NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002095794|ref|NP_001307513|]
View 

transcriptional regulator QRICH1 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 10109286)

protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DUF3504 pfam12012
Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. ...
 599-759 1.93e-83

Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 156 to 173 amino acids in length.


:

Pssm-ID: 463430  Cd Length: 162  Bit Score: 262.20  E-value: 1.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095794 599 LPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKNPSnpkDKSTSIRYLKALGI-- 676
Cdd:pfam12012   1 VFSRVEEEHLWECKQLGAHSPIVLLNTLVYFNTKYFNLRTVEEHRRLSFSNVVRHTKPNPR---EKSTYLRYYEPPDQve 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095794 677 HQTGQKVTDD--MYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQML 754
Cdd:pfam12012  78 TGGRKKRDEGvnKVVEQHENSENPLRCPVKLYEFYLSKCPESVKQRKDVFYLQPEPSCVPDSPLWYSSQPLGRNTLESML 157


                  ....*
gi 1002095794 755 TRILV 759
Cdd:pfam12012 158 TRILL 162
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 6-45 3.54e-03

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 37.11  E-value: 3.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002095794   6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEF 45
Cdd:cd01671    24 KGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVF 63
 
Name Accession Description Interval E-value
DUF3504 pfam12012
Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. ...
 599-759 1.93e-83

Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 156 to 173 amino acids in length.


Pssm-ID: 463430  Cd Length: 162  Bit Score: 262.20  E-value: 1.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095794 599 LPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKNPSnpkDKSTSIRYLKALGI-- 676
Cdd:pfam12012   1 VFSRVEEEHLWECKQLGAHSPIVLLNTLVYFNTKYFNLRTVEEHRRLSFSNVVRHTKPNPR---EKSTYLRYYEPPDQve 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095794 677 HQTGQKVTDD--MYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQML 754
Cdd:pfam12012  78 TGGRKKRDEGvnKVVEQHENSENPLRCPVKLYEFYLSKCPESVKQRKDVFYLQPEPSCVPDSPLWYSSQPLGRNTLESML 157


                  ....*
gi 1002095794 755 TRILV 759
Cdd:pfam12012 158 TRILL 162
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 6-45 3.54e-03

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 37.11  E-value: 3.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002095794   6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEF 45
Cdd:cd01671    24 KGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVF 63
 
Name Accession Description Interval E-value
DUF3504 pfam12012
Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. ...
 599-759 1.93e-83

Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 156 to 173 amino acids in length.


Pssm-ID: 463430  Cd Length: 162  Bit Score: 262.20  E-value: 1.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095794 599 LPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKNPSnpkDKSTSIRYLKALGI-- 676
Cdd:pfam12012   1 VFSRVEEEHLWECKQLGAHSPIVLLNTLVYFNTKYFNLRTVEEHRRLSFSNVVRHTKPNPR---EKSTYLRYYEPPDQve 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095794 677 HQTGQKVTDD--MYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQML 754
Cdd:pfam12012  78 TGGRKKRDEGvnKVVEQHENSENPLRCPVKLYEFYLSKCPESVKQRKDVFYLQPEPSCVPDSPLWYSSQPLGRNTLESML 157


                  ....*
gi 1002095794 755 TRILV 759
Cdd:pfam12012 158 TRILL 162
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 6-45 3.54e-03

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 37.11  E-value: 3.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002095794   6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEF 45
Cdd:cd01671    24 KGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVF 63
 
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