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Conserved domains on  [gi|1539581780|ref|NP_001354781|]
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troponin T, fast skeletal muscle isoform 12 [Homo sapiens]

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 ...
 1-130 3.67e-15

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: 68.74  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780   1 MELQALIDSHFEARKKEEEELVALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDDLKKKKA 78
Cdd:pfam00992   8 LLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLKKKV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539581780  79 LSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLGEDKLRD 130
Cdd:pfam00992  88 NDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 1-130 3.67e-15

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: 68.74  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780   1 MELQALIDSHFEARKKEEEELVALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDDLKKKKA 78
Cdd:pfam00992   8 LLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLKKKV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539581780  79 LSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLGEDKLRD 130
Cdd:pfam00992  88 NDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-169 6.34e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780    1 MELQALIDSHFEARKKEEEELVALKERIEK--------RRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDD 72
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780   73 LKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLGEDKLRDKAKELWETLHQLEIDKFEFGEK 152
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          170
                   ....*....|....*..
gi 1539581780  153 LKRQKYDITTLRSRIDQ 169
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDN 940
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 1-130 3.67e-15

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: 68.74  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780   1 MELQALIDSHFEARKKEEEELVALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDDLKKKKA 78
Cdd:pfam00992   8 LLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLKKKV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539581780  79 LSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLGEDKLRD 130
Cdd:pfam00992  88 NDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-169 6.34e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780    1 MELQALIDSHFEARKKEEEELVALKERIEK--------RRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDD 72
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539581780   73 LKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLGEDKLRDKAKELWETLHQLEIDKFEFGEK 152
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          170
                   ....*....|....*..
gi 1539581780  153 LKRQKYDITTLRSRIDQ 169
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDN 940
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 13-81 3.62e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 37.44  E-value: 3.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539581780  13 ARKKEEEelvalkerIEKrrAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAeddlkkkKALSS 81
Cdd:pfam03154 586 AKKREEA--------LEK--AKREAEQKAREEKEREKEKEKEREREREREREAERAA-------KASSS 637
 
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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