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Conserved domains on  [gi|148237498|ref|NP_055992|]
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E3 ubiquitin-protein ligase DTX4 isoform 1 [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 ...
475-609 1.98e-86

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: 265.13  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  475 TGTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFSarGFPRHCYLPDSEKGRKVLKLLLVAWDRR 554
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148237498  555 LIFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQGI 609
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133
RING-H2_DTX1_4 cd16671
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), ...
406-472 1.84e-43

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: 149.63  E-value: 1.84e-43
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498 406 DEDCTICMERLTAPSGYKGPQPT--VKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16671    1 DEDCTICMERLVTPSGYEGVLSHkgVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
8-86 6.50e-28

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


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 106.66  E-value: 6.50e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498     8 VVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQvdsrlaPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSA 86
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
92-144 8.90e-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: 80.42  E-value: 8.90e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148237498   92 VWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDL--TSIGFSYVIDFNTMGQIN 144
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTN 55
PHA03247 super family cl33720
large tegument protein UL36; Provisional
169-365 4.00e-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: 43.77  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  169 PKAQSWPVSPGPATSPPMSPCSCPqcvlvmsvkAAVVNGSTGPLQLPVtrknmPPPGVVKLPPLPGSGAKPLDSTGTIRG 248
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHAPDPPPPSP---------SPAANEPDPHPPPTV-----PPPERPRDDPAPGRVSRPRRARRLGRA 2673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  249 PLKTAPSQVIRRQASSMPTGTTMGS---PASPPGPNSKTGRVALATLNRTNLQRLAIAQSRVLIASGVPTVPVKNLNGSS 325
Cdd:PHA03247 2674 AQASSPPQRPRRRAARPTVGSLTSLadpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 148237498  326 PVNPALAGITGILMSAAGLPVCLTRPPKLVLHPPPVSKSE 365
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
 
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 ...
475-609 1.98e-86

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: 265.13  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  475 TGTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFSarGFPRHCYLPDSEKGRKVLKLLLVAWDRR 554
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148237498  555 LIFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQGI 609
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 ...
476-608 1.16e-81

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: 252.88  E-value: 1.16e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 476 GTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFsaRGFPRHCYLPDSEKGRKVLKLLLVAWDRRL 555
Cdd:cd09633    1 GNQPPGTMTYHVIDTSLPGYEGCGTIVIVYNIPSGIQGPEHPGPGKPY--RGTPRIAYLPDNEEGRKVLRLLKKAFDRRL 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148237498 556 IFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQG 608
Cdd:cd09633   79 IFTVGTSVTTGREDVVVWNGIHHKTSLTGGPSGHGYPDPTYLDRVLEELAAKG 131
RING-H2_DTX1_4 cd16671
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), ...
406-472 1.84e-43

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: 149.63  E-value: 1.84e-43
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498 406 DEDCTICMERLTAPSGYKGPQPT--VKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16671    1 DEDCTICMERLVTPSGYEGVLSHkgVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
8-86 6.50e-28

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 106.66  E-value: 6.50e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498     8 VVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQvdsrlaPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSA 86
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
9-78 4.49e-21

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: 86.97  E-value: 4.49e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498    9 VWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRaggSVVLGQVDSRlAPYIIDLQSMNQFRQDTGTLRPVRR 78
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKP---SVDLSITTAG-FPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
92-144 8.90e-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: 80.42  E-value: 8.90e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148237498   92 VWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDL--TSIGFSYVIDFNTMGQIN 144
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTN 55
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
91-144 8.74e-18

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 77.77  E-value: 8.74e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 148237498    91 VVWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDLTSIGFSYVIDFNTMGQIN 144
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYN 54
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
409-467 6.93e-05

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 40.18  E-value: 6.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498   409 CTICMERLTAPsgykgpqPTVKPdlvgklsrCGHVYHIYCLVAMYNNGNKdgslQCPTC 467
Cdd:smart00184   1 CPICLEEYLKD-------PVILP--------CGHTFCRSCIRKWLESGNN----TCPIC 40
PHA02929 PHA02929
N1R/p28-like protein; Provisional
385-471 1.13e-04

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 44.00  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 385 KKGKTPEE-------VLKKYLQKVRHPPDEDCTICMERLTAPSgykgpqptVKPDLVGKLSRCGHVYHIYCLVAMYNNGN 457
Cdd:PHA02929 146 KKGKNYKKflktipsVLSEYEKLYNRSKDKECAICMEKVYDKE--------IKNMYFGILSNCNHVFCIECIDIWKKEKN 217
                         90
                 ....*....|....
gi 148237498 458 KdgslqCPTCKTIY 471
Cdd:PHA02929 218 T-----CPVCRTPF 226
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
409-467 1.53e-04

