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Conserved domains on  [gi|170016069|ref|NP_060212|]
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zinc finger CCHC domain-containing protein 2 [Homo sapiens]

Protein Classification

zinc finger CCHC domain-containing protein( domain architecture ID 13063153)

zinc finger CCHC (ZCCHC) domain-containing protein contains a zinc knuckle or a zinc binding motif, CX2CX4HX4C, where X can be any amino acid, and may bind single-stranded RNA

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 ...
 676-1011 4.91e-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: 47.84  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   676 TGYGSVNQTVTVKPPVQIASLGNEngnlLEDPLNSPKYQHISFMPTlHCVMHNGAQKSEVVVPAPKPADGKTIGMLVPSP 755
Cdd:pfam03154  186 PPPPGTTQAATAGPTPSAPSVPPQ----GSPATSQPPNQTQSTAAP-HTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQ 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   756 VAISAIRESANSTPVGILGPTACTGESEKHLELLASPLPIPSTFL-----PHSSTPALHLTVQRLKLPPPQGSSEsctvn 830
Cdd:pfam03154  261 VSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQ----- 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   831 iPQQPPGSLSIASPNTAFIPIHNPGSFPGSPVATTDPiTKSASQVVGlnqmvPQIEGNTGTVPQPTNVKvvlPAAGLSAA 910
Cdd:pfam03154  336 -SQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQS-HKHPPHLSG-----PSPFQMNSNLPPPPALK---PLSSLSTH 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   911 QPPASYPLP------GSPLAAGvlPSQNSSVLSTAATSPQPASAGISQAQATVPPAVPTHTPGPAPSPSPALT------- 977
Cdd:pfam03154  406 HPPSAHPPPlqlmpqSQQLPPP--PAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITppsgppt 483

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 170016069   978 -----HSTAQSDSTSYISAVGNT-NANGTVVPPQQMGSGP 1011
Cdd:pfam03154  484 stssaMPGIQPPSSASVSSSGPVpAAVSCPLPPVQIKEEA 523
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 1133-1148 7.53e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


:

Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 7.53e-04
                           10
                   ....*....|....*.
gi 170016069  1133 CYNCGVSGHYAQDCKQ 1148
Cdd:pfam00098    3 CYNCGEPGHIARDCPK 18
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 363-461 4.09e-03

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


The actual alignment was detected with superfamily member cd06883:

Pssm-ID: 470617  Cd Length: 109  Bit Score: 38.11  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  363 QRKRADKYWEYTFKVNWSDLSVTT-VTKTHQELQEF---------LLKLPKELSSETFDKTILRALnqgslkrEERRHPD 432
Cdd:cd06883     9 KRYSPEKYYIYVVKVTRENQTEPSfVFRTFEEFQELhnklsllfpSLKLPSFPARVVLGRSHIKQV-------AERRKIE 81

                          90       100
                  ....*....|....*....|....*....
gi 170016069  433 LEPILRQLFSSSSQAfLQSQKVHSFFQSI 461
Cdd:cd06883    82 LNSYLKSLFNASPEV-AESDLVYTFFHPL 109
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 676-1011 4.91e-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: 47.84  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   676 TGYGSVNQTVTVKPPVQIASLGNEngnlLEDPLNSPKYQHISFMPTlHCVMHNGAQKSEVVVPAPKPADGKTIGMLVPSP 755
Cdd:pfam03154  186 PPPPGTTQAATAGPTPSAPSVPPQ----GSPATSQPPNQTQSTAAP-HTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQ 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   756 VAISAIRESANSTPVGILGPTACTGESEKHLELLASPLPIPSTFL-----PHSSTPALHLTVQRLKLPPPQGSSEsctvn 830
Cdd:pfam03154  261 VSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQ----- 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   831 iPQQPPGSLSIASPNTAFIPIHNPGSFPGSPVATTDPiTKSASQVVGlnqmvPQIEGNTGTVPQPTNVKvvlPAAGLSAA 910
Cdd:pfam03154  336 -SQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQS-HKHPPHLSG-----PSPFQMNSNLPPPPALK---PLSSLSTH 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   911 QPPASYPLP------GSPLAAGvlPSQNSSVLSTAATSPQPASAGISQAQATVPPAVPTHTPGPAPSPSPALT------- 977
Cdd:pfam03154  406 HPPSAHPPPlqlmpqSQQLPPP--PAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITppsgppt 483

