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Conserved domains on  [gi|169234719|ref|NP_919258|]
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protein lin-54 homolog isoform a [Homo sapiens]

Protein Classification

TCR domain-containing protein( domain architecture ID 13590193)

TCR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TCR pfam03638
Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two ...
 596-631 2.68e-20

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.


:

Pssm-ID: 461001  Cd Length: 38  Bit Score: 84.19  E-value: 2.68e-20
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 169234719  596 SKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKN 631
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVFCSSNCKCEGCKN 36
TCR pfam03638
Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two ...
 522-545 5.34e-10

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.


:

Pssm-ID: 461001  Cd Length: 38  Bit Score: 54.92  E-value: 5.34e-10
                          10        20
                  ....*....|....*....|....
gi 169234719  522 RKPCNCTKSLCLKLYCDCFANGEF 545
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVF 24
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 214-461 1.62e-03

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: 42.06  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  214 TQPSVLQTQQLKTVQIAKKPRTPT--SGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESG 291
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  292 VIGSTlnsTTQTPNKIAISPLKSP--NKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPgskfhyvrLVTATSA 369
Cdd:pfam03154 249 LQPMT---QPPPPSQVSPQPLPQPslHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVP--------PGPSPAA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  370 SSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPivsaqavkQVVPKPINPTSQIvTTSQPQQRLIMPATPLPQIQPn 449
Cdd:pfam03154 318 PGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP--------HIKPPPTTPIPQL-PNPQSHKHPPHLSGPSPFQMN- 387

                         250
                  ....*....|..
gi 169234719  450 lTNLPPGTVLAP 461
Cdd:pfam03154 388 -SNLPPPPALKP 398
 
Name Accession Description Interval E-value
TCR pfam03638
Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two ...
 596-631 2.68e-20

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.


Pssm-ID: 461001  Cd Length: 38  Bit Score: 84.19  E-value: 2.68e-20
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 169234719  596 SKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKN 631
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVFCSSNCKCEGCKN 36
TCR pfam03638
Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two ...
 522-545 5.34e-10

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.


Pssm-ID: 461001  Cd Length: 38  Bit Score: 54.92  E-value: 5.34e-10
                          10        20
                  ....*....|....*....|....
gi 169234719  522 RKPCNCTKSLCLKLYCDCFANGEF 545
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVF 24
MSL2_CXC cd13122
DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC ...
 596-631 3.17e-04

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.


Pssm-ID: 240555  Cd Length: 50  Bit Score: 38.91  E-value: 3.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 169234719 596 SKGCNCKRSG-------CLKNYCECYEAKIMCSSiCKCIGCKN 631
Cdd:cd13122    4 KKGCRCGTATqspgvltCRGQRCPCYSNGKSCLD-CKCRGCKN 45
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 214-461 1.62e-03

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: 42.06  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  214 TQPSVLQTQQLKTVQIAKKPRTPT--SGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESG 291
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  292 VIGSTlnsTTQTPNKIAISPLKSP--NKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPgskfhyvrLVTATSA 369
Cdd:pfam03154 249 LQPMT---QPPPPSQVSPQPLPQPslHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVP--------PGPSPAA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  370 SSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPivsaqavkQVVPKPINPTSQIvTTSQPQQRLIMPATPLPQIQPn 449
Cdd:pfam03154 318 PGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP--------HIKPPPTTPIPQL-PNPQSHKHPPHLSGPSPFQMN- 387

                         250
                  ....*....|..
gi 169234719  450 lTNLPPGTVLAP 461
Cdd:pfam03154 388 -SNLPPPPALKP 398
 
Name Accession Description Interval E-value
TCR pfam03638
Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two ...
 596-631 2.68e-20

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.


Pssm-ID: 461001  Cd Length: 38  Bit Score: 84.19  E-value: 2.68e-20
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 169234719  596 SKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKN 631
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVFCSSNCKCEGCKN 36
TCR pfam03638
Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two ...
 522-545 5.34e-10

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.


Pssm-ID: 461001  Cd Length: 38  Bit Score: 54.92  E-value: 5.34e-10
                          10        20
                  ....*....|....*....|....
gi 169234719  522 RKPCNCTKSLCLKLYCDCFANGEF 545
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVF 24
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 592-631 2.67e-04

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


Pssm-ID: 435512  Cd Length: 55  Bit Score: 39.34  E-value: 2.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 169234719  592 DRRHSKGCNCKRSG-------CLKNYCECYEAKIMCSSiCKCIGCKN 631
Cdd:pfam16682   1 KPPEKKGCRCGTSTptppkltCRNQRCPCYSNGKSCTD-CKCRGCKN 46
MSL2_CXC cd13122
DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC ...
 596-631 3.17e-04

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.


Pssm-ID: 240555  Cd Length: 50  Bit Score: 38.91  E-value: 3.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 169234719 596 SKGCNCKRSG-------CLKNYCECYEAKIMCSSiCKCIGCKN 631
Cdd:cd13122    4 KKGCRCGTATqspgvltCRGQRCPCYSNGKSCLD-CKCRGCKN 45
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 214-461 1.62e-03

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: 42.06  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  214 TQPSVLQTQQLKTVQIAKKPRTPT--SGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESG 291
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  292 VIGSTlnsTTQTPNKIAISPLKSP--NKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPgskfhyvrLVTATSA 369
Cdd:pfam03154 249 LQPMT---QPPPPSQVSPQPLPQPslHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVP--------PGPSPAA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234719  370 SSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPivsaqavkQVVPKPINPTSQIvTTSQPQQRLIMPATPLPQIQPn 449
Cdd:pfam03154 318 PGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP--------HIKPPPTTPIPQL-PNPQSHKHPPHLSGPSPFQMN- 387

                         250
                  ....*....|..
gi 169234719  450 lTNLPPGTVLAP 461
Cdd:pfam03154 388 -SNLPPPPALKP 398
 
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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