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Conserved domains on  [gi|444716890|gb|ELW57730|]
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Troponin I, slow skeletal muscle [Tupaia chinensis]

Protein Classification

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 ...
 157-288 7.37e-55

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: 175.45  E-value: 7.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  157 KLMLKSLMLAKAKECWEQEHEEREAEKARYLAERIPSLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREI 236
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 444716890  237 KDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVK 288
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
PTZ00335 super family cl30503
tubulin alpha chain; Provisional
 3-102 4.51e-20

tubulin alpha chain; Provisional


The actual alignment was detected with superfamily member PTZ00335:

Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 90.15  E-value: 4.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890   3 PYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNR---------------------------------P 41
Cdd:PTZ00335 184 PYNSVLSTHSLLEHTdvAVMLDNEAIYDicrrnlDIERPTYTNLNRliaqvissltaslrfdgalnvdltefqtnlvpyP 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  42 ----------------------LSAAEVTKTCLSP--------------------------------------------- 54
Cdd:PTZ00335 264 rihfmlssyapiisaekayheqLSVAEITNSAFEPanmmakcdprhgkymacclmyrgdvvpkdvnaaiatiktkrtiqf 343

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 444716890  55 ----PTRWR-----NVP--LPWGDLAKVQRAVCMLSDTRAIAEAWAHLDHEFDLVYAKQ 102
Cdd:PTZ00335 344 vdwcPTGFKcginyQPPtvVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKR 402
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 157-288 7.37e-55

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: 175.45  E-value: 7.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  157 KLMLKSLMLAKAKECWEQEHEEREAEKARYLAERIPSLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREI 236
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 444716890  237 KDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVK 288
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
 3-102 4.51e-20

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 90.15  E-value: 4.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890   3 PYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNR---------------------------------P 41
Cdd:PTZ00335 184 PYNSVLSTHSLLEHTdvAVMLDNEAIYDicrrnlDIERPTYTNLNRliaqvissltaslrfdgalnvdltefqtnlvpyP 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  42 ----------------------LSAAEVTKTCLSP--------------------------------------------- 54
Cdd:PTZ00335 264 rihfmlssyapiisaekayheqLSVAEITNSAFEPanmmakcdprhgkymacclmyrgdvvpkdvnaaiatiktkrtiqf 343

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 444716890  55 ----PTRWR-----NVP--LPWGDLAKVQRAVCMLSDTRAIAEAWAHLDHEFDLVYAKQ 102
Cdd:PTZ00335 344 vdwcPTGFKcginyQPPtvVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKR 402
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 3-108 3.03e-16

The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276955 [Multi-domain]  Cd Length: 434  Bit Score: 79.12  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890   3 PYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNR---------------------------------P 41
Cdd:cd02186  183 PYNSVLTTHSLLEHSdcSILLDNEALYDicrrqlDIERPTYTNLNRliaqvvssltaslrfdgalnvdlnefqtnlvpyP 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  42 ----------------------LSAAEVTKTCLSP--------------------------------------------- 54
Cdd:cd02186  263 rihfplvsyapiisaekanheqLSVQEITNSCFEPanqmvkcdprhgkymaccllyrgdvvpkdvnaaiatiktkrtiqf 342

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  55 ----PTRWR-------NVPLPWGDLAKVQRAVCMLSDTRAIAEAWAHLDHEFDLVYAKQ-----HLCTGM 108
Cdd:cd02186  343 vdwcPTGFKvginyqpPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRafvhwYVGEGM 412
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 157-288 7.37e-55

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: 175.45  E-value: 7.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  157 KLMLKSLMLAKAKECWEQEHEEREAEKARYLAERIPSLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREI 236
Cdd:pfam00992   1 KRLLKSLLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 444716890  237 KDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVK 288
Cdd:pfam00992  81 NDLKKKVNDLRGKFKKPLLKKVRKTADAMLKALLGSKHKVSMDFRANLKQVK 132
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
 3-102 4.51e-20