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 39.26  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498  409 CTICMERLTAPSgykgpqptvkpdlvgKLSRCGHVYHIYCLVAMYNNGNKdgslQCPTC 467
Cdd:pfam00097   1 CPICLEEPKDPV---------------TLLPCGHLFCSKCIRSWLESGNV----TCPLC 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
169-365 4.00e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  169 PKAQSWPVSPGPATSPPMSPCSCPqcvlvmsvkAAVVNGSTGPLQLPVtrknmPPPGVVKLPPLPGSGAKPLDSTGTIRG 248
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHAPDPPPPSP---------SPAANEPDPHPPPTV-----PPPERPRDDPAPGRVSRPRRARRLGRA 2673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  249 PLKTAPSQVIRRQASSMPTGTTMGS---PASPPGPNSKTGRVALATLNRTNLQRLAIAQSRVLIASGVPTVPVKNLNGSS 325
Cdd:PHA03247 2674 AQASSPPQRPRRRAARPTVGSLTSLadpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 148237498  326 PVNPALAGITGILMSAAGLPVCLTRPPKLVLHPPPVSKSE 365
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
390-469 2.97e-03

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 40.36  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 390 PEEVLKKYLQK------VRHPPDEDCTICMERLTapsgyKGPQPTVKPdlvgklsrCGHVYHIYCLVAMYNngnkDGSLQ 463
Cdd:COG5540  301 PTTTTKGSLKPlsieraVEADKGVECAICMSNFI-----KNDRLRVLP--------CDHRFHVGCVDKWLL----GYSNK 363

                 ....*.
gi 148237498 464 CPTCKT 469
Cdd:COG5540  364 CPVCRT 369
 
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 ...
475-609 1.98e-86

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: 265.13  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  475 TGTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFSarGFPRHCYLPDSEKGRKVLKLLLVAWDRR 554
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148237498  555 LIFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQGI 609
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 ...
476-608 1.16e-81

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: 252.88  E-value: 1.16e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 476 GTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFsaRGFPRHCYLPDSEKGRKVLKLLLVAWDRRL 555
Cdd:cd09633    1 GNQPPGTMTYHVIDTSLPGYEGCGTIVIVYNIPSGIQGPEHPGPGKPY--RGTPRIAYLPDNEEGRKVLRLLKKAFDRRL 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148237498 556 IFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQG 608
Cdd:cd09633   79 IFTVGTSVTTGREDVVVWNGIHHKTSLTGGPSGHGYPDPTYLDRVLEELAAKG 131
RING-H2_DTX1_4 cd16671
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), ...
406-472 1.84e-43

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: 149.63  E-value: 1.84e-43
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498 406 DEDCTICMERLTAPSGYKGPQPT--VKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16671    1 DEDCTICMERLVTPSGYEGVLSHkgVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69
RING-H2_DTX2 cd16672
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ...
408-477 1.30e-34

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: 125.32  E-value: 1.30e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237498 408 DCTICMERLTAPSGYKGP--QPTVKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYGVKTGT 477
Cdd:cd16672    1 DCIICMEKLSCASGYSDVseSKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKTGT 72
RING-H2_DTX1-like cd16459
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ...
408-472 4.04e-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: 112.61  E-value: 4.04e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237498 408 DCTICMERLTAPSGYKGPQpTVKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16459    1 DCPICCEPLCVASGYEESK-LEGSKVVVRLKKCSHMYHKACLVAMYSNGAKDGSLQCPTCKTIYG 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
8-86 6.50e-28

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 106.66  E-value: 6.50e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498     8 VVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQvdsrlaPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSA 86
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
9-78 4.49e-21

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: 86.97  E-value: 4.49e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498    9 VWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRaggSVVLGQVDSRlAPYIIDLQSMNQFRQDTGTLRPVRR 78
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKP---SVDLSITTAG-FPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
92-144 8.90e-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: 80.42  E-value: 8.90e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148237498   92 VWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDL--TSIGFSYVIDFNTMGQIN 144
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTN 55
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
91-144 8.74e-18

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 77.77  E-value: 8.74e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 148237498    91 VVWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDLTSIGFSYVIDFNTMGQIN 144
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYN 54
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
407-469 4.81e-06

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: 44.07  E-value: 4.81e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237498 407 EDCTICMERLtaPSGykgpqptvkpdlVGKLSRCGHVYHIYCLVAMYnngNKDGSLQCPTCKT 469
Cdd:cd23120    2 EECPICLEEM--NSG------------TGYLADCGHEFHLTCIREWH---NKSGNLDCPICRV 47
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
409-468 9.28e-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: 42.77  E-value: 9.28e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 409 CTICMERLTAPSgykgpqptvkpdlVGKLSRCGHVYHIYCLVAMYNNGNKdgslQCPTCK 468
Cdd:cd16448    1 CVICLEEFEEGD-------------VVRLLPCGHVFHLACILRWLESGNN----TCPLCR 43
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
409-467 6.93e-05

