ID B3RS88_TRIAD Unreviewed; 1303 AA.
AC B3RS88;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=TRIADDRAFT_54511 {ECO:0000313|EMBL:EDV27012.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV27012.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV27012.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV27012.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the VPS8 family.
CC {ECO:0000256|ARBA:ARBA00009422}.
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DR EMBL; DS985243; EDV27012.1; -; Genomic_DNA.
DR RefSeq; XP_002111008.1; XM_002110972.1.
DR STRING; 10228.B3RS88; -.
DR EnsemblMetazoa; TriadT54511; TriadP54511; TriadG54511.
DR GeneID; 6751685; -.
DR KEGG; tad:TRIADDRAFT_54511; -.
DR CTD; 6751685; -.
DR eggNOG; KOG2079; Eukaryota.
DR HOGENOM; CLU_000917_1_2_1; -.
DR InParanoid; B3RS88; -.
DR OMA; WAHQDKH; -.
DR OrthoDB; 120292at2759; -.
DR PhylomeDB; B3RS88; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR045111; Vps41/Vps8.
DR InterPro; IPR025941; Vps8_central_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR PANTHER; PTHR12616:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 8 HOMOLOG; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF12816; Vps8; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 235..276
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1148..1194
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 147273 MW; 43DDDE5515F59C4C CRC64;
MTALPDFSQD YFNSEEELQT ADEILQESNE ADPFLIDLEN DVASLAISAG GTTTTTYDPA
SDLTSLLEAD DDIPEDFESD LQQVDNLPSL DSILQAPDDF EAELPAMQDL PTLDSILNES
VDDPFLTDEL GFDIRSETSD NQSAKSGHSN SESGASTSAA PFDSRRRHKS HGKKLLVKHD
VSGSIVKVSK LQTLTAQICK KