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Conserved domains on  [gi|256818825|ref|NP_057047|]
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peroxynitrite isomerase THAP4 isoform 1 [Homo sapiens]

Protein Classification

lipocalin/fatty acid-binding family protein; lipocalin family protein( domain architecture ID 10527263)

lipocalin/fatty acid-binding family protein contains a large beta-barrel cavity that binds hydrophobic ligands| lipocalin/fatty-acid binding family protein similar to Arabidopsis thaliana temperature-induced lipocalin-1, which is involved in basal (BT) and acquired thermotolerance (AT), probably by preventing plasma membrane lipids peroxidation induced by severe heat-shock (HS)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lipocalin_heme-bd-THAP4-like cd07828
heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar ...
 422-575 4.39e-61

heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins; Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


:

Pssm-ID: 381185  Cd Length: 150  Bit Score: 198.62  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825 422 VEPLSWMLGTWlsDPPGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPDTNKVAFVSAQ 501
Cdd:cd07828    1 LEPLSWLLGTW--RGSGKGGYPTIKDFSYGEEITFSHDGQPFLNYTARTWTLDTGKPMHRESGFLRIKPDGNKVELLIAH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256818825 502 NTGVVEVEEGEVNGQELCIASHSIARISFAkePHVEQITRKFRLNSEGKLEQTVSMATTTQPMTQHLHVTYKKV 575
Cdd:cd07828   79 NTGLVEIEEGEVTGNTLELTTDAVARTSFA--PEVTAIKRLFGLVDGNTLEYTVDMATAGKPLTPHLSARLKKV 150
THAP pfam05485
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ...
 5-85 5.89e-24

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: 95.68  E-value: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825    5 CAAVNCSNRQGKgeKRAVSFHRFPlKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRleDQHRLLKPTAVPSI 84
Cdd:pfam05485   1 CSVPGCTNRKKK--NPRTSFHKFP-KDPERRKKWLNACKRKDLPPPSNSYVCSLHFEENDFEKS--GGKRKLKPGAIPTL 75


                  .
gi 256818825   85 F 85
Cdd:pfam05485  76 F 76
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 78-440 4.09e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825   78 PTAVPSIFHLTEKKRGAGGHGRTRRKDASKATGGVRghSSAATSRGAA---GWSPSSSGNPMAKPESRRLKQAALQGEAT 154
Cdd:PHA03307  128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA--SDAASSRQAAlplSSPEETARAPSSPPAEPPPSTPPAAASPR 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  155 PRAAQEAASQEQaqqaleRTPGDGLATMVAGSQGKAEASATDAGDESATSSIEGGVTDKSGISMDDFTPPGSGAC-KFIG 233
Cdd:PHA03307  206 PPRRSSPISASA------SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGwNGPS 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  234 SLHSYSFSSKHTRERPSVPREPIDRKRLK----KDVEPSCSGSSLGPDKGLAQSPPSSSLTATPQKPSQ---SPSAPPAD 306
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPApsspRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSrspSPSRPPPP 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  307 VTPKPATEAVQSEHSDASPmsinevilSASGACKlidslhsycfSSRQNKSQVcclreqvekknGELKSLRQRVSRSDSQ 386
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSP--------AASAGRP----------TRRRARAAV-----------AGRARRRDATGRFPAG 410

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 256818825  387 VRKLQEKLDELRRVSVPYPSSLLSPSREPpkmnpvveplsWmlgtWLSDPPGAG 440
Cdd:PHA03307  411 RPRPSPLDAGAASGAFYARYPLLTPSGEP-----------W----PGSPPPPPG 449
 
Name Accession Description Interval E-value
lipocalin_heme-bd-THAP4-like cd07828
heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar ...
 422-575 4.39e-61

heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins; Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381185  Cd Length: 150  Bit Score: 198.62  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825 422 VEPLSWMLGTWlsDPPGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPDTNKVAFVSAQ 501
Cdd:cd07828    1 LEPLSWLLGTW--RGSGKGGYPTIKDFSYGEEITFSHDGQPFLNYTARTWTLDTGKPMHRESGFLRIKPDGNKVELLIAH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256818825 502 NTGVVEVEEGEVNGQELCIASHSIARISFAkePHVEQITRKFRLNSEGKLEQTVSMATTTQPMTQHLHVTYKKV 575
Cdd:cd07828   79 NTGLVEIEEGEVTGNTLELTTDAVARTSFA--PEVTAIKRLFGLVDGNTLEYTVDMATAGKPLTPHLSARLKKV 150
THAP4_heme-bd pfam08768
THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals ...
 422-574 1.07e-53

THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals and At1g79260 from Arabidopsis. THAP4 catalyzes the heme-based conversion of peroxynitrite into nitrate-NO3- in vitro. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport. This entry also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-beta-barrel structural organization. Proteins containing this domain are putatively related to fatty acid-binding proteins (FABPs).


