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Conserved domains on  [gi|110624770|ref|NP_001036070|]
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H-2 class II histocompatibility antigen gamma chain isoform 1 [Mus musculus]

Protein Classification

Kazal-type serine protease inhibitor family protein( domain architecture ID 10558261)

Kazal-type serine protease inhibitor family protein may function as a serine protease inhibitor; similar to SPARC-related modular calcium-binding protein

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 ...
1-112 2.08e-54

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: 171.52  E-value: 2.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624770    1 MDDQRDLISNHEQLPILGNRPREPERCSRGALYTGVSVLVALLLAGQATTAYFLYQQQGRLDKLTITSQNLQLESLRMKL 80
Cdd:pfam09307   1 EEQQRDLISNPSSEPVLNVRGGARSSLSRGAKITGLSILVALLIAGQAVTAYFVYQQKGQITKLTQTSQNLQLELLRMKL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 110624770   81 PKSAKPvsqMRMATPLLMRPMSMDNMLLGPVK 112
Cdd:pfam09307  81 PKPSKP---MRMAMPMNNMPLVMDYSDPAPSQ 109
MHCassoc_trimer pfam08831
Class II MHC-associated invariant chain trimerization domain; The class II associated ...
119-184 1.47e-36

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: 124.48  E-value: 1.47e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110624770  119 NMTQDHVMHLLTRSGPLE-YPQLKGTFPENLKHLKNSMDGVNWKIFESWMKQWLLFEMSKNSLEEKK 184
Cdd:pfam08831   1 NKTEDQVKHLLLRSDPLKkYPELNGSFLENLKHLKNTMDDEDWKNFESWMHQWLLFEMSKNPKEEEP 67
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
195-254 1.05e-20

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 83.28  E-value: 1.05e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110624770 195 KCQEEVSHIPA-----VYPGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGRH-NC 254
Cdd:cd00191    1 PCERERASALEslagpKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPpNC 66
 
Name Accession Description Interval E-value
MHC2-interact pfam09307
CLIP, MHC2 interacting; Members of this family are found in class II invariant ...
1-112 2.08e-54

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: 171.52  E-value: 2.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624770    1 MDDQRDLISNHEQLPILGNRPREPERCSRGALYTGVSVLVALLLAGQATTAYFLYQQQGRLDKLTITSQNLQLESLRMKL 80
Cdd:pfam09307   1 EEQQRDLISNPSSEPVLNVRGGARSSLSRGAKITGLSILVALLIAGQAVTAYFVYQQKGQITKLTQTSQNLQLELLRMKL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 110624770   81 PKSAKPvsqMRMATPLLMRPMSMDNMLLGPVK 112
Cdd:pfam09307  81 PKPSKP---MRMAMPMNNMPLVMDYSDPAPSQ 109
MHCassoc_trimer pfam08831
Class II MHC-associated invariant chain trimerization domain; The class II associated ...
119-184 1.47e-36

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: 124.48  E-value: 1.47e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110624770  119 NMTQDHVMHLLTRSGPLE-YPQLKGTFPENLKHLKNSMDGVNWKIFESWMKQWLLFEMSKNSLEEKK 184
Cdd:pfam08831   1 NKTEDQVKHLLLRSDPLKkYPELNGSFLENLKHLKNTMDDEDWKNFESWMHQWLLFEMSKNPKEEEP 67
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
195-254 1.05e-20

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 83.28  E-value: 1.05e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110624770 195 KCQEEVSHIPA-----VYPGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGRH-NC 254
Cdd:cd00191    1 PCERERASALEslagpKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPpNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
208-251 4.57e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 76.19  E-value: 4.57e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 110624770  208 PGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGR 251
Cdd:pfam00086  19 SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGG 62
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
213-256 2.62e-16

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 70.87  E-value: 2.62e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 110624770   213 PKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKS-RGRHNCSE 256
Cdd:smart00211   2 PQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTeGGDPDCPS 46
 
Name Accession Description Interval E-value
MHC2-interact pfam09307
CLIP, MHC2 interacting; Members of this family are found in class II invariant ...
1-112 2.08e-54

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: 171.52  E-value: 2.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624770    1 MDDQRDLISNHEQLPILGNRPREPERCSRGALYTGVSVLVALLLAGQATTAYFLYQQQGRLDKLTITSQNLQLESLRMKL 80
Cdd:pfam09307   1 EEQQRDLISNPSSEPVLNVRGGARSSLSRGAKITGLSILVALLIAGQAVTAYFVYQQKGQITKLTQTSQNLQLELLRMKL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 110624770   81 PKSAKPvsqMRMATPLLMRPMSMDNMLLGPVK 112
Cdd:pfam09307  81 PKPSKP---MRMAMPMNNMPLVMDYSDPAPSQ 109
MHCassoc_trimer pfam08831
Class II MHC-associated invariant chain trimerization domain; The class II associated ...
119-184 1.47e-36

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: 124.48  E-value: 1.47e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110624770  119 NMTQDHVMHLLTRSGPLE-YPQLKGTFPENLKHLKNSMDGVNWKIFESWMKQWLLFEMSKNSLEEKK 184
Cdd:pfam08831   1 NKTEDQVKHLLLRSDPLKkYPELNGSFLENLKHLKNTMDDEDWKNFESWMHQWLLFEMSKNPKEEEP 67
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
195-254 1.05e-20

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 83.28  E-value: 1.05e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110624770 195 KCQEEVSHIPA-----VYPGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGRH-NC 254
Cdd:cd00191    1 PCERERASALEslagpKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPpNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
208-251 4.57e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 76.19  E-value: 4.57e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 110624770  208 PGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGR 251
Cdd:pfam00086  19 SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGG 62
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
213-256 2.62e-16

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 70.87  E-value: 2.62e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 110624770   213 PKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKS-RGRHNCSE 256
Cdd:smart00211   2 PQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTeGGDPDCPS 46
 
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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