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 40.18  E-value: 6.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498   409 CTICMERLTAPsgykgpqPTVKPdlvgklsrCGHVYHIYCLVAMYNNGNKdgslQCPTC 467
Cdd:smart00184   1 CPICLEEYLKD-------PVILP--------CGHTFCRSCIRKWLESGNN----TCPIC 40
PHA02929 PHA02929
N1R/p28-like protein; Provisional
385-471 1.13e-04

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 44.00  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 385 KKGKTPEE-------VLKKYLQKVRHPPDEDCTICMERLTAPSgykgpqptVKPDLVGKLSRCGHVYHIYCLVAMYNNGN 457
Cdd:PHA02929 146 KKGKNYKKflktipsVLSEYEKLYNRSKDKECAICMEKVYDKE--------IKNMYFGILSNCNHVFCIECIDIWKKEKN 217
                         90
                 ....*....|....
gi 148237498 458 KdgslqCPTCKTIY 471
Cdd:PHA02929 218 T-----CPVCRTPF 226
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
403-468 1.36e-04

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438136 [Multi-domain]  Cd Length: 55  Bit Score: 39.95  E-value: 1.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237498 403 HPPDEDCTICMErltapsgykgpqpTVKPDLVGKLSRCGHVYHIYCLVAMYNNGNKdgslQCPTCK 468
Cdd:cd16473    1 MLECEECAICLE-------------NYQNGDLLRGLPCGHVFHQNCIDVWLERDNH----CCPVCR 49
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
409-467 1.53e-04

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 39.26  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498  409 CTICMERLTAPSgykgpqptvkpdlvgKLSRCGHVYHIYCLVAMYNNGNKdgslQCPTC 467
Cdd:pfam00097   1 CPICLEEPKDPV---------------TLLPCGHLFCSKCIRSWLESGNV----TCPLC 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
169-365 4.00e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  169 PKAQSWPVSPGPATSPPMSPCSCPqcvlvmsvkAAVVNGSTGPLQLPVtrknmPPPGVVKLPPLPGSGAKPLDSTGTIRG 248
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHAPDPPPPSP---------SPAANEPDPHPPPTV-----PPPERPRDDPAPGRVSRPRRARRLGRA 2673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  249 PLKTAPSQVIRRQASSMPTGTTMGS---PASPPGPNSKTGRVALATLNRTNLQRLAIAQSRVLIASGVPTVPVKNLNGSS 325
Cdd:PHA03247 2674 AQASSPPQRPRRRAARPTVGSLTSLadpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 148237498  326 PVNPALAGITGILMSAAGLPVCLTRPPKLVLHPPPVSKSE 365
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
406-469 4.29e-04

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) and similar proteins; This subfamily includes Arabidopsis thaliana RHA1A, RHA1B and XERICO. RHA1A is a probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. RHA1B possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro. XERICO functions on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438483 [Multi-domain]  Cd Length: 50  Bit Score: 38.23  E-value: 4.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237498 406 DEDCTICMERLTapSGYKGPQptvkpdlvgkLSRCGHVYHIYCLVA--MYNNgnkdgsLQCPTCKT 469
Cdd:cd23121    1 DDCCAICLSDFN--SDEKLRQ----------LPKCGHIFHHHCLDRwiRYNK------ITCPLCRA 48
RING-H2_RNF32_rpt2 cd16678
second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
408-471 1.51e-03

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: 37.35  E-value: 1.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237498 408 DCTICMERLTAPSGYKGPQPTVKPDLVgkLSRCGHVYHIYCLVAM--YNNGNKdgsLQCPTCKTIY 471
Cdd:cd16678    1 DCPICLTPLQSSGDSSDAKRVSSRPTV--LLSCSHVFHATCLEAFeeFSVGEE---LVCPVCRSHY 61
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
406-468 2.12e-03

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 36.18  E-value: 2.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237498 406 DEDCTICMERLTaPSGYKGPqptvkpdlvgklsrCGHVYHIYCLVAMYNNgnkdgSLQCPTCK 468
Cdd:cd16479    1 DNTCIICREEMT-VGAKKLP--------------CGHIFHLSCLRSWLQR-----QQTCPTCR 43
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
407-479 2.18e-03

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 438372 [Multi-domain]  Cd Length: 56  Bit Score: 36.64  E-value: 2.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237498 407 EDCTICMERLTAPSgykgpqptvkpdlvgKLSRCGHVYHIYCLvamyNNGNKDGSLqCPTCKTIYGVKTGTQP 479
Cdd:cd16712    4 DECPICMDRISNKK---------------VLPKCKHVFCAACI----DKAMKYKPV-CPVCGTIYGVIKGNQP 56
RING-H2_Vps11 cd16688
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ...
409-469 2.93e-03

RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole.


