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Conserved domains on  [gi|156564384|ref|NP_001096065|]
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probable E3 ubiquitin-protein ligase DTX2 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DTC pfam18102
Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family ...
 480-614 1.56e-88

Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family of proteins which comprises five members (DTX1, 2, 3, 4, and 3L). This conserved C-terminal region of about 150 residues of the Deltex family, is preceded by a RING E3 ligase domain in four of the members. Crystal structure of the Deltex C-terminal (DTC) domain reveals a fold composed of a central beta-sheet lined with two long parallel alpha-helices.


:

Pssm-ID: 465650  Cd Length: 133  Bit Score: 270.52  E-value: 1.56e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  480 TGTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFTarGFPRQCYLPDNAQGRKVLELLKVAWKRR 559
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156564384  560 LIFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQGV 614
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133
RING-H2_DTX2 cd16672
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ...
 411-482 3.89e-47

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals.


:

Pssm-ID: 438334  Cd Length: 72  Bit Score: 159.99  E-value: 3.89e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384 411 DCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGT 482
Cdd:cd16672    1 DCIICMEKLSCASGYSDVSESKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKTGT 72
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 21-105 9.39e-25

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 97.80  E-value: 9.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384    21 VWEWQDGLGTWHPYSATVCSFIEQQFVQQKgqrfglgSLAHSIPLGQadpslaPYIIDLPSWTQFRQDTGTMRAVRRHLF 100
Cdd:smart00678   2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGK-------KLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTY 68


                   ....*
gi 156564384   101 PQHSA 105
Cdd:smart00678  69 SPYSK 73
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 110-181 1.10e-24

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 97.41  E-value: 1.10e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384   110 VVWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDLAPLGYNYTVNYTTHTQTNKTSSFCRSVRRQAGPPYP 181
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYS 72
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 166-394 2.55e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  166 SSFCRSVRRQAGPPY--PVTTIIAPPGHTGV-ACSCHQCLSGSRTGPVSGRYRHSMTNLPAYPVPQHPPHRTASVFGTHQ 242
Cdd:PHA03247 2677 SSPPQRPRRRAARPTvgSLTSLADPPPPPPTpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAR 2756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  243 -------AFAPYNKPSLSGARSAPRLNTTNAWGAAPPSLGSQPLYRSSLSHLGPQHLPPGSSTSGAvsasLPSGPSSSPG 315
Cdd:PHA03247 2757 parppttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA----SPAGPLPPPT 2832

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  316 SVPATVPMQMPKPSRVQQALAGMTsvlmsAIGLPVclSRAPqPTSPPASRLASKSHGSVKRLRKMSVKGAT---PKPEPE 392
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSV-----APGGDV--RRRP-PSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQ 2904


                  ..
gi 156564384  393 PE 394
Cdd:PHA03247 2905 PE 2906
 
Name Accession Description Interval E-value
DTC pfam18102
Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family ...
 480-614 1.56e-88

Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family of proteins which comprises five members (DTX1, 2, 3, 4, and 3L). This conserved C-terminal region of about 150 residues of the Deltex family, is preceded by a RING E3 ligase domain in four of the members. Crystal structure of the Deltex C-terminal (DTC) domain reveals a fold composed of a central beta-sheet lined with two long parallel alpha-helices.


Pssm-ID: 465650  Cd Length: 133  Bit Score: 270.52  E-value: 1.56e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  480 TGTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFTarGFPRQCYLPDNAQGRKVLELLKVAWKRR 559
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156564384  560 LIFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQGV 614
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133
Deltex_C cd09633
Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in ...
 481-613 1.11e-80

Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in the regulation of Notch signaling, and therefore may play roles in cell-to-cell communications that regulate mechanisms determining cell fate. They have a central RING-type zinc finger domain and contain a C-terminal domain, described here, that is also found in other domain architectures. Deltex-1 (DTX1) contains a RING finger and two WWE domains, indicating that it may be an E3 ubiquitin ligase. Human deltex 3-like, which contains an additional N-terminal domain (presumably with ubiquitin ligase activity) is also described as E3 ubiquitin-protein ligase DTX3L, B-lymphoma- and BAL-associated protein (BBAP), or rhysin-2. DTX3L mediates monoubiquitination of K91 of histone H4 in response to DNA damage.


