NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907089469|ref|XP_036013536|]
View 

putative Polycomb group protein ASXL2 isoform X7 [Mus musculus]

Protein Classification

ASXH and PHD_3 domain-containing protein( domain architecture ID 10621630)

ASXH and PHD_3 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
88-209 1.58e-38

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


:

Pssm-ID: 464041  Cd Length: 129  Bit Score: 140.12  E-value: 1.58e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469   88 RQMKRTKCADIDVETPDSILVNTNLRALINKHTFSVLPGDCQQRLLLLLPEVDRQVGPDGLMKLN--GSALNNEFFTSAA 165
Cdd:pfam13919    5 AQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTDDSRPalPSLRNNEFFRHAC 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907089469  166 QGWKERLSEGEFTPEMQVRIRQEIEKEK-KVELWKEQFFENYYGQ 209
Cdd:pfam13919   85 ARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
1182-1242 3.02e-27

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


:

Pssm-ID: 316444  Cd Length: 68  Bit Score: 105.75  E-value: 3.02e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469 1182 MNPSSHGQTIPVQTFPddNSIEDTP---------SKCYCRLKAMIMCKGCGAFCHDDCIGPSKLCVSCLV 1242
Cdd:pfam13922    1 QNPQQQQQHPLLQLAH--QSGENTPpgneathtaNKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
PHA03247 super family cl33720
large tegument protein UL36; Provisional
355-799 1.14e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  355 SKNAGLQKPIIKPVAeaSPLNPDMKMPPAtvtdqiqeslkRKSSLTDEEATSSWEKRP-------RITENRQHQQPFQVS 427
Cdd:PHA03247  2545 SDDAGDPPPPLPPAA--PPAAPDRSVPPP-----------RPAPRPSEPAVTSRARRPdappqsaRPRAPVDDRGDPRGP 2611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  428 PQPFLNRGDRVQVRkvPPLKIPVSRISPMLFSTSQVSPRARFPISITSPYRTGARTLADIKAKAQLVKAQKAAAAAAAAA 507
Cdd:PHA03247  2612 APPSPLPPDTHAPD--PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  508 AAAASVGGTIPGPGPGGGQSPREggeRKIAGGGSAGSDPVSTNGKGPTLELAGTGSRGGTRELLPCGPQ-----PETNMP 582
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAP---HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArparpPTTAGP 2766
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  583 GQAQPPGISGAQLQQTSSVPTGLASSGACTSVPLPAHIEISNSEKPNLHKATATAASPCHLQDPRScrlekALSPTGPPL 662
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-----SAQPTAPPP 2841
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  663 ISGASTVYFVADGTVEPKAGSNKNAPKPSALAKTTAPA--PLDMTSSPVTTASLEKLPVPQISGTATSTGSAPSSSTL-- 738
Cdd:PHA03247  2842 PPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPqp 2921
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089469  739 ---PAASSLKTPGTSANMNGPISRTSSSIPANNP--LVTQLLQGKDVPLEQILPKPLTKIEMKTVP 799
Cdd:PHA03247  2922 qppPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
88-209 1.58e-38

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 140.12  E-value: 1.58e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469   88 RQMKRTKCADIDVETPDSILVNTNLRALINKHTFSVLPGDCQQRLLLLLPEVDRQVGPDGLMKLN--GSALNNEFFTSAA 165
Cdd:pfam13919    5 AQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTDDSRPalPSLRNNEFFRHAC 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907089469  166 QGWKERLSEGEFTPEMQVRIRQEIEKEK-KVELWKEQFFENYYGQ 209
Cdd:pfam13919   85 ARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
1182-1242 3.02e-27

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 105.75  E-value: 3.02e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469 1182 MNPSSHGQTIPVQTFPddNSIEDTP---------SKCYCRLKAMIMCKGCGAFCHDDCIGPSKLCVSCLV 1242
Cdd:pfam13922    1 QNPQQQQQHPLLQLAH--QSGENTPpgneathtaNKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
355-799 1.14e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  355 SKNAGLQKPIIKPVAeaSPLNPDMKMPPAtvtdqiqeslkRKSSLTDEEATSSWEKRP-------RITENRQHQQPFQVS 427
Cdd:PHA03247  2545 SDDAGDPPPPLPPAA--PPAAPDRSVPPP-----------RPAPRPSEPAVTSRARRPdappqsaRPRAPVDDRGDPRGP 2611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  428 PQPFLNRGDRVQVRkvPPLKIPVSRISPMLFSTSQVSPRARFPISITSPYRTGARTLADIKAKAQLVKAQKAAAAAAAAA 507
Cdd:PHA03247  2612 APPSPLPPDTHAPD--PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  508 AAAASVGGTIPGPGPGGGQSPREggeRKIAGGGSAGSDPVSTNGKGPTLELAGTGSRGGTRELLPCGPQ-----PETNMP 582
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAP---HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArparpPTTAGP 2766
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  583 GQAQPPGISGAQLQQTSSVPTGLASSGACTSVPLPAHIEISNSEKPNLHKATATAASPCHLQDPRScrlekALSPTGPPL 662
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-----SAQPTAPPP 2841
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  663 ISGASTVYFVADGTVEPKAGSNKNAPKPSALAKTTAPA--PLDMTSSPVTTASLEKLPVPQISGTATSTGSAPSSSTL-- 738
Cdd:PHA03247  2842 PPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPqp 2921
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089469  739 ---PAASSLKTPGTSANMNGPISRTSSSIPANNP--LVTQLLQGKDVPLEQILPKPLTKIEMKTVP 799
Cdd:PHA03247  2922 qppPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
546-763 9.44e-03

