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Conserved domains on  [gi|698466949|ref|XP_009705059|]
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PREDICTED: troponin I, fast skeletal muscle [Cariama cristata]

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 ...
 47-177 5.07e-51

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: 161.58  E-value: 5.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698466949   47 RQHLKSAMLQLAATEIEKEAAAKEVEKQNYLAEHCPPLSLPG-SMQELQDLCRKLHAKIDSVDEERYDTEVKLQKTVKEL 125
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 698466949  126 EDLSQKLFDLRGKFKRPPLRRVRMSADAMLRALLGSKHKVCMDLRANLKQVK 177
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 ...
 47-177 5.07e-51

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: 161.58  E-value: 5.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698466949   47 RQHLKSAMLQLAATEIEKEAAAKEVEKQNYLAEHCPPLSLPG-SMQELQDLCRKLHAKIDSVDEERYDTEVKLQKTVKEL 125
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 698466949  126 EDLSQKLFDLRGKFKRPPLRRVRMSADAMLRALLGSKHKVCMDLRANLKQVK 177
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-141 1.79e-03

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: 38.88  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698466949    40 RRAATARRQHLKSAMLQLAATEIEKEAAAKEVEKQNYLAEhcpplSLPGSMQELQDLCRKLHAKIDSVDEERYDTEVKLQ 119
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-----SLAAEIEELEELIEELESELEALLNERASLEEALA 890

                           90       100
                   ....*....|....*....|..
gi 698466949   120 KTVKELEDLSQKLFDLRGKFKR 141
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSE 912
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 47-177 5.07e-51

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: 161.58  E-value: 5.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698466949   47 RQHLKSAMLQLAATEIEKEAAAKEVEKQNYLAEHCPPLSLPG-SMQELQDLCRKLHAKIDSVDEERYDTEVKLQKTVKEL 125
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGlSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 698466949  126 EDLSQKLFDLRGKFKRPPLRRVRMSADAMLRALLGSKHKVCMDLRANLKQVK 177
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-141 1.79e-03

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: 38.88  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698466949    40 RRAATARRQHLKSAMLQLAATEIEKEAAAKEVEKQNYLAEhcpplSLPGSMQELQDLCRKLHAKIDSVDEERYDTEVKLQ 119
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-----SLAAEIEELEELIEELESELEALLNERASLEEALA 890

                           90       100
                   ....*....|....*....|..
gi 698466949   120 KTVKELEDLSQKLFDLRGKFKR 141
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSE 912
 
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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