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Conserved domains on  [gi|555976763|ref|XP_005900342|]
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PREDICTED: troponin I, slow skeletal muscle [Bos mutus]

Protein Classification

troponin( domain architecture ID 12013160)

troponin such as troponin I (TnI, inhibitory) and T (TnT, tropomyosin binding) subunits, which together with troponin C (TnC, Ca2+ binding) subunit, form the troponin complex that regulates Ca2+ induced muscle contraction

CATH:  1.20.5.350
Gene Ontology:  GO:0005861|GO:0003009
PubMed:  18154728

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 84-215 5.16e-52

Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). this Pfam contains members of the TnT subunit. Troponin is a complex of three proteins, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). The troponin complex regulates Ca++ induced muscle contraction. This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin.


:

Pssm-ID: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 165.43  E-value: 5.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555976763   84 KLLLSGLMLAKAKECWEQEHEEREAEKKRYLAERIPALQTRGLSLSALQDLCRDLHAKVEVVDEERYDIEAKCLHNTREI 163
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 555976763  164 KDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVK 215
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 84-215 5.16e-52

Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). this Pfam contains members of the TnT subunit. Troponin is a complex of three proteins, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). The troponin complex regulates Ca++ induced muscle contraction. This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin.


Pssm-ID: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 165.43  E-value: 5.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555976763   84 KLLLSGLMLAKAKECWEQEHEEREAEKKRYLAERIPALQTRGLSLSALQDLCRDLHAKVEVVDEERYDIEAKCLHNTREI 163
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 555976763  164 KDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVK 215
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 84-215 5.16e-52

Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). this Pfam contains members of the TnT subunit. Troponin is a complex of three proteins, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). The troponin complex regulates Ca++ induced muscle contraction. This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin.


Pssm-ID: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 165.43  E-value: 5.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555976763   84 KLLLSGLMLAKAKECWEQEHEEREAEKKRYLAERIPALQTRGLSLSALQDLCRDLHAKVEVVDEERYDIEAKCLHNTREI 163
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 555976763  164 KDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVK 215
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
 
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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