Pssm-ID: 193607  Cd Length: 131  Bit Score: 250.18  E-value: 1.11e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384 481 GTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFtaRGFPRQCYLPDNAQGRKVLELLKVAWKRRL 560
Cdd:cd09633    1 GNQPPGTMTYHVIDTSLPGYEGCGTIVIVYNIPSGIQGPEHPGPGKPY--RGTPRIAYLPDNEEGRKVLRLLKKAFDRRL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156564384 561 IFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQG 613
Cdd:cd09633   79 IFTVGTSVTTGREDVVVWNGIHHKTSLTGGPSGHGYPDPTYLDRVLEELAAKG 131
RING-H2_DTX2 cd16672
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ...
 411-482 3.89e-47

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals.


Pssm-ID: 438334  Cd Length: 72  Bit Score: 159.99  E-value: 3.89e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384 411 DCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGT 482
Cdd:cd16672    1 DCIICMEKLSCASGYSDVSESKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKTGT 72
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 21-105 9.39e-25

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 97.80  E-value: 9.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384    21 VWEWQDGLGTWHPYSATVCSFIEQQFVQQKgqrfglgSLAHSIPLGQadpslaPYIIDLPSWTQFRQDTGTMRAVRRHLF 100
Cdd:smart00678   2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGK-------KLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTY 68


                   ....*
gi 156564384   101 PQHSA 105
Cdd:smart00678  69 SPYSK 73
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 110-181 1.10e-24

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 97.41  E-value: 1.10e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384   110 VVWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDLAPLGYNYTVNYTTHTQTNKTSSFCRSVRRQAGPPYP 181
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYS 72
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 21-97 2.07e-19

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 82.34  E-value: 2.07e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156564384   21 VWEWQDGLGTWHPYSATVCSFIEQQFvqQKGQRfglgslahSIPLGQADPSlAPYIIDLPSWTQFRQDTGTMRAVRR 97
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAY--QKGKP--------SVDLSITTAG-FPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 111-174 4.84e-19

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 81.19  E-value: 4.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156564384  111 VWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDL--APLGYNYTVNYTTHTQTNKTSSFCRSVRR 174
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
PHA03247 PHA03247
large tegument protein UL36; Provisional
 166-394 2.55e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  166 SSFCRSVRRQAGPPY--PVTTIIAPPGHTGV-ACSCHQCLSGSRTGPVSGRYRHSMTNLPAYPVPQHPPHRTASVFGTHQ 242
Cdd:PHA03247 2677 SSPPQRPRRRAARPTvgSLTSLADPPPPPPTpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAR 2756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  243 -------AFAPYNKPSLSGARSAPRLNTTNAWGAAPPSLGSQPLYRSSLSHLGPQHLPPGSSTSGAvsasLPSGPSSSPG 315
Cdd:PHA03247 2757 parppttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA----SPAGPLPPPT 2832

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  316 SVPATVPMQMPKPSRVQQALAGMTsvlmsAIGLPVclSRAPqPTSPPASRLASKSHGSVKRLRKMSVKGAT---PKPEPE 392
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSV-----APGGDV--RRRP-PSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQ 2904


                  ..
gi 156564384  393 PE 394
Cdd:PHA03247 2905 PE 2906
 
Name Accession Description Interval E-value
DTC pfam18102
Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family ...
 480-614 1.56e-88

Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family of proteins which comprises five members (DTX1, 2, 3, 4, and 3L). This conserved C-terminal region of about 150 residues of the Deltex family, is preceded by a RING E3 ligase domain in four of the members. Crystal structure of the Deltex C-terminal (DTC) domain reveals a fold composed of a central beta-sheet lined with two long parallel alpha-helices.


