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Conserved domains on  [gi|967503364|ref|XP_014981922|]
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THAP domain-containing protein 11 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cc_THAP11_C cd22291
C-terminal coiled-coil domain of THAP domain-containing protein 11; THAP domain-containing ...
242-302 9.56e-36

C-terminal coiled-coil domain of THAP domain-containing protein 11; THAP domain-containing protein 11 (THAP11) is a cell cycle and cell growth regulator differentially expressed in cancer cells. It acts as a transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. This model corresponds to the C-terminal coiled-coil domain of THAP11, which is involved in protein dimerization.


:

Pssm-ID: 412087  Cd Length: 61  Bit Score: 123.05  E-value: 9.56e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967503364 242 SLSSGTTEEELLRKLNEQRDILALMEVKMKEMKGSIRHLRLTEAKLREELREKDRLLAMAV 302
Cdd:cd22291    1 SLSSGTTSEELLRKLNEQRDIIALMEVKMKEMKGSIRQLRVTEAKLREELREKDRLLSMAV 61
THAP smart00980
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ...
6-81 1.12e-18

The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes.


:

Pssm-ID: 214951  Cd Length: 80  Bit Score: 79.02  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967503364     6 CCVPGCYNNSHRDKALHFYTFPK-DAELRRLWLKNVSRAGvsgcFSTFQPTTGHRLCSVHFQGGRKTYTVR------VPT 78
Cdd:smart00980   2 CCVPGCGNRSKKNPGLSFFRFPKeDPELRKKWLENLGLPD----DPNRKPKKRSRICSRHFEPDDFDNSGRrlkpgaVPT 77

                   ...
gi 967503364    79 IFP 81
Cdd:smart00980  78 LFL 80
 
Name Accession Description Interval E-value
cc_THAP11_C cd22291
C-terminal coiled-coil domain of THAP domain-containing protein 11; THAP domain-containing ...
242-302 9.56e-36

C-terminal coiled-coil domain of THAP domain-containing protein 11; THAP domain-containing protein 11 (THAP11) is a cell cycle and cell growth regulator differentially expressed in cancer cells. It acts as a transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. This model corresponds to the C-terminal coiled-coil domain of THAP11, which is involved in protein dimerization.


Pssm-ID: 412087  Cd Length: 61  Bit Score: 123.05  E-value: 9.56e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967503364 242 SLSSGTTEEELLRKLNEQRDILALMEVKMKEMKGSIRHLRLTEAKLREELREKDRLLAMAV 302
Cdd:cd22291    1 SLSSGTTSEELLRKLNEQRDIIALMEVKMKEMKGSIRQLRVTEAKLREELREKDRLLSMAV 61
THAP smart00980
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ...
6-81 1.12e-18

The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes.


Pssm-ID: 214951  Cd Length: 80  Bit Score: 79.02  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967503364     6 CCVPGCYNNSHRDKALHFYTFPK-DAELRRLWLKNVSRAGvsgcFSTFQPTTGHRLCSVHFQGGRKTYTVR------VPT 78
Cdd:smart00980   2 CCVPGCGNRSKKNPGLSFFRFPKeDPELRKKWLENLGLPD----DPNRKPKKRSRICSRHFEPDDFDNSGRrlkpgaVPT 77

                   ...
gi 967503364    79 IFP 81
Cdd:smart00980  78 LFL 80
THAP pfam05485
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ...
6-80 2.18e-16

THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes.


Pssm-ID: 461662  Cd Length: 76  Bit Score: 72.57  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967503364    6 CCVPGCYNNSHRDKALHFYTFPKDAELRRLWLKNVSRAGvsgcfstFQPTTGHRLCSVHFQGG--RKTYTVR------VP 77
Cdd:pfam05485   1 CSVPGCTNRKKKNPRTSFHKFPKDPERRKKWLNACKRKD-------LPPPSNSYVCSLHFEENdfEKSGGKRklkpgaIP 73

                  ...
gi 967503364   78 TIF 80
Cdd:pfam05485  74 TLF 76
 
Name Accession Description Interval E-value
cc_THAP11_C cd22291
C-terminal coiled-coil domain of THAP domain-containing protein 11; THAP domain-containing ...
242-302 9.56e-36

C-terminal coiled-coil domain of THAP domain-containing protein 11; THAP domain-containing protein 11 (THAP11) is a cell cycle and cell growth regulator differentially expressed in cancer cells. It acts as a transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. This model corresponds to the C-terminal coiled-coil domain of THAP11, which is involved in protein dimerization.


Pssm-ID: 412087  Cd Length: 61  Bit Score: 123.05  E-value: 9.56e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967503364 242 SLSSGTTEEELLRKLNEQRDILALMEVKMKEMKGSIRHLRLTEAKLREELREKDRLLAMAV 302
Cdd:cd22291    1 SLSSGTTSEELLRKLNEQRDIIALMEVKMKEMKGSIRQLRVTEAKLREELREKDRLLSMAV 61
THAP smart00980
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ...
6-81 1.12e-18

The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes.


Pssm-ID: 214951  Cd Length: 80  Bit Score: 79.02  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967503364     6 CCVPGCYNNSHRDKALHFYTFPK-DAELRRLWLKNVSRAGvsgcFSTFQPTTGHRLCSVHFQGGRKTYTVR------VPT 78
Cdd:smart00980   2 CCVPGCGNRSKKNPGLSFFRFPKeDPELRKKWLENLGLPD----DPNRKPKKRSRICSRHFEPDDFDNSGRrlkpgaVPT 77

                   ...
gi 967503364    79 IFP 81
Cdd:smart00980  78 LFL 80
THAP pfam05485
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ...
6-80 2.18e-16

THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes.


Pssm-ID: 461662  Cd Length: 76  Bit Score: 72.57  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967503364    6 CCVPGCYNNSHRDKALHFYTFPKDAELRRLWLKNVSRAGvsgcfstFQPTTGHRLCSVHFQGG--RKTYTVR------VP 77
Cdd:pfam05485   1 CSVPGCTNRKKKNPRTSFHKFPKDPERRKKWLNACKRKD-------LPPPSNSYVCSLHFEENdfEKSGGKRklkpgaIP 73

                  ...
gi 967503364   78 TIF 80
Cdd:pfam05485  74 TLF 76
DM3 smart00692
Zinc finger domain in CG10631, C. elegans LIN-15B and human P52rIPK;
23-81 1.57e-12

Zinc finger domain in CG10631, C. elegans LIN-15B and human P52rIPK;


Pssm-ID: 128933  Cd Length: 59  Bit Score: 61.55  E-value: 1.57e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967503364    23 FYTFPKDAELRRLWLKNVsragvsGCFSTFQPTTGHRLCSVHFQ-----GGRKTYTVRVPTIFP 81
Cdd:smart00692   1 LFRFPKDPELLKKWEHNL------RLSPDEKKLKNSRICSRHFEpecfgKRRRLKPGAVPTLEL 58
 
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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