Pssm-ID: 462593  Cd Length: 151  Bit Score: 179.31  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  422 VEPLSWMLGTWLSDppGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPDTNKVAFVSAQ 501
Cdd:pfam08768   2 LGPLAWLLGTWRGE--GEGGYPTIEDFTYGEEITFSHDGRPFLNYTSRTWRLDDGKPLHRETGFWRWEPGTGEVELVLAH 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818825  502 NT--GVVEVEEGEVNGQELCIASHSIARISFAKEphVEQITRKFRLNsEGKLEQTVSMATTTQPMTQHLHVTYKK 574
Cdd:pfam08768  80 PTgvVEIEEGTVKNGGNTIELATDAIARTSFAKE--VTAGKRLYGLV-DGDLSYTVDMATVGGPLQHHLSATLKR 151
THAP pfam05485
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ...
 5-85 5.89e-24

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: 95.68  E-value: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825    5 CAAVNCSNRQGKgeKRAVSFHRFPlKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRleDQHRLLKPTAVPSI 84
Cdd:pfam05485   1 CSVPGCTNRKKK--NPRTSFHKFP-KDPERRKKWLNACKRKDLPPPSNSYVCSLHFEENDFEKS--GGKRKLKPGAIPTL 75


                  .
gi 256818825   85 F 85
Cdd:pfam05485  76 F 76
THAP smart00980
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ...
 4-85 9.84e-24

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: 94.81  E-value: 9.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825     4 CCAAVNCSNRQGKGEKraVSFHRFPLKDSKRLIQWLKAVQRDN---WTPTKYSFLCSEHFTKDSFSKRledqHRLLKPTA 80
Cdd:smart00980   1 KCCVPGCGNRSKKNPG--LSFFRFPKEDPELRKKWLENLGLPDdpnRKPKKRSRICSRHFEPDDFDNS----GRRLKPGA 74


                   ....*
gi 256818825    81 VPSIF 85
Cdd:smart00980  75 VPTLF 79
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 78-440 4.09e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825   78 PTAVPSIFHLTEKKRGAGGHGRTRRKDASKATGGVRghSSAATSRGAA---GWSPSSSGNPMAKPESRRLKQAALQGEAT 154
Cdd:PHA03307  128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA--SDAASSRQAAlplSSPEETARAPSSPPAEPPPSTPPAAASPR 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  155 PRAAQEAASQEQaqqaleRTPGDGLATMVAGSQGKAEASATDAGDESATSSIEGGVTDKSGISMDDFTPPGSGAC-KFIG 233
Cdd:PHA03307  206 PPRRSSPISASA------SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGwNGPS 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  234 SLHSYSFSSKHTRERPSVPREPIDRKRLK----KDVEPSCSGSSLGPDKGLAQSPPSSSLTATPQKPSQ---SPSAPPAD 306
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPApsspRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSrspSPSRPPPP 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  307 VTPKPATEAVQSEHSDASPmsinevilSASGACKlidslhsycfSSRQNKSQVcclreqvekknGELKSLRQRVSRSDSQ 386
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSP--------AASAGRP----------TRRRARAAV-----------AGRARRRDATGRFPAG 410

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 256818825  387 VRKLQEKLDELRRVSVPYPSSLLSPSREPpkmnpvveplsWmlgtWLSDPPGAG 440
Cdd:PHA03307  411 RPRPSPLDAGAASGAFYARYPLLTPSGEP-----------W----PGSPPPPPG 449
 
Name Accession Description Interval E-value
lipocalin_heme-bd-THAP4-like cd07828
heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar ...
 422-575 4.39e-61

heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins; Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381185  Cd Length: 150  Bit Score: 198.62  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825 422 VEPLSWMLGTWlsDPPGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPDTNKVAFVSAQ 501
Cdd:cd07828    1 LEPLSWLLGTW--RGSGKGGYPTIKDFSYGEEITFSHDGQPFLNYTARTWTLDTGKPMHRESGFLRIKPDGNKVELLIAH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256818825 502 NTGVVEVEEGEVNGQELCIASHSIARISFAkePHVEQITRKFRLNSEGKLEQTVSMATTTQPMTQHLHVTYKKV 575
Cdd:cd07828   79 NTGLVEIEEGEVTGNTLELTTDAVARTSFA--PEVTAIKRLFGLVDGNTLEYTVDMATAGKPLTPHLSARLKKV 150
THAP4_heme-bd pfam08768
THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals ...
 422-574 1.07e-53

THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals and At1g79260 from Arabidopsis. THAP4 catalyzes the heme-based conversion of peroxynitrite into nitrate-NO3- in vitro. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport. This entry also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-beta-barrel structural organization. Proteins containing this domain are putatively related to fatty acid-binding proteins (FABPs).


