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Conserved domains on  [gi|568952846|ref|XP_006508651|]
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troponin T, fast skeletal muscle isoform X10 [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 ...
 58-194 3.34e-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: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 77.99  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846   58 KRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 135
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952846  136 DMKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLSDDKLRD 194
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 58-194 3.34e-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: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 77.99  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846   58 KRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 135
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952846  136 DMKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLSDDKLRD 194
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 56-233 7.48e-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: 7.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846    56 QKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEK-RRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAE 134
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846   135 DDMKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFG 214
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921

                          170
                   ....*....|....*....
gi 568952846   215 EKLKRQKYDITTLRSRIDQ 233
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-241 8.14e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.22  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846  56 QKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEd 135
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA- 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846 136 dmkkkkalssmgANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFGE 215
Cdd:COG1196  396 ------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        170       180
                 ....*....|....*....|....*.
gi 568952846 216 KLKRQKYDITTLRSRIDQAQKHSKKA 241
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEA 489
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 58-194 3.34e-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: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 77.99  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846   58 KRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 135
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952846  136 DMKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLSDDKLRD 194
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 56-233 7.48e-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: 7.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846    56 QKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEK-RRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAE 134
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846   135 DDMKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFG 214
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921

                          170
                   ....*....|....*....
gi 568952846   215 EKLKRQKYDITTLRSRIDQ 233
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-241 8.14e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.22  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846  56 QKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEd 135
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA- 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952846 136 dmkkkkalssmgANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFGE 215
Cdd:COG1196  396 ------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        170       180
                 ....*....|....*....|....*.
gi 568952846 216 KLKRQKYDITTLRSRIDQAQKHSKKA 241
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEA 489
 
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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