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 170016069   978 -----HSTAQSDSTSYISAVGNT-NANGTVVPPQQMGSGP 1011
Cdd:pfam03154  484 stssaMPGIQPPSSASVSSSGPVpAAVSCPLPPVQIKEEA 523
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 791-962 1.25e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.07  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  791 SPLPIPSTFLPHSSTPALhlTVQRLKLPPPQGSSEScTVNIPQQPPGSLSIA-----SPNTAFIPIHNPGSFPGSPVATT 865
Cdd:PLN03209  385 SPIPTPPSSSPASSKSVD--AVAKPAEPDVVPSPGS-ASNVPEVEPAQVEAKktrplSPYARYEDLKPPTSPSPTAPTGV 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  866 DPITKSASQVVGLNQMVPQIEGNTGTVPQPTNVKVVLPAAGLSAAQPPASyPLPGSPLAAGVLPSQNSSVLSTAATSPQP 945
Cdd:PLN03209  462 SPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTS-PSPAAPVGKVAPSSTNEVVKVGNSAPPTA 540

                         170
                  ....*....|....*..
gi 170016069  946 ASAGISQAQATVPPAVP 962
Cdd:PLN03209  541 LADEQHHAQPKPRPLSP 557
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 1133-1148 7.53e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 7.53e-04
                           10
                   ....*....|....*.
gi 170016069  1133 CYNCGVSGHYAQDCKQ 1148
Cdd:pfam00098    3 CYNCGEPGHIARDCPK 18
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 1123-1146 2.03e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 39.79  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|....
gi 170016069 1123 SGPKKNGNVSCYNCGVSGHYAQDC 1146
Cdd:PTZ00368   70 EAPPGSGPRSCYNCGQTGHISREC 93
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
 363-461 4.09e-03

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 38.11  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  363 QRKRADKYWEYTFKVNWSDLSVTT-VTKTHQELQEF---------LLKLPKELSSETFDKTILRALnqgslkrEERRHPD 432
Cdd:cd06883     9 KRYSPEKYYIYVVKVTRENQTEPSfVFRTFEEFQELhnklsllfpSLKLPSFPARVVLGRSHIKQV-------AERRKIE 81

                          90       100
                  ....*....|....*....|....*....
gi 170016069  433 LEPILRQLFSSSSQAfLQSQKVHSFFQSI 461
Cdd:cd06883    82 LNSYLKSLFNASPEV-AESDLVYTFFHPL 109
ZnF_C2HC smart00343
zinc finger;
1133-1148 6.96e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.11  E-value: 6.96e-03
                            10
                    ....*....|....*.
gi 170016069   1133 CYNCGVSGHYAQDCKQ 1148
Cdd:smart00343    2 CYNCGKEGHIARDCPS 17
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 676-1011 4.91e-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: 47.84  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   676 TGYGSVNQTVTVKPPVQIASLGNEngnlLEDPLNSPKYQHISFMPTlHCVMHNGAQKSEVVVPAPKPADGKTIGMLVPSP 755
Cdd:pfam03154  186 PPPPGTTQAATAGPTPSAPSVPPQ----GSPATSQPPNQTQSTAAP-HTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQ 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   756 VAISAIRESANSTPVGILGPTACTGESEKHLELLASPLPIPSTFL-----PHSSTPALHLTVQRLKLPPPQGSSEsctvn 830
Cdd:pfam03154  261 VSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQ----- 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   831 iPQQPPGSLSIASPNTAFIPIHNPGSFPGSPVATTDPiTKSASQVVGlnqmvPQIEGNTGTVPQPTNVKvvlPAAGLSAA 910
Cdd:pfam03154  336 -SQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQS-HKHPPHLSG-----PSPFQMNSNLPPPPALK---PLSSLSTH 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   911 QPPASYPLP------GSPLAAGvlPSQNSSVLSTAATSPQPASAGISQAQATVPPAVPTHTPGPAPSPSPALT------- 977
Cdd:pfam03154  406 HPPSAHPPPlqlmpqSQQLPPP--PAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITppsgppt 483

