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Conserved domains on  [gi|1720405487|ref|XP_030108742|]
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TSSK6-activating co-chaperone protein isoform X1 [Mus musculus]

Protein Classification

SSTK-IP domain-containing protein( domain architecture ID 11239432)

SSTK-IP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SSTK-IP pfam15836
SSTK-interacting protein, TSSK6-activating co-chaperone protein; SSTK-IP, SSTK-interacting ...
1-149 7.37e-66

SSTK-interacting protein, TSSK6-activating co-chaperone protein; SSTK-IP, SSTK-interacting protein or TSSK6-activating co-chaperone, is a family of proteins found in eukaryotes. SSTK-IP directly binds to HSP70, is found associated with HSP70 and HSP90 in cells, and facilitates HSP90-dependent enzymatic activation of SSTK. SSTK is a small serine/threonine kinase expressed post-meiotically and essential for male fertility along with two other serine threonine kinases. SSTK is one of the smallest protein kinases, consisting only of N- and C-lobes of a kinase catalytic domain, and forms stable associations with heat shock protein (HSP) 70 and 90. SSTK-IP, its interacting protein, thus represents the first germ cell-specific co-chaperone and protein kinase that requires the HSP90 machinery for catalytic activation.


:

Pssm-ID: 406308  Cd Length: 125  Bit Score: 196.36  E-value: 7.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405487   1 MEQHTSNPTKEKellyrpacpqtrnspatafpaaeltAKEEDSVACFCPAKSSPSYIDLPANFTPANFLTIQ-TKLSSGA 79
Cdd:pfam15836   1 MEQHTSNPTNEK-------------------------AKEEDNAVCLCRAKPSPSYINLQANSPPATFLNIQtTKLPSGA 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405487  80 GQKPKGCLGVLECMYANLQLQTQLAQRQIAILENLQASLSQPGSGRESKNCSLPGLCCKLLLNHLPQFHK 149
Cdd:pfam15836  56 GQKPKECLGLLECMYANLQLQTQLAQQQMAILENLQASLSQLAPGRESKNSSLPALCCNLLLNHLPQFHK 125
 
Name Accession Description Interval E-value
SSTK-IP pfam15836
SSTK-interacting protein, TSSK6-activating co-chaperone protein; SSTK-IP, SSTK-interacting ...
1-149 7.37e-66

SSTK-interacting protein, TSSK6-activating co-chaperone protein; SSTK-IP, SSTK-interacting protein or TSSK6-activating co-chaperone, is a family of proteins found in eukaryotes. SSTK-IP directly binds to HSP70, is found associated with HSP70 and HSP90 in cells, and facilitates HSP90-dependent enzymatic activation of SSTK. SSTK is a small serine/threonine kinase expressed post-meiotically and essential for male fertility along with two other serine threonine kinases. SSTK is one of the smallest protein kinases, consisting only of N- and C-lobes of a kinase catalytic domain, and forms stable associations with heat shock protein (HSP) 70 and 90. SSTK-IP, its interacting protein, thus represents the first germ cell-specific co-chaperone and protein kinase that requires the HSP90 machinery for catalytic activation.


Pssm-ID: 406308  Cd Length: 125  Bit Score: 196.36  E-value: 7.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405487   1 MEQHTSNPTKEKellyrpacpqtrnspatafpaaeltAKEEDSVACFCPAKSSPSYIDLPANFTPANFLTIQ-TKLSSGA 79
Cdd:pfam15836   1 MEQHTSNPTNEK-------------------------AKEEDNAVCLCRAKPSPSYINLQANSPPATFLNIQtTKLPSGA 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405487  80 GQKPKGCLGVLECMYANLQLQTQLAQRQIAILENLQASLSQPGSGRESKNCSLPGLCCKLLLNHLPQFHK 149
Cdd:pfam15836  56 GQKPKECLGLLECMYANLQLQTQLAQQQMAILENLQASLSQLAPGRESKNSSLPALCCNLLLNHLPQFHK 125
 
Name Accession Description Interval E-value
SSTK-IP pfam15836
SSTK-interacting protein, TSSK6-activating co-chaperone protein; SSTK-IP, SSTK-interacting ...
1-149 7.37e-66

SSTK-interacting protein, TSSK6-activating co-chaperone protein; SSTK-IP, SSTK-interacting protein or TSSK6-activating co-chaperone, is a family of proteins found in eukaryotes. SSTK-IP directly binds to HSP70, is found associated with HSP70 and HSP90 in cells, and facilitates HSP90-dependent enzymatic activation of SSTK. SSTK is a small serine/threonine kinase expressed post-meiotically and essential for male fertility along with two other serine threonine kinases. SSTK is one of the smallest protein kinases, consisting only of N- and C-lobes of a kinase catalytic domain, and forms stable associations with heat shock protein (HSP) 70 and 90. SSTK-IP, its interacting protein, thus represents the first germ cell-specific co-chaperone and protein kinase that requires the HSP90 machinery for catalytic activation.


Pssm-ID: 406308  Cd Length: 125  Bit Score: 196.36  E-value: 7.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405487   1 MEQHTSNPTKEKellyrpacpqtrnspatafpaaeltAKEEDSVACFCPAKSSPSYIDLPANFTPANFLTIQ-TKLSSGA 79
Cdd:pfam15836   1 MEQHTSNPTNEK-------------------------AKEEDNAVCLCRAKPSPSYINLQANSPPATFLNIQtTKLPSGA 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405487  80 GQKPKGCLGVLECMYANLQLQTQLAQRQIAILENLQASLSQPGSGRESKNCSLPGLCCKLLLNHLPQFHK 149
Cdd:pfam15836  56 GQKPKECLGLLECMYANLQLQTQLAQQQMAILENLQASLSQLAPGRESKNSSLPALCCNLLLNHLPQFHK 125
 
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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