Pssm-ID: 465650  Cd Length: 133  Bit Score: 270.52  E-value: 1.56e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  480 TGTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFTarGFPRQCYLPDNAQGRKVLELLKVAWKRR 559
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156564384  560 LIFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQGV 614
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133
Deltex_C cd09633
Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in ...
 481-613 1.11e-80

Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in the regulation of Notch signaling, and therefore may play roles in cell-to-cell communications that regulate mechanisms determining cell fate. They have a central RING-type zinc finger domain and contain a C-terminal domain, described here, that is also found in other domain architectures. Deltex-1 (DTX1) contains a RING finger and two WWE domains, indicating that it may be an E3 ubiquitin ligase. Human deltex 3-like, which contains an additional N-terminal domain (presumably with ubiquitin ligase activity) is also described as E3 ubiquitin-protein ligase DTX3L, B-lymphoma- and BAL-associated protein (BBAP), or rhysin-2. DTX3L mediates monoubiquitination of K91 of histone H4 in response to DNA damage.


Pssm-ID: 193607  Cd Length: 131  Bit Score: 250.18  E-value: 1.11e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384 481 GTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFtaRGFPRQCYLPDNAQGRKVLELLKVAWKRRL 560
Cdd:cd09633    1 GNQPPGTMTYHVIDTSLPGYEGCGTIVIVYNIPSGIQGPEHPGPGKPY--RGTPRIAYLPDNEEGRKVLRLLKKAFDRRL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156564384 561 IFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQG 613
Cdd:cd09633   79 IFTVGTSVTTGREDVVVWNGIHHKTSLTGGPSGHGYPDPTYLDRVLEELAAKG 131
RING-H2_DTX2 cd16672
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ...
 411-482 3.89e-47

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals.


Pssm-ID: 438334  Cd Length: 72  Bit Score: 159.99  E-value: 3.89e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384 411 DCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGT 482
Cdd:cd16672    1 DCIICMEKLSCASGYSDVSESKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKTGT 72
RING-H2_DTX1_4 cd16671
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), ...
 409-477 1.60e-30

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), and similar proteins; DTX1 functions as a Notch downstream transcription regulator that mediates a Notch signal to block differentiation of neural progenitor cells. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 appears to promote B-cell development at the expense of T-cell development. It also promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1 and likely interacts with the intracellular domain of Notch as well. Both DTX1 and DTX4 contain two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. They also harbor two nuclear localization signals.


Pssm-ID: 438333  Cd Length: 69  Bit Score: 113.80  E-value: 1.60e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156564384 409 DEDCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYG 477
Cdd:cd16671    1 DEDCTICMERLVTPSGYEGVLSHKGVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69
RING-H2_DTX1-like cd16459
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ...
 411-477 7.66e-30

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), Deltex4 (DTX4), and similar proteins; This subfamily contains the vertebrate homologs of Drosophila melanogaster Deltex, specifically DTX1, DTX2, and DTX4, and other similar proteins mainly from eumetazoa. The vertebrate homologs of Deltex are involved in Notch signaling and neurogenesis. Mammalian DTX1 is most closely related to the Drosophila Deltex. Both of them bind to SH3-domain containing protein Grb2 and further inhibit E2A. DTX1 functions as a Notch downstream transcription regulator. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1. So it likely interacts with the intracellular domain of Notch as well. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. In contrast to other DTXs, DTX3 does not contain two Notch-binding WWE domains at the N-terminus, but rather a short unique N-terminal domain. It does not interact with the intracellular domain of Notch. In addition, it has a different class of RING finger (C3HC4 type or RING-HC subclass), compared with the other DTXs which harbor a C3H2C3-type RING-H2 finger. Thus DTX3 is not included in this subfamily. Drosophila melanogaster Deltex also does not belong to this subfamily.