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 170016069   978 -----HSTAQSDSTSYISAVGNT-NANGTVVPPQQMGSGP 1011
Cdd:pfam03154  484 stssaMPGIQPPSSASVSSSGPVpAAVSCPLPPVQIKEEA 523
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 756-1041 1.21e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.45  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   756 VAISAIRESANSTPV----GILGPTACTGesekhlelLASPLPIPSTFL-PHSSTPALhlTVQRLKLPPPQGSSESCTVN 830
Cdd:pfam05109  419 VIFSKAPESTTTSPTlnttGFAAPNTTTG--------LPSSTHVPTNLTaPASTGPTV--STADVTSPTPAGTTSGASPV 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   831 IPQQPP---GSLSIA----SPNTAfIPIHNPGSFPGSPVATTdPITKSASQVVGLNQMVPQIegntgTVPQPTNVKvvlP 903
Cdd:pfam05109  489 TPSPSPrdnGTESKApdmtSPTSA-VTTPTPNATSPTPAVTT-PTPNATSPTLGKTSPTSAV-----TTPTPNATS---P 558

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   904 AAGLSAAQPPASYPLPG--SPLAAGVLPSQNSSVLSTAATSPQPASAGISQAQATVPPAV---PTHTPGPAPSPSPALTH 978
Cdd:pfam05109  559 TPAVTTPTPNATIPTLGktSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVtspPKNATSAVTTGQHNITS 638

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170016069   979 STAQSDS--TSYISAV--GNTNANGTVVPPQQMGSGPCGscGRRCSCGTNGNLQLNSYYYPNPMPGP 1041
Cdd:pfam05109  639 SSTSSMSlrPSSISETlsPSTSDNSTSHMPLLTSAHPTG--GENITQVTPASTSTHHVSTSSPAPRP 703
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 791-962 1.25e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.07  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  791 SPLPIPSTFLPHSSTPALhlTVQRLKLPPPQGSSEScTVNIPQQPPGSLSIA-----SPNTAFIPIHNPGSFPGSPVATT 865
Cdd:PLN03209  385 SPIPTPPSSSPASSKSVD--AVAKPAEPDVVPSPGS-ASNVPEVEPAQVEAKktrplSPYARYEDLKPPTSPSPTAPTGV 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  866 DPITKSASQVVGLNQMVPQIEGNTGTVPQPTNVKVVLPAAGLSAAQPPASyPLPGSPLAAGVLPSQNSSVLSTAATSPQP 945
Cdd:PLN03209  462 SPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTS-PSPAAPVGKVAPSSTNEVVKVGNSAPPTA 540

                         170
                  ....*....|....*..
gi 170016069  946 ASAGISQAQATVPPAVP 962
Cdd:PLN03209  541 LADEQHHAQPKPRPLSP 557
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 738-997 5.60e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.80  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   738 PAPKPADGKTIGMLVPSPVAISAIRESANSTPVGILGPT-----ACTGESEKHLELLASPLPIPSTFLPHSSTPALHLTV 812
Cdd:pfam17823  100 PATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPseafsAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAA 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   813 QRLKLPPPQGSSESCTVNIPQQPPGSLSIASPNTAfipihnpgsfpgSPVATTDPITKSASQVVGLNQMVPQIEGNTGTV 892
Cdd:pfam17823  180 SSTTAASSTTAASSAPTTAASSAPATLTPARGIST------------AATATGHPAAGTALAAVGNSSPAAGTVTAAVGT 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069   893 PQPTNVKVVLPAAGLSAAQppASYPLPGSPLAAGVLPSQNSSVlSTAATSPQPASAgiSQAQAT---VPPAVPTHTPGPA 969
Cdd:pfam17823  248 VTPAALATLAAAAGTVASA--AGTINMGDPHARRLSPAKHMPS-DTMARNPAAPMG--AQAQGPiiqVSTDQPVHNTAGE 322

                          250       260       270
                   ....*....|....*....|....*....|.
gi 170016069   970 ---PSPSPALTHSTAQSDSTSYISAVGNTNA 997
Cdd:pfam17823  323 ptpSPSNTTLEPNTPKSVASTNLAVVTTTKA 353
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 1133-1148 7.53e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 7.53e-04
                           10
                   ....*....|....*.
gi 170016069  1133 CYNCGVSGHYAQDCKQ 1148
Cdd:pfam00098    3 CYNCGEPGHIARDCPK 18
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-1004 1.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  738 PAPKPAdGKTIGMLVPSPvaiSAIRESAN-STPVGILGPTACTGESEKHLELLASPLPIPSTFLPHSSTPALHLTVQRLK 816
Cdd:PHA03247 2573 PAPRPS-EPAVTSRARRP---DAPPQSARpRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP 2648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  817 LPPPQGSSESCTVNIPQQppgSLSIASPNTAFIPIHNPGsfPGSPVATTDPITKSASQVVGLNQMVPQIEGNTGTVPQPT 896
Cdd:PHA03247 2649 PERPRDDPAPGRVSRPRR---ARRLGRAAQASSPPQRPR--RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPP 2723