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: 40.28  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  546 PVSTNgKGPTLELAGTGSRGGTRELlPCGPQPETNMPGQAQP-PGISGAQLqqTSSVPTGlASSGACTSVPLPAHIEI-S 623
Cdd:pfam05109  425 PESTT-TSPTLNTTGFAAPNTTTGL-PSSTHVPTNLTAPASTgPTVSTADV--TSPTPAG-TTSGASPVTPSPSPRDNgT 499
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  624 NSEKPNLHKATATAASPC-HLQDPRSCRLEKALSPTGPPLISGASTVyfvADGTVEPKAGSNKNA---PKPSALAKT--- 696
Cdd:pfam05109  500 ESKAPDMTSPTSAVTTPTpNATSPTPAVTTPTPNATSPTLGKTSPTS---AVTTPTPNATSPTPAvttPTPNATIPTlgk 576
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089469  697 TAPAPLDMTSSPVTTASLEKLPVPQISGTATSTGsapSSSTLPAASSLKTPGTSANMNGPISRTSSS 763
Cdd:pfam05109  577 TSPTSAVTTPTPNATSPTVGETSPQANTTNHTLG---GTSSTPVVTSPPKNATSAVTTGQHNITSSS 640
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
88-209 1.58e-38

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 140.12  E-value: 1.58e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469   88 RQMKRTKCADIDVETPDSILVNTNLRALINKHTFSVLPGDCQQRLLLLLPEVDRQVGPDGLMKLN--GSALNNEFFTSAA 165
Cdd:pfam13919    5 AQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTDDSRPalPSLRNNEFFRHAC 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907089469  166 QGWKERLSEGEFTPEMQVRIRQEIEKEK-KVELWKEQFFENYYGQ 209
Cdd:pfam13919   85 ARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
1182-1242 3.02e-27

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 105.75  E-value: 3.02e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469 1182 MNPSSHGQTIPVQTFPddNSIEDTP---------SKCYCRLKAMIMCKGCGAFCHDDCIGPSKLCVSCLV 1242
Cdd:pfam13922    1 QNPQQQQQHPLLQLAH--QSGENTPpgneathtaNKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
355-799 1.14e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  355 SKNAGLQKPIIKPVAeaSPLNPDMKMPPAtvtdqiqeslkRKSSLTDEEATSSWEKRP-------RITENRQHQQPFQVS 427
Cdd:PHA03247  2545 SDDAGDPPPPLPPAA--PPAAPDRSVPPP-----------RPAPRPSEPAVTSRARRPdappqsaRPRAPVDDRGDPRGP 2611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  428 PQPFLNRGDRVQVRkvPPLKIPVSRISPMLFSTSQVSPRARFPISITSPYRTGARTLADIKAKAQLVKAQKAAAAAAAAA 507
Cdd:PHA03247  2612 APPSPLPPDTHAPD--PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  508 AAAASVGGTIPGPGPGGGQSPREggeRKIAGGGSAGSDPVSTNGKGPTLELAGTGSRGGTRELLPCGPQ-----PETNMP 582
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAP---HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArparpPTTAGP 2766
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  583 GQAQPPGISGAQLQQTSSVPTGLASSGACTSVPLPAHIEISNSEKPNLHKATATAASPCHLQDPRScrlekALSPTGPPL 662
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-----SAQPTAPPP 2841
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  663 ISGASTVYFVADGTVEPKAGSNKNAPKPSALAKTTAPA--PLDMTSSPVTTASLEKLPVPQISGTATSTGSAPSSSTL-- 738
Cdd:PHA03247  2842 PPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPqp 2921
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089469  739 ---PAASSLKTPGTSANMNGPISRTSSSIPANNP--LVTQLLQGKDVPLEQILPKPLTKIEMKTVP 799
Cdd:PHA03247  2922 qppPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
546-763 9.44e-03

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: 40.28  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  546 PVSTNgKGPTLELAGTGSRGGTRELlPCGPQPETNMPGQAQP-PGISGAQLqqTSSVPTGlASSGACTSVPLPAHIEI-S 623
Cdd:pfam05109  425 PESTT-TSPTLNTTGFAAPNTTTGL-PSSTHVPTNLTAPASTgPTVSTADV--TSPTPAG-TTSGASPVTPSPSPRDNgT 499
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089469  624 NSEKPNLHKATATAASPC-HLQDPRSCRLEKALSPTGPPLISGASTVyfvADGTVEPKAGSNKNA---PKPSALAKT--- 696
Cdd:pfam05109  500 ESKAPDMTSPTSAVTTPTpNATSPTPAVTTPTPNATSPTLGKTSPTS---AVTTPTPNATSPTPAvttPTPNATIPTlgk 576
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089469  697 TAPAPLDMTSSPVTTASLEKLPVPQISGTATSTGsapSSSTLPAASSLKTPGTSANMNGPISRTSSS 763
Cdd:pfam05109  577 TSPTSAVTTPTPNATSPTVGETSPQANTTNHTLG---GTSSTPVVTSPPKNATSAVTTGQHNITSSS 640
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH