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 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

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498     8 VVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQvdsrlaPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSA 86
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGF------PYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73

large tegument protein UL36; Provisional

                          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

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 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 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 148237498 406 DEDCTICMERLTAPSGYKGPQPT--VKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16671    1 DEDCTICMERLVTPSGYEGVLSHkgVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498    9 VWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRaggSVVLGQVDSRlAPYIIDLQSMNQFRQDTGTLRPVRR 78
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKP---SVDLSITTAG-FPYTIDFKSMTQTNKDTGTTRPVRR 66

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 148237498    91 VVWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDLTSIGFSYVIDFNTMGQIN 144
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYN 54

N1R/p28-like protein; Provisional

                         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

large tegument protein UL36; Provisional

                          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

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 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 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 148237498 406 DEDCTICMERLTAPSGYKGPQPT--VKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16671    1 DEDCTICMERLVTPSGYEGVLSHkgVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG 69

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237498 408 DCTICMERLTAPSGYKGPQpTVKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYG 472
Cdd:cd16459    1 DCPICCEPLCVASGYEESK-LEGSKVVVRLKKCSHMYHKACLVAMYSNGAKDGSLQCPTCKTIYG 64

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237498    9 VWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRaggSVVLGQVDSRlAPYIIDLQSMNQFRQDTGTLRPVRR 78
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKP---SVDLSITTAG-FPYTIDFKSMTQTNKDTGTTRPVRR 66

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 148237498    91 VVWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDLTSIGFSYVIDFNTMGQIN 144
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYN 54

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 148237498 409 CTICMERLTAPSgykgpqptvkpdlVGKLSRCGHVYHIYCLVAMYNNGNKdgslQCPTCK 468
Cdd:cd16448    1 CVICLEEFEEGD-------------VVRLLPCGHVFHLACILRWLESGNN----TCPLCR 43

N1R/p28-like protein; Provisional

                         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

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148237498  409 CTICMERLTAPSgykgpqptvkpdlvgKLSRCGHVYHIYCLVAMYNNGNKdgslQCPTC 467
Cdd:pfam00097   1 CPICLEEPKDPV---------------TLLPCGHLFCSKCIRSWLESGNV----TCPLC 40

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237498 406 DEDCTICMERLTapSGYKGPQptvkpdlvgkLSRCGHVYHIYCLVA--MYNNgnkdgsLQCPTCKT 469
Cdd:cd23121    1 DDCCAICLSDFN--SDEKLRQ----------LPKCGHIFHHHCLDRwiRYNK------ITCPLCRA 48

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237498 406 DEDCTICMERLTaPSGYKGPqptvkpdlvgklsrCGHVYHIYCLVAMYNNgnkdgSLQCPTCK 468
Cdd:cd16479    1 DNTCIICREEMT-VGAKKLP--------------CGHIFHLSCLRSWLQR-----QQTCPTCR 43

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237498 409 CTICMERLTAPSgykgpqptvkpdlVGKLsrCGHVYHIYCLVAMYNNGNKdgslqCPTCKT 469
Cdd:cd16688    3 CSACGSTLDLPS-------------VHFL--CGHSFHQHCLEDYEENDRE-----CPLCAP 43

large tegument protein UL36; Provisional

                          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

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.

                         10        20        30
                 ....*....|....*....|....*....|
gi 148237498 438 SRCGHVYHIYCLVAMYNNGNKDGSLQCPTC 467
Cdd:cd15489   19 DGCGKWFHADCLGPPLSSFVPNGKWICPVC 48