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 90.15  E-value: 4.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890   3 PYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNR---------------------------------P 41
Cdd:PTZ00335 184 PYNSVLSTHSLLEHTdvAVMLDNEAIYDicrrnlDIERPTYTNLNRliaqvissltaslrfdgalnvdltefqtnlvpyP 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  42 ----------------------LSAAEVTKTCLSP--------------------------------------------- 54
Cdd:PTZ00335 264 rihfmlssyapiisaekayheqLSVAEITNSAFEPanmmakcdprhgkymacclmyrgdvvpkdvnaaiatiktkrtiqf 343

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 444716890  55 ----PTRWR-----NVP--LPWGDLAKVQRAVCMLSDTRAIAEAWAHLDHEFDLVYAKQ 102
Cdd:PTZ00335 344 vdwcPTGFKcginyQPPtvVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKR 402
PLN00221 PLN00221
tubulin alpha chain; Provisional
 3-102 2.62e-18

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 85.25  E-value: 2.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890   3 PYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNR---------------------------------- 40
Cdd:PLN00221 184 PYNSVLSTHSLLEHTdvAVLLDNEAIYDicrrslDIERPTYTNLNRlisqvissltaslrfdgalnvditefqtnlvpyp 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  41 ---------------------PLSAAEVTKTCLSPPT-------------------RWRNVP------------------ 62
Cdd:PLN00221 264 rihfmlssyapvisaekayheQLSVAEITNSAFEPASmmakcdprhgkymacclmyRGDVVPkdvnaavatiktkrtiqf 343

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 444716890  63 -------------------LPWGDLAKVQRAVCMLSDTRAIAEAWAHLDHEFDLVYAKQ 102
Cdd:PLN00221 344 vdwcptgfkcginyqpptvVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKR 402
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 3-108 3.03e-16

The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276955 [Multi-domain]  Cd Length: 434  Bit Score: 79.12  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890   3 PYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNR---------------------------------P 41
Cdd:cd02186  183 PYNSVLTTHSLLEHSdcSILLDNEALYDicrrqlDIERPTYTNLNRliaqvvssltaslrfdgalnvdlnefqtnlvpyP 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  42 ----------------------LSAAEVTKTCLSP--------------------------------------------- 54
Cdd:cd02186  263 rihfplvsyapiisaekanheqLSVQEITNSCFEPanqmvkcdprhgkymaccllyrgdvvpkdvnaaiatiktkrtiqf 342

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444716890  55 ----PTRWR-------NVPLPWGDLAKVQRAVCMLSDTRAIAEAWAHLDHEFDLVYAKQ-----HLCTGM 108
Cdd:cd02186  343 vdwcPTGFKvginyqpPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRafvhwYVGEGM 412
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 2-45 2.84e-05

Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, gamma-, delta-, epsilon, and zeta-tubulins as well as FtsZ and CetZ, all of which are involved in polymer formation. Tubulin is the major component of microtubules, but also exists as a heterodimer and as a curved oligomer. Microtubules exist in all eukaryotic cells and are responsible for many functions, including cellular transport, cell motility, and mitosis. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria, archaea, and chloroplasts. A recent study found that CetZ proteins, formerly annotated FtsZ type 2, are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.


Pssm-ID: 276954 [Multi-domain]  Cd Length: 332  Bit Score: 45.09  E-value: 2.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 444716890   2 RPYNSILTTHTTLEHS--AFMEDNEAVYD------DSEHPAYTNLNRPLSAA 45
Cdd:cd00286  141 YPYNAALTLKTLTEHAdcLLLVDNEALYDicprplHIDAPAYDHINELVAQR 192
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 2-39 3.46e-03

The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology.


Pssm-ID: 276963 [Multi-domain]  Cd Length: 387  Bit Score: 38.72  E-value: 3.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 444716890   2 RPYNSILTTHTTLEHS--AFMEDNEAVYD---------DSEHPAYTNLN 39
Cdd:cd06059  142 SPYNSVLALNHLTEHAdcVLPIDNEALYDicnrqpatlDIDFPPFDDMN 190
 
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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