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Conserved domains on  [gi|1907179325|ref|XP_036008790|]
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troponin T, fast skeletal muscle isoform X2 [Mus musculus]

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 ...
70-205 1.84e-18

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: 425977 [Multi-domain]  Cd Length: 132  Bit Score: 79.15  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325  70 KRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 147
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLDGlsAEQLQELCEELHERIDKLEEERYDLEEKVAKKDKEI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907179325 148 DMKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLSDDKLR 205
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPALKKVRKSADAMLKALLGSKHK-VSMDLRANLKQV 131
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
70-205 1.84e-18

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: 425977 [Multi-domain]  Cd Length: 132  Bit Score: 79.15  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325  70 KRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 147
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLDGlsAEQLQELCEELHERIDKLEEERYDLEEKVAKKDKEI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907179325 148 DMKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLSDDKLR 205
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPALKKVRKSADAMLKALLGSKHK-VSMDLRANLKQV 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-245 7.99e-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: 40.81  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325   68 QKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEK-RRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAE 146
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325  147 DDMKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFG 226
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
                          170
                   ....*....|....*....
gi 1907179325  227 EKLKRQKYDITTLRSRIDQ 245
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
70-205 1.84e-18

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: 425977 [Multi-domain]  Cd Length: 132  Bit Score: 79.15  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325  70 KRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 147
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLDGlsAEQLQELCEELHERIDKLEEERYDLEEKVAKKDKEI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907179325 148 DMKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLSDDKLR 205
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPALKKVRKSADAMLKALLGSKHK-VSMDLRANLKQV 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-245 7.99e-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: 40.81  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325   68 QKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEK-RRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAE 146
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179325  147 DDMKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFG 226
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
                          170
                   ....*....|....*....
gi 1907179325  227 EKLKRQKYDITTLRSRIDQ 245
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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