Pssm-ID: 438349 [Multi-domain]  Cd Length: 44  Bit Score: 35.79  E-value: 2.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237498 409 CTICMERLTAPSgykgpqptvkpdlVGKLsrCGHVYHIYCLVAMYNNGNKdgslqCPTCKT 469
Cdd:cd16688    3 CSACGSTLDLPS-------------VHFL--CGHSFHQHCLEDYEENDRE-----CPLCAP 43
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
390-469 2.97e-03

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 40.36  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498 390 PEEVLKKYLQK------VRHPPDEDCTICMERLTapsgyKGPQPTVKPdlvgklsrCGHVYHIYCLVAMYNngnkDGSLQ 463
Cdd:COG5540  301 PTTTTKGSLKPlsieraVEADKGVECAICMSNFI-----KNDRLRVLP--------CDHRFHVGCVDKWLL----GYSNK 363

                 ....*.
gi 148237498 464 CPTCKT 469
Cdd:COG5540  364 CPVCRT 369
PHA03247 PHA03247
large tegument protein UL36; Provisional
179-427 4.28e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  179 GPATSPPMSPCScPQCVLVMSVKAAVVNGSTGPLQLPVTRKNMPPPgvvklPPLPGSgakpldstgtirgPLKTAPSQVi 258
Cdd:PHA03247 2866 PPSRSPAAKPAA-PARPPVRRLARPAVSRSTESFALPPDQPERPPQ-----PQAPPP-------------PQPQPQPPP- 2925
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  259 rrQASSMPTGTTMGSPASPPGPNSKTGRVALATLNRTNLQRLAIAQSRV-----LIASGVPTVPVKNLNGSSPVNPALAG 333
Cdd:PHA03247 2926 --PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavprfRVPQPAPSREAPASSTPPLTGHSLSR 3003
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498  334 ITGILMSaaglpvcltrppkLVLH----PPPVSKSEIKSIPGVSNTSRKTTKKQAKKGKTPEEVLK----KYLQKVRHPP 405
Cdd:PHA03247 3004 VSSWASS-------------LALHeetdPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDplppEPHDPFAHEP 3070
                         250       260
                  ....*....|....*....|..
gi 148237498  406 DEDcTICMERLTAPSGYKGPQP 427
Cdd:PHA03247 3071 DPA-TPEAGARESPSSQFGPPP 3091
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
409-469 5.78e-03

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 36.51  E-value: 5.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237498 409 CTICMERLTAPsgykgpqptVKpdlvgklSRCGHVYHIYCLVAMYNNgnKDGSLQCPTCKT 469
Cdd:cd16498   19 CPICLELLKEP---------VS-------TKCDHQFCRFCILKLLQK--KKKPAPCPLCKK 61
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
438-467 6.25e-03

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 34.99  E-value: 6.25e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 148237498 438 SRCGHVYHIYCLVAMYNNGNKDGSLQCPTC 467
Cdd:cd15489   19 DGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
RING-H2_TUL1-like cd23117
RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ...
408-468 9.64e-03

RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ligase 1 (TUL1) and similar proteins; This subfamily includes Saccharomyces cerevisiae TUL1, Schizosaccharomyces pombe DSC E3 ubiquitin ligase complex subunit 1 (DSC1), and Arabidopsis thaliana protein FLYING SAUCER 2 (FLY2). TUL1 is the catalytic component of DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions, and support a role in protein quality control. It mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes. TUL1 also targets the unpalmitoylated endosomal SNARE TLG1 to the multivesicular body (MVB) pathway. DSC1, also known as defective for SREBP cleavage protein 1, is the catalytic component of the DSC E3 ubiquitin ligase complex required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. FLY2 acts as an E3 ubiquitin-protein ligase that may be involved in xylem development. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438479 [Multi-domain]  Cd Length: 59  Bit Score: 35.06  E-value: 9.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237498 408 DCTICMERLTAPSGYKGPQ-PTVKPdlvgklsrCGHVYHIYCLvamynNGNKDGSLQCPTCK 468
Cdd:cd23117    6 DCVICMSDIELPSTNSVRRdYMVTP--------CNHIFHTNCL-----ERWMDIKLECPTCR 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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