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Conserved domains on  [gi|1034575160|ref|XP_016873704|]
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troponin T, fast skeletal muscle isoform X15 [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 ...
47-183 2.85e-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: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  47 KRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 124
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034575160 125 DLKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLGEDKLRD 183
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 ...
47-183 2.85e-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: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  47 KRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 124
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034575160 125 DLKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLGEDKLRD 183
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-222 1.02e-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: 43.12  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160   37 EKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEK--------RRAERAEQQRIRAEKERERQNRLAE 108
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  109 EKARREEEDAKRRAEDDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLGEDKLRDKAKEL 188
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034575160  189 WETLHQLEIDKFEFGEKLKRQKYDITTLRSRIDQ 222
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
45-230 3.55e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  45 QKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 124
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160 125 DLKKKKAlssmganyssYLAKADQKRGKKQTAREMKKKILAERRKPLNIDhlgEDKLRDKAKELWETLHQLEIDKFEFGE 204
Cdd:COG1196   397 ELAAQLE----------ELEEAEEALLERLERLEEELEELEEALAELEEE---EEEEEEALEEAAEEEAELEEEEEALLE 463
                         170       180
                  ....*....|....*....|....*.
gi 1034575160 205 KLKRQKYDITTLRSRIDQAQKHSKKA 230
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEELAEA 489
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
36-122 7.48e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 37.41  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160   36 GEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVAlKERIEKRRAERAEQQRIRAEK-----------ERERQN 104
Cdd:PTZ00266   427 GGRVDKDHAERARIEKENAHRKALEMKILEKKRIERLEREE-RERLERERMERIERERLERERlererlerdrlERDRLD 505
                           90
                   ....*....|....*...
gi 1034575160  105 RLAEEKARREEEDAKRRA 122
Cdd:PTZ00266   506 RLERERVDRLERDRLEKA 523
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
47-183 2.85e-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: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  47 KRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAER--AEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 124
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlsAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034575160 125 DLKKKKALSSMGAnyssylAKADQKRGKKQTAREMKKKILAERRKpLNIDHLGEDKLRD 183
Cdd:pfam00992  81 NDLKKKVNDLRGK------FKKPLLKKVRKTADAMLKALLGSKHK-VSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-222 1.02e-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: 43.12  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160   37 EKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEK--------RRAERAEQQRIRAEKERERQNRLAE 108
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  109 EKARREEEDAKRRAEDDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLGEDKLRDKAKEL 188
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034575160  189 WETLHQLEIDKFEFGEKLKRQKYDITTLRSRIDQ 222
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
45-230 3.55e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160  45 QKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAED 124
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160 125 DLKKKKAlssmganyssYLAKADQKRGKKQTAREMKKKILAERRKPLNIDhlgEDKLRDKAKELWETLHQLEIDKFEFGE 204
Cdd:COG1196   397 ELAAQLE----------ELEEAEEALLERLERLEEELEELEEALAELEEE---EEEEEEALEEAAEEEAELEEEEEALLE 463
                         170       180
                  ....*....|....*....|....*.
gi 1034575160 205 KLKRQKYDITTLRSRIDQAQKHSKKA 230
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEELAEA 489
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
36-122 7.48e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 37.41  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575160   36 GEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVAlKERIEKRRAERAEQQRIRAEK-----------ERERQN 104
Cdd:PTZ00266   427 GGRVDKDHAERARIEKENAHRKALEMKILEKKRIERLEREE-RERLERERMERIERERLERERlererlerdrlERDRLD 505
                           90
                   ....*....|....*...
gi 1034575160  105 RLAEEKARREEEDAKRRA 122
Cdd:PTZ00266   506 RLERERVDRLERDRLEKA 523
 
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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