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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809   476 TGTQPWGKMEVFRFQMSLPGHEDCGTILIVYNIPHGIQGPEHPSPGKPFTarGFPRQCYLPDSPQGRKVLELLKVAWKRR 555
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12963809   556 LIFTVGTSSTTGETDTVVWNEIHHKTEMDRNVTGHGYPDPNYLQNVLAELAAQGV 610
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809     21 VWEWQDGLGIWHPYSATVCSFIEQHFVRQrgqhfglGSLAHSIPLGQadpslaPYIIDLPSWTQFRQNTGTMRSVRRHLF 100
Cdd:smart00678   2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAG-------KKLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTY 68

                   ....*
gi 12963809    101 SQNSA 105
Cdd:smart00678  69 SPYSK 73

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809   204 GSGTGPVSGRYRHSMTNLPAYPAPQAPHRTTTVSGAHQAFAPYNKPSLSGARSAPRLNTTNPWAAAPPVAGnqslfhSSL 283
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV------ASL 2791

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809   284 ShlgpQLLPSGPSTSSGASASFPSGPSSSSPGSAPTTVPVQMPKASrVQQALAGMTSVLSAIGLPVCLSRAP-------R 356
Cdd:PHA03247 2792 S----ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS-AQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrP 2866

                         170       180       190
                  ....*....|....*....|....*....|...
gi 12963809   357 PTGPPASRPASKSHSSVKRLRKMSVKGAPKPEP 389
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809   476 TGTQPWGKMEVFRFQMSLPGHEDCGTILIVYNIPHGIQGPEHPSPGKPFTarGFPRQCYLPDSPQGRKVLELLKVAWKRR 555
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12963809   556 LIFTVGTSSTTGETDTVVWNEIHHKTEMDRNVTGHGYPDPNYLQNVLAELAAQGV 610
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12963809 407 DCIICMEKLAVASGYSDMTDSKALGPMVVGRLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGT 478
Cdd:cd16672   1 DCIICMEKLSCASGYSDVSESKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKTGT 72

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12963809    110 IVWEWLGDDGSWVAYEARICDYLEQQVARGIQVVDLAPLGYNYTVNYATLTQTNKTSSFCRSVRRQVGPVYP 181
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYS 72

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12963809   111 VWEWLGDDGSWVAYEARICDYLEQQVARGIQVVDL--APLGYNYTVNYATLTQTNKTSSFCRSVRR 174
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12963809   408 CIICMEKLAVASgysdmtdskalgpmvvgRLTKCSHAFHLLCLLAMYcngnKDGSLQCPSC 468
Cdd:pfam00097   1 CPICLEEPKDPV-----------------TLLPCGHLFCSKCIRSWL----ESGNVTCPLC 40

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809   476 TGTQPWGKMEVFRFQMSLPGHEDCGTILIVYNIPHGIQGPEHPSPGKPFTarGFPRQCYLPDSPQGRKVLELLKVAWKRR 555
Cdd:pfam18102   1 TGNQPDGTMTVSTIPTSLPGYENCGTIVITYNIPGGIQGPEHPNPGKPYS--GTPRTAYLPDNEEGRKVLKLLKRAFDQR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12963809   556 LIFTVGTSSTTGETDTVVWNEIHHKTEMDRNVTGHGYPDPNYLQNVLAELAAQGV 610
Cdd:pfam18102  79 LIFTVGTSRTTGASNVVTWNDIHHKTSISGGPTGFGYPDPDYLKRVKEELAAKGI 133

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12963809 407 DCIICMEKLAVASGYSDMTDSKALGPMVVGRLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGT 478
Cdd:cd16672   1 DCIICMEKLSCASGYSDVSESKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKTGT 72

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12963809 405 EEDCIICMEKLAVASGYSDMTDSKALGPMVVGRLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYG 473
Cdd:cd16671   1 DEDCTICMERLVTPSGYEGVLSHKGVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12963809    110 IVWEWLGDDGSWVAYEARICDYLEQQVARGIQVVDLAPLGYNYTVNYATLTQTNKTSSFCRSVRRQVGPVYP 181
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYS 72

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12963809   111 VWEWLGDDGSWVAYEARICDYLEQQVARGIQVVDL--APLGYNYTVNYATLTQTNKTSSFCRSVRR 174
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLsiTTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12963809 408 CIICMEKLAVASgysdmtdskalgpmvVGRLTKCSHAFHLLCLLAMYCNGNKdgslQCPSCK 469
Cdd:cd16448   1 CVICLEEFEEGD---------------VVRLLPCGHVFHLACILRWLESGNN----TCPLCR 43

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12963809 407 DCIICMEKLAvASGYSDMTDSKALGPMVvgrLTKCSHAFHLLCLLAM--YCNGNKdgsLQCPSCKTIY 472
Cdd:cd16678   1 DCPICLTPLQ-SSGDSSDAKRVSSRPTV---LLSCSHVFHATCLEAFeeFSVGEE---LVCPVCRSHY 61

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963809 405 EEDCIICMeklavasgySDMTDSKALgpmvvgrlTKCSHAFhllcllamyCNGNKDGSLQ----CPSCKTIYGEKTGTQP 480
Cdd:cd16711   1 EETCPICL---------GEIQNKKTL--------DKCKHSF---------CEDCITRALQvkkaCPMCGEFYGQLIGNQP 54

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12963809   408 CIICMEKLAVASgysdmtdskalgpmvvgRLTKCSHAFHLLCLLAMYcngnKDGSLQCPSC 468
Cdd:pfam00097   1 CPICLEEPKDPV-----------------TLLPCGHLFCSKCIRSWL----ESGNVTCPLC 40