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Conserved domains on  [gi|2068748097|ref|XP_042213867|]
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troponin T, skeletal muscle-like isoform X4 [Homarus americanus]

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
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 96-157 3.64e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068748097  96 AKRKILRAEEEKklTEQKRSEEDRKMREETER-KQREQEEKRKRLEEAEKKRQSMMKGSSEDG 157
Cdd:pfam03154 581 AGSKLAKKREEA--LEKAKREAEQKAREEKEReKEKEKEREREREREREAERAAKASSSSHEG 641
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 173-247 3.95e-04

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: 40.24  E-value: 3.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068748097 173 QAAKGELGKTREQLAEEKKIALSIRVKPLNVDGIGSSSLRCKADEMWNLIIKLETEKYDMEERMKRQDYDLKELK 247
Cdd:pfam00992  10 QKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLK 84
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
25-145 6.20e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  25 QQVREEVKEKIREDAEEEERRKKGDEGANFLKNRQqmKMSELDEQLAEY----------IAEWRKQRSKEEDELKKLKeK 94
Cdd:COG2433   379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEE--EIRRLEEQVERLeaeveeleaeLEEKDERIERLERELSEAR-S 455

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2068748097  95 QAKRKILRAEEEKKLteQKRSEEDRKMREETERKQREQEEKRKRLEEAEKK 145
Cdd:COG2433   456 EERREIRKDREISRL--DREIERLERELEEERERIEELKRKLERLKELWKL 504
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 96-157 3.64e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068748097  96 AKRKILRAEEEKklTEQKRSEEDRKMREETER-KQREQEEKRKRLEEAEKKRQSMMKGSSEDG 157
Cdd:pfam03154 581 AGSKLAKKREEA--LEKAKREAEQKAREEKEReKEKEKEREREREREREAERAAKASSSSHEG 641
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 173-247 3.95e-04

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: 40.24  E-value: 3.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068748097 173 QAAKGELGKTREQLAEEKKIALSIRVKPLNVDGIGSSSLRCKADEMWNLIIKLETEKYDMEERMKRQDYDLKELK 247
Cdd:pfam00992  10 QKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLK 84
PTZ00121 PTZ00121
MAEBL; Provisional
 29-289 5.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097   29 EEVKEKIREDAEEEERRKKGDEGANFLKNRQQMKMSELDEQLAEYIAEWRK---------QRSKEEDELKKLKEKQAKRK 99
Cdd:PTZ00121  1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKkadeakkaaEAKKKADEAKKAEEAKKADE 1526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  100 ILRAEEEKKLTEQKRSEEDRKMRE--------------ETERKQREQEEKRKRLEEAEKKRQsMMKGSSEDGVKKFGSKG 165
Cdd:PTZ00121  1527 AKKAEEAKKADEAKKAEEKKKADElkkaeelkkaeekkKAEEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEEEK 1605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  166 GDKLSNIQAAKGELGKTREQLAEEKKIALSIRVKPLNVDGIGSSSLRCKADEMwNLIIKLETEKYDMEERMKRQDYDLKE 245
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE-NKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2068748097  246 LKERQKQQLRHKAQKRGLDPEALTGKHPPKIQTASKFERRTDRR 289
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
25-145 6.20e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  25 QQVREEVKEKIREDAEEEERRKKGDEGANFLKNRQqmKMSELDEQLAEY----------IAEWRKQRSKEEDELKKLKeK 94
Cdd:COG2433   379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEE--EIRRLEEQVERLeaeveeleaeLEEKDERIERLERELSEAR-S 455

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2068748097  95 QAKRKILRAEEEKKLteQKRSEEDRKMREETERKQREQEEKRKRLEEAEKK 145
Cdd:COG2433   456 EERREIRKDREISRL--DREIERLERELEEERERIEELKRKLERLKELWKL 504
PTZ00121 PTZ00121
MAEBL; Provisional
 29-155 6.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 6.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097   29 EEVKEKIREDAEEEERRKKG------DEGANFLKNRQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRKILR 102
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKaeelkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2068748097  103 --AEEEKKLTEQKRSEEDRKMREETERKQREQEEKRK----RLEEAEKKRQSMMKGSSE 155
Cdd:PTZ00121  1709 kkEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaeeaKKDEEEKKKIAHLKKEEE 1767
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-261 1.52e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  56 KNRQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRKilRAEEEKKLTEQKRSE-EDRKMREETERKQREQEE 134
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE--EAEEELEEAEAELAEaEEALLEAEAELAEAEEEL 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097 135 KRKRLEEAEKKRQSMMKGSSEDGVKKfgskggdKLSNIQAAKGELGKTREQLAEEKKIALSIRVKplnvdgigsssLRCK 214
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEE-------AEEALLERLERLEEELEELEEALAELEEEEEE-----------EEEA 443

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2068748097 215 ADEMWNLIIKLETEKYDMEERMKRQDYDLKELKERQKQQLRHKAQKR 261
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 96-157 3.64e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068748097  96 AKRKILRAEEEKklTEQKRSEEDRKMREETER-KQREQEEKRKRLEEAEKKRQSMMKGSSEDG 157
Cdd:pfam03154 581 AGSKLAKKREEA--LEKAKREAEQKAREEKEReKEKEKEREREREREREAERAAKASSSSHEG 641
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 78-136 2.70e-04

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.55  E-value: 2.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068748097  78 RKQRSKEEDELKKL--KEKQAKRKILRAEEEKKLTEQKRSEEDRKMREETERKQREQEEKR 136
Cdd:pfam07946 263 KKTREEEIEKIKKAaeEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKKEQRK 323
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 173-247 3.95e-04

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: 40.24  E-value: 3.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068748097 173 QAAKGELGKTREQLAEEKKIALSIRVKPLNVDGIGSSSLRCKADEMWNLIIKLETEKYDMEERMKRQDYDLKELK 247
Cdd:pfam00992  10 QKAAEELEFEQEKKEEEKLRYLAERIPPLRLRGLSAEQLQELCEELHERIDKLEEERYDIEEKVAKKDKEINDLK 84
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 94-147 4.21e-04

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 41.78  E-value: 4.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068748097  94 KQAKRKI--LRAEEEKKL---TEQKRSEEDRKMREETERKQREQ-------EEKRKRLEEAEKKRQ 147
Cdd:pfam07946 256 PEALKKAkkTREEEIEKIkkaAEEERAEEAQEKKEEAKKKEREEklaklspEEQRKYEEKERKKEQ 321
PTZ00121 PTZ00121
MAEBL; Provisional
 29-289 5.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097   29 EEVKEKIREDAEEEERRKKGDEGANFLKNRQQMKMSELDEQLAEYIAEWRK---------QRSKEEDELKKLKEKQAKRK 99
Cdd:PTZ00121  1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKkadeakkaaEAKKKADEAKKAEEAKKADE 1526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  100 ILRAEEEKKLTEQKRSEEDRKMRE--------------ETERKQREQEEKRKRLEEAEKKRQsMMKGSSEDGVKKFGSKG 165
Cdd:PTZ00121  1527 AKKAEEAKKADEAKKAEEKKKADElkkaeelkkaeekkKAEEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEEEK 1605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  166 GDKLSNIQAAKGELGKTREQLAEEKKIALSIRVKPLNVDGIGSSSLRCKADEMwNLIIKLETEKYDMEERMKRQDYDLKE 245
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE-NKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2068748097  246 LKERQKQQLRHKAQKRGLDPEALTGKHPPKIQTASKFERRTDRR 289
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
25-145 6.20e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  25 QQVREEVKEKIREDAEEEERRKKGDEGANFLKNRQqmKMSELDEQLAEY----------IAEWRKQRSKEEDELKKLKeK 94
Cdd:COG2433   379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEE--EIRRLEEQVERLeaeveeleaeLEEKDERIERLERELSEAR-S 455

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2068748097  95 QAKRKILRAEEEKKLteQKRSEEDRKMREETERKQREQEEKRKRLEEAEKK 145
Cdd:COG2433   456 EERREIRKDREISRL--DREIERLERELEEERERIEELKRKLERLKELWKL 504
PTZ00121 PTZ00121
MAEBL; Provisional
 29-155 6.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 6.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097   29 EEVKEKIREDAEEEERRKKG------DEGANFLKNRQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRKILR 102
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKaeelkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2068748097  103 --AEEEKKLTEQKRSEEDRKMREETERKQREQEEKRK----RLEEAEKKRQSMMKGSSE 155
Cdd:PTZ00121  1709 kkEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaeeaKKDEEEKKKIAHLKKEEE 1767
PTZ00121 PTZ00121
MAEBL; Provisional
 75-283 1.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097   75 AEWRKQRSKEEDELKKLKEKQAKRKILRAEEEKKLTEQKRSEEDRKMREETERKQ--REQEEKRKRLEEAEKKRQSMMKG 152
Cdd:PTZ00121  1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKA 1413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  153 SSEDGVKKFGSKGGDKLSNIQAAKGELGKTR-----EQLAEEKKIALSIRVKPlnVDGIGSSSLRCKADEMwnliIKLET 227
Cdd:PTZ00121  1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKkadeaKKKAEEAKKAEEAKKKA--EEAKKADEAKKKAEEA----KKADE 1487

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2068748097  228 EKYDMEERMKRQDYDLKELKERQKQQLRHKAQKRGLDPEALTGKHPPKIQTASKFE 283
Cdd:PTZ00121  1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-261 1.52e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  56 KNRQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRKilRAEEEKKLTEQKRSE-EDRKMREETERKQREQEE 134
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE--EAEEELEEAEAELAEaEEALLEAEAELAEAEEEL 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097 135 KRKRLEEAEKKRQSMMKGSSEDGVKKfgskggdKLSNIQAAKGELGKTREQLAEEKKIALSIRVKplnvdgigsssLRCK 214
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEE-------AEEALLERLERLEEELEELEEALAELEEEEEE-----------EEEA 443

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2068748097 215 ADEMWNLIIKLETEKYDMEERMKRQDYDLKELKERQKQQLRHKAQKR 261
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 74-192 1.57e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  74 IAEWRKQRSKEEDELKKL------KEKQAKRKILRAEEEKKLTEQKRSEEDRKMREETERKQR---EQEEK-RKRLEEAE 143
Cdd:PRK00409  504 IEEAKKLIGEDKEKLNELiasleeLERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlleEAEKEaQQAIKEAK 583

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2068748097 144 KKRQSMMKGSSEDGVKKfgsKGGDKLSNIQAAKGELGKTREQLAEEKKI 192
Cdd:PRK00409  584 KEADEIIKELRQLQKGG---YASVKAHELIEARKRLNKANEKKEKKKKK 629
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 57-147 1.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  57 NRQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRKILRAEEEKKLTEQKRSEEDRK-MREETERKQREQEEK 135
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAEL 328

                          90
                  ....*....|..
gi 2068748097 136 RKRLEEAEKKRQ 147
Cdd:COG1196   329 EEELEELEEELE 340
Caldesmon pfam02029
Caldesmon;
58-161 1.86e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  58 RQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKqaKRKILRAEEEKKlteqKRSEEDRKMREETERKQREQEEKRK 137
Cdd:pfam02029 252 ELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRR----KQEEAERKLREEEEKRRMKEEIERR 325

                          90       100
                  ....*....|....*....|....
gi 2068748097 138 RLEEAEkKRQSMMKGSSEDGVKKF 161
Cdd:pfam02029 326 RAEAAE-KRQKLPEDSSSEGKKPF 348
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 95-200 3.05e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 39.55  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  95 QAKRKIlRAEEEKKlteqKRSEEDRKMREE-TERKQREQEEKRKRLEEAEKKRQSMMKGSSEDGVKKFGSKGGDKLSNIQ 173
Cdd:PRK05035  433 QAKAEI-RAIEQEK----KKAEEAKARFEArQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507

                          90       100
                  ....*....|....*....|....*..
gi 2068748097 174 AAKGELGKTREQLAEEKKIALSIRVKP 200
Cdd:PRK05035  508 IKAGARPDNSAVIAAREARKAQARARQ 534
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 58-155 5.37e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.95  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  58 RQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRKILRAEEEKKLTEQKRSEEDRKMRE----ETERKQREQE 133
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREmervRLEEQERQQQ 461

                          90       100
                  ....*....|....*....|..
gi 2068748097 134 EKRKRLEEAEKKRQSMMKGSSE 155
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEK 483
Nop14 pfam04147
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ...
 79-169 5.55e-03

Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.


Pssm-ID: 461196  Cd Length: 835  Bit Score: 38.76  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  79 KQRSKEEDEL------KKLKE--------KQAKRKILRAEEEKKLTEQKRSEEDRKMRE--------ETERKQREQE--- 133
Cdd:pfam04147 182 RQKAKEEDEElreeldKELKDlrsllsgsKRPKPEQAKKPEEKPDRKKPDDDYDKLVRElafdkrakPSDRTKTEEElae 261

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2068748097 134 EKRKRLEEAEKKRQSMMKG----SSEDGVKKFGSKGGDKL 169
Cdd:pfam04147 262 EEKERLEKLEEERLRRMRGeedeEEEDGKKKKKHKSADDL 301
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 56-149 7.33e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  56 KNRQQMKMSELDEQLAEYIAEWRKQRSKEEDELKKLKEKQAKRK---ILRAEEEKKLTEQKRSEEDRKMREETERKQREQ 132
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERqkaIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561

                          90
                  ....*....|....*..
gi 2068748097 133 EEKRKRLEEAEKKRQSM 149
Cdd:pfam17380 562 TEERSRLEAMEREREMM 578
PRK12704 PRK12704
phosphodiesterase; Provisional
 51-151 8.06e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068748097  51 GANFLKNRQQMKMSELDEQLAEYIAEWRKqrskEEDELKKLKEKQAKRKI--LRAEEEKKLTEQ----KRSEEDRKMREE 124
Cdd:PRK12704   21 GYFVRKKIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIhkLRNEFEKELRERrnelQKLEKRLLQKEE 96

                          90       100
                  ....*....|....*....|....*..
gi 2068748097 125 TERKQREQEEKRKrlEEAEKKRQSMMK 151
Cdd:PRK12704   97 NLDRKLELLEKRE--EELEKKEKELEQ 121
 
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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