Pssm-ID: 438122 [Multi-domain]  Cd Length: 64  Bit Score: 111.84  E-value: 7.66e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156564384 411 DCIICMEKLSTASGYSDvtdSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYG 477
Cdd:cd16459    1 DCPICCEPLCVASGYEE---SKLEGSKVVVRLKKCSHMYHKACLVAMYSNGAKDGSLQCPTCKTIYG 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 21-105 9.39e-25

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 97.80  E-value: 9.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384    21 VWEWQDGLGTWHPYSATVCSFIEQQFVQQKgqrfglgSLAHSIPLGQadpslaPYIIDLPSWTQFRQDTGTMRAVRRHLF 100
Cdd:smart00678   2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGK-------KLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTY 68


                   ....*
gi 156564384   101 PQHSA 105
Cdd:smart00678  69 SPYSK 73
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 110-181 1.10e-24

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 97.41  E-value: 1.10e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384   110 VVWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDLAPLGYNYTVNYTTHTQTNKTSSFCRSVRRQAGPPYP 181
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYS 72
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 21-97 2.07e-19

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 82.34  E-value: 2.07e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156564384   21 VWEWQDGLGTWHPYSATVCSFIEQQFvqQKGQRfglgslahSIPLGQADPSlAPYIIDLPSWTQFRQDTGTMRAVRR 97
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAY--QKGKP--------SVDLSITTAG-FPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 111-174 4.84e-19

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 81.19  E-value: 4.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156564384  111 VWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDL--APLGYNYTVNYTTHTQTNKTSSFCRSVRR 174
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 412-473 1.18e-06

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 45.47  E-value: 1.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564384 412 CIICMEKLSTASgysdvtdskaigslaVGHLTKCSHAFHLLCLLAMYCNGNKdgslQCPSCK 473
Cdd:cd16448    1 CVICLEEFEEGD---------------VVRLLPCGHVFHLACILRWLESGNN----TCPLCR 43
RING-H2_RNF32_rpt2 cd16678
second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
 411-476 4.32e-05

second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the second RING-H2 finger.


Pssm-ID: 438340 [Multi-domain]  Cd Length: 61  Bit Score: 41.58  E-value: 4.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156564384 411 DCIICMEKLStASGYSDVTDSKAIGSLAvghLTKCSHAFHLLCLLAM--YCNGNKdgsLQCPSCKTIY 476
Cdd:cd16678    1 DCPICLTPLQ-SSGDSSDAKRVSSRPTV---LLSCSHVFHATCLEAFeeFSVGEE---LVCPVCRSHY 61
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
 410-474 1.41e-04

RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger protein 1 (ASR1) and similar proteins; ASR1 is required for tolerance to alcohol. It signals alcohol stress to the nucleus. ASR1 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438482 [Multi-domain]  Cd Length: 54  Bit Score: 39.83  E-value: 1.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156564384 410 EDCIICMEKLSTASGYsdvtdskaigslavghLTKCSHAFHLLCLLAMYcngNKDGSLQCPSCKT 474
Cdd:cd23120    2 EECPICLEEMNSGTGY----------------LADCGHEFHLTCIREWH---NKSGNLDCPICRV 47
PHA03247 PHA03247
large tegument protein UL36; Provisional
 166-394 2.55e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  166 SSFCRSVRRQAGPPY--PVTTIIAPPGHTGV-ACSCHQCLSGSRTGPVSGRYRHSMTNLPAYPVPQHPPHRTASVFGTHQ 242
Cdd:PHA03247 2677 SSPPQRPRRRAARPTvgSLTSLADPPPPPPTpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAR 2756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  243 -------AFAPYNKPSLSGARSAPRLNTTNAWGAAPPSLGSQPLYRSSLSHLGPQHLPPGSSTSGAvsasLPSGPSSSPG 315
Cdd:PHA03247 2757 parppttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA----SPAGPLPPPT 2832

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564384  316 SVPATVPMQMPKPSRVQQALAGMTsvlmsAIGLPVclSRAPqPTSPPASRLASKSHGSVKRLRKMSVKGAT---PKPEPE 392
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSV-----APGGDV--RRRP-PSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQ 2904


                  ..
gi 156564384  393 PE 394
Cdd:PHA03247 2905 PE 2906
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
 442-484 4.48e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 438371 [Multi-domain]  Cd Length: 54  Bit Score: 35.86  E-value: 4.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 156564384 442 LTKCSHAFhllcllamyCNGNKDGSLQ----CPSCKTIYGEKTGTQP 484
Cdd:cd16711   17 LDKCKHSF---------CEDCITRALQvkkaCPMCGEFYGQLIGNQP 54
 
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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