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Conserved domains on  [gi|564365414|ref|XP_006243806|]
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transcriptional regulator QRICH1 isoform X1 [Rattus norvegicus]

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

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List of domain hits

Name Accession Description Interval E-value
DUF3504 pfam12012
Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. ...
600-760 6.61e-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: 261.05  E-value: 6.61e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365414  600 LPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKspsNPKDKSTSIRYLKALGI-- 677
Cdd:pfam12012   1 VFSRVEEEHLWECKQLGAHSPIVLLNTLVYFNTKYFNLRTVEEHRRLSFSNVVRHTKP---NPREKSTYLRYYEPPDQve 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365414  678 HQTGQKVTDD--MYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQML 755
Cdd:pfam12012  78 TGGRKKRDEGvnKVVEQHENSENPLRCPVKLYEFYLSKCPESVKQRKDVFYLQPEPSCVPDSPLWYSSQPLGRNTLESML 157

                  ....*
gi 564365414  756 TRILV 760
Cdd:pfam12012 158 TRILL 162
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
6-48 2.64e-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: 37.50  E-value: 2.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564365414   6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQS 48
Cdd:cd01671   24 KGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEA 66
 
Name Accession Description Interval E-value
DUF3504 pfam12012
Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. ...
600-760 6.61e-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: 261.05  E-value: 6.61e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365414  600 LPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKspsNPKDKSTSIRYLKALGI-- 677
Cdd:pfam12012   1 VFSRVEEEHLWECKQLGAHSPIVLLNTLVYFNTKYFNLRTVEEHRRLSFSNVVRHTKP---NPREKSTYLRYYEPPDQve 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365414  678 HQTGQKVTDD--MYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQML 755
Cdd:pfam12012  78 TGGRKKRDEGvnKVVEQHENSENPLRCPVKLYEFYLSKCPESVKQRKDVFYLQPEPSCVPDSPLWYSSQPLGRNTLESML 157

                  ....*
gi 564365414  756 TRILV 760
Cdd:pfam12012 158 TRILL 162
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
6-48 2.64e-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: 37.50  E-value: 2.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564365414   6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQS 48
Cdd:cd01671   24 KGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEA 66
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
6-48 8.94e-03

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 36.00  E-value: 8.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564365414    6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQS 48
Cdd:pfam00619  28 KNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEA 70
 
Name Accession Description Interval E-value
DUF3504 pfam12012
Domain of unknown function (DUF3504); This presumed domain is functionally uncharacterized. ...
600-760 6.61e-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: 261.05  E-value: 6.61e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365414  600 LPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKspsNPKDKSTSIRYLKALGI-- 677
Cdd:pfam12012   1 VFSRVEEEHLWECKQLGAHSPIVLLNTLVYFNTKYFNLRTVEEHRRLSFSNVVRHTKP---NPREKSTYLRYYEPPDQve 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365414  678 HQTGQKVTDD--MYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQML 755
Cdd:pfam12012  78 TGGRKKRDEGvnKVVEQHENSENPLRCPVKLYEFYLSKCPESVKQRKDVFYLQPEPSCVPDSPLWYSSQPLGRNTLESML 157

                  ....*
gi 564365414  756 TRILV 760
Cdd:pfam12012 158 TRILL 162
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
6-48 2.64e-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: 37.50  E-value: 2.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564365414   6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQS 48
Cdd:cd01671   24 KGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEA 66
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
6-48 8.94e-03

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 36.00  E-value: 8.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564365414    6 ENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQS 48
Cdd:pfam00619  28 KNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEA 70
 
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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