Pssm-ID: 462593  Cd Length: 151  Bit Score: 179.31  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  422 VEPLSWMLGTWLSDppGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPDTNKVAFVSAQ 501
Cdd:pfam08768   2 LGPLAWLLGTWRGE--GEGGYPTIEDFTYGEEITFSHDGRPFLNYTSRTWRLDDGKPLHRETGFWRWEPGTGEVELVLAH 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818825  502 NT--GVVEVEEGEVNGQELCIASHSIARISFAKEphVEQITRKFRLNsEGKLEQTVSMATTTQPMTQHLHVTYKK 574
Cdd:pfam08768  80 PTgvVEIEEGTVKNGGNTIELATDAIARTSFAKE--VTAGKRLYGLV-DGDLSYTVDMATVGGPLQHHLSATLKR 151
THAP pfam05485
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ...
 5-85 5.89e-24

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: 95.68  E-value: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825    5 CAAVNCSNRQGKgeKRAVSFHRFPlKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRleDQHRLLKPTAVPSI 84
Cdd:pfam05485   1 CSVPGCTNRKKK--NPRTSFHKFP-KDPERRKKWLNACKRKDLPPPSNSYVCSLHFEENDFEKS--GGKRKLKPGAIPTL 75


                  .
gi 256818825   85 F 85
Cdd:pfam05485  76 F 76
THAP smart00980
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ...
 4-85 9.84e-24

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: 94.81  E-value: 9.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825     4 CCAAVNCSNRQGKGEKraVSFHRFPLKDSKRLIQWLKAVQRDN---WTPTKYSFLCSEHFTKDSFSKRledqHRLLKPTA 80
Cdd:smart00980   1 KCCVPGCGNRSKKNPG--LSFFRFPKEDPELRKKWLENLGLPDdpnRKPKKRSRICSRHFEPDDFDNS----GRRLKPGA 74


                   ....*
gi 256818825    81 VPSIF 85
Cdd:smart00980  75 VPTLF 79
DM3 smart00692
Zinc finger domain in CG10631, C. elegans LIN-15B and human P52rIPK;
24-85 1.01e-09

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


Pssm-ID: 128933  Cd Length: 59  Bit Score: 54.62  E-value: 1.01e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256818825    24 FHRFPlKDSKRLIQWLKAVQ-RDNWTPTKYSFLCSEHFTKDSFSKRledqhRLLKPTAVPSIF 85
Cdd:smart00692   1 LFRFP-KDPELLKKWEHNLRlSPDEKKLKNSRICSRHFEPECFGKR-----RRLKPGAVPTLE 57
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 78-440 4.09e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825   78 PTAVPSIFHLTEKKRGAGGHGRTRRKDASKATGGVRghSSAATSRGAA---GWSPSSSGNPMAKPESRRLKQAALQGEAT 154
Cdd:PHA03307  128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA--SDAASSRQAAlplSSPEETARAPSSPPAEPPPSTPPAAASPR 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  155 PRAAQEAASQEQaqqaleRTPGDGLATMVAGSQGKAEASATDAGDESATSSIEGGVTDKSGISMDDFTPPGSGAC-KFIG 233
Cdd:PHA03307  206 PPRRSSPISASA------SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGwNGPS 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  234 SLHSYSFSSKHTRERPSVPREPIDRKRLK----KDVEPSCSGSSLGPDKGLAQSPPSSSLTATPQKPSQ---SPSAPPAD 306
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPApsspRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSrspSPSRPPPP 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818825  307 VTPKPATEAVQSEHSDASPmsinevilSASGACKlidslhsycfSSRQNKSQVcclreqvekknGELKSLRQRVSRSDSQ 386
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSP--------AASAGRP----------TRRRARAAV-----------AGRARRRDATGRFPAG 410

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 256818825  387 VRKLQEKLDELRRVSVPYPSSLLSPSREPpkmnpvveplsWmlgtWLSDPPGAG 440
Cdd:PHA03307  411 RPRPSPLDAGAASGAFYARYPLLTPSGEP-----------W----PGSPPPPPG 449
 
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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