-ID: 462750  Cd Length: 109  Bit Score: 154.95  E-value: 7.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395777166  17 MDDQRDLISNNEQLPMLGRRPGAPESkCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMK 96
Cdd:pfam09307   1 EEQQRDLISNPSSEPVLNVRGGARSS-LSRGAKITGLSILVALLIAGQAVTAYFVYQQKGQITKLTQTSQNLQLELLRMK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1395777166  97 LPKPPKPvskMRMATPLLMQALPMGALPQG 126
Cdd:pfam09307  80 LPKPSKP---MRMAMPMNNMPLVMDYSDPA 106
MHCassoc_trimer super family cl07439
Class II MHC-associated invariant chain trimerization domain; The class II associated ...
 128-182 3.20e-27

Class II MHC-associated invariant chain trimerization domain; The class II associated invariant chain peptide is required for folding and localization of MHC class II heterodimers. This domain is involved in trimerization of the ectoderm and interferes with DM/class II binding. The trimeric protein forms a cylindrical shape which is thought to be important for interactions between the invariant chain and class II molecules.


The actual alignment was detected with superfamily member pfam08831:

Pssm-ID: 462614  Cd Length: 69  Bit Score: 98.67  E-value: 3.20e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395777166 128 ADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPT 182
Cdd:pfam08831  14 SDPLKKYPELNGSFLENLKHLKNTMDDEDWKNFESWMHQWLLFEMSKNPKEEEPT 68
 
Name Accession Description Interval E-value
MHC2-interact pfam09307
CLIP, MHC2 interacting; Members of this family are found in class II invariant ...
 17-126 7.81e-49

CLIP, MHC2 interacting; Members of this family are found in class II invariant chain-associated peptide (CLIP), and are required for association with class II major histocompatibility complex (MHC) in the MHC class II processing pathway.


Pssm-ID: 462750  Cd Length: 109  Bit Score: 154.95  E-value: 7.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395777166  17 MDDQRDLISNNEQLPMLGRRPGAPESkCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMK 96
Cdd:pfam09307   1 EEQQRDLISNPSSEPVLNVRGGARSS-LSRGAKITGLSILVALLIAGQAVTAYFVYQQKGQITKLTQTSQNLQLELLRMK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1395777166  97 LPKPPKPvskMRMATPLLMQALPMGALPQG 126
Cdd:pfam09307  80 LPKPSKP---MRMAMPMNNMPLVMDYSDPA 106
MHCassoc_trimer pfam08831
Class II MHC-associated invariant chain trimerization domain; The class II associated ...
 128-182 3.20e-27

Class II MHC-associated invariant chain trimerization domain; The class II associated invariant chain peptide is required for folding and localization of MHC class II heterodimers. This domain is involved in trimerization of the ectoderm and interferes with DM/class II binding. The trimeric protein forms a cylindrical shape which is thought to be important for interactions between the invariant chain and class II molecules.


Pssm-ID: 462614  Cd Length: 69  Bit Score: 98.67  E-value: 3.20e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395777166 128 ADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPT 182
Cdd:pfam08831  14 SDPLKKYPELNGSFLENLKHLKNTMDDEDWKNFESWMHQWLLFEMSKNPKEEEPT 68
 
Name Accession Description Interval E-value
MHC2-interact pfam09307
CLIP, MHC2 interacting; Members of this family are found in class II invariant ...
 17-126 7.81e-49

CLIP, MHC2 interacting; Members of this family are found in class II invariant chain-associated peptide (CLIP), and are required for association with class II major histocompatibility complex (MHC) in the MHC class II processing pathway.


Pssm-ID: 462750  Cd Length: 109  Bit Score: 154.95  E-value: 7.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395777166  17 MDDQRDLISNNEQLPMLGRRPGAPESkCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMK 96
Cdd:pfam09307   1 EEQQRDLISNPSSEPVLNVRGGARSS-LSRGAKITGLSILVALLIAGQAVTAYFVYQQKGQITKLTQTSQNLQLELLRMK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1395777166  97 LPKPPKPvskMRMATPLLMQALPMGALPQG 126
Cdd:pfam09307  80 LPKPSKP---MRMAMPMNNMPLVMDYSDPA 106
MHCassoc_trimer pfam08831
Class II MHC-associated invariant chain trimerization domain; The class II associated ...
 128-182 3.20e-27

Class II MHC-associated invariant chain trimerization domain; The class II associated invariant chain peptide is required for folding and localization of MHC class II heterodimers. This domain is involved in trimerization of the ectoderm and interferes with DM/class II binding. The trimeric protein forms a cylindrical shape which is thought to be important for interactions between the invariant chain and class II molecules.


Pssm-ID: 462614  Cd Length: 69  Bit Score: 98.67  E-value: 3.20e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395777166 128 ADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPT 182
Cdd:pfam08831  14 SDPLKKYPELNGSFLENLKHLKNTMDDEDWKNFESWMHQWLLFEMSKNPKEEEPT 68
 
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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