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  897 NvkvvlPAAGLSAAQPPASYPLPGSPLAAGVLPSQNSSVLSTAATSPQPASAGISQAQATVPPAVPTHTPGPAPSPSPAL 976
Cdd:PHA03247 2724 G-----PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL 2798

                         250       260       270
                  ....*....|....*....|....*....|..
gi 170016069  977 THSTAQSDSTSYI----SAVGNTNANGTVVPP 1004
Cdd:PHA03247 2799 PSPWDPADPPAAVlapaAALPPAASPAGPLPP 2830
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-963 1.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  738 PAPKPADGKTIGMlVPSPVAISAIRESANSTPVGILGPTACTGESEKHLEllASPLPIPSTFLPHSST-PALHLTVQRLK 816
Cdd:PHA03247 2706 PTPEPAPHALVSA-TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGP--ARPARPPTTAGPPAPApPAAPAAGPPRR 2782

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  817 LPPPQGSSESCTVNIPQQPPGSLSIASPNTAFIPIHNPGSFPGSPVATTDPITKSASQVVglNQMVPQIEGNTGTVPQ-- 894
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP--PGPPPPSLPLGGSVAPgg 2860

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  895 ------PTNVKVVLPAA-----GLSAAQPPASYPLPGSPLAAGVLPSQNSSVLSTAATSPQPASAGISQAQATVPPAVPT 963
Cdd:PHA03247 2861 dvrrrpPSRSPAAKPAAparppVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
PHA03247 PHA03247
large tegument protein UL36; Provisional
 818-967 1.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  818 PPPQGSSesctvniPQQPPGSLSIASPnTAFIPIHNPGSFPGSPVATTDPITKSASqvvglnqMVPQIEGNTGTVPQPTN 897
Cdd:PHA03247 2701 PPPPPPT-------PEPAPHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGP-------ATPGGPARPARPPTTAG 2765

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  898 VKVVLPAAGLSAAQPPASYPLPGSPLAAGVLPSQNSSVLSTAATSPQPASAGISQAQATVPPAVPTHTPG 967
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ 2835
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 1123-1146 2.03e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 39.79  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|....
gi 170016069 1123 SGPKKNGNVSCYNCGVSGHYAQDC 1146
Cdd:PTZ00368   70 EAPPGSGPRSCYNCGQTGHISREC 93
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
 363-461 4.09e-03

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 38.11  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  363 QRKRADKYWEYTFKVNWSDLSVTT-VTKTHQELQEF---------LLKLPKELSSETFDKTILRALnqgslkrEERRHPD 432
Cdd:cd06883     9 KRYSPEKYYIYVVKVTRENQTEPSfVFRTFEEFQELhnklsllfpSLKLPSFPARVVLGRSHIKQV-------AERRKIE 81

                          90       100
                  ....*....|....*....|....*....
gi 170016069  433 LEPILRQLFSSSSQAfLQSQKVHSFFQSI 461
Cdd:cd06883    82 LNSYLKSLFNASPEV-AESDLVYTFFHPL 109
ZnF_C2HC smart00343
zinc finger;
1133-1148 6.96e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.11  E-value: 6.96e-03
                            10
                    ....*....|....*.
gi 170016069   1133 CYNCGVSGHYAQDCKQ 1148
Cdd:smart00343    2 CYNCGKEGHIARDCPS 17
PHA03247 PHA03247
large tegument protein UL36; Provisional
 729-945 9.39e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 9.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  729 GAQKSEVVVPAPKPADGKTigmlVPSPVAISAIRESANSTPVGILGP--TACTGESEKHLELLASPLPI----------- 795
Cdd:PHA03247 2788 VASLSESRESLPSPWDPAD----PPAAVLAPAAALPPAASPAGPLPPptSAQPTAPPPPPGPPPPSLPLggsvapggdvr 2863

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170016069  796 ---PSTFLPHSSTPALHLTVQRLKLPPPQGSSESCTVNIPQQPPgslsiaspntafipihnpgsfPGSPVATTDPITKSA 872
Cdd:PHA03247 2864 rrpPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPER---------------------PPQPQAPPPPQPQPQ 2922

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170016069  873 SQVVGLNQMVPQIEGNTGTVPQPTNVKVVLPAAGLSAAQPPASYPLPGSPLAAGVLPSQNSSVLSTAATSPQP 945
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
 
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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