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Conserved domains on  [gi|386764361|ref|NP_001245653|]
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upheld, isoform N [Drosophila melanogaster]

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 ...
153-230 1.68e-05

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: 44.09  E-value: 1.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386764361  153 LGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLEERQKRQDYDLKELK 230
Cdd:pfam00992   7 LLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLK 84
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-243 1.46e-04

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  37 IKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEkqakrkvtrAEEEQKMAQRKKEEEERRVREAEEKKQREIEEK 116
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEE---------LEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361 117 RMRLEEAEKKRQAMLQAMKDKDkkgpNFTIAKKDAGLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLRE 196
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 386764361 197 KAQELWELIVKLETEKYDLEERQKRQDYDLKELKERQKQQLRHKALK 243
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
153-230 1.68e-05

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: 44.09  E-value: 1.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386764361  153 LGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLEERQKRQDYDLKELK 230
Cdd:pfam00992   7 LLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLK 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-243 1.46e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  37 IKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEkqakrkvtrAEEEQKMAQRKKEEEERRVREAEEKKQREIEEK 116
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEE---------LEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361 117 RMRLEEAEKKRQAMLQAMKDKDkkgpNFTIAKKDAGLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLRE 196
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 386764361 197 KAQELWELIVKLETEKYDLEERQKRQDYDLKELKERQKQQLRHKALK 243
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
PTZ00121 PTZ00121
MAEBL; Provisional
59-314 7.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361   59 RKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQ--REIEEKRMRLEEAEKKRQAMLQAMKD 136
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAA 1416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  137 KDKKGpnfTIAKKDAGLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLE 216
Cdd:PTZ00121 1417 KKKAD---EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  217 ERQKRQDYDLKELKERQKQQLRHKALKKGLDPEALTGKYPPKIQVASKYErrvDTRSYDDKKKLFEGGWDEISKDSNEKI 296
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKKAEELKKAEEKKKAEEAK 1570
                         250
                  ....*....|....*...
gi 386764361  297 WNEKKEQYTGRQKSKLPK 314
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKK 1588
 
Name Accession Description Interval E-value
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
153-230 1.68e-05

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: 44.09  E-value: 1.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386764361  153 LGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLEERQKRQDYDLKELK 230
Cdd:pfam00992   7 LLLQKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLK 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-243 1.46e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  37 IKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEkqakrkvtrAEEEQKMAQRKKEEEERRVREAEEKKQREIEEK 116
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEE---------LEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361 117 RMRLEEAEKKRQAMLQAMKDKDkkgpNFTIAKKDAGLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLRE 196
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 386764361 197 KAQELWELIVKLETEKYDLEERQKRQDYDLKELKERQKQQLRHKALK 243
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
PTZ00121 PTZ00121
MAEBL; Provisional
59-314 7.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361   59 RKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQ--REIEEKRMRLEEAEKKRQAMLQAMKD 136
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAA 1416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  137 KDKKGpnfTIAKKDAGLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLE 216
Cdd:PTZ00121 1417 KKKAD---EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764361  217 ERQKRQDYDLKELKERQKQQLRHKALKKGLDPEALTGKYPPKIQVASKYErrvDTRSYDDKKKLFEGGWDEISKDSNEKI 296
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKKAEELKKAEEKKKAEEAK 1570
                         250
                  ....*....|....*...
gi 386764361  297 WNEKKEQYTGRQKSKLPK 314
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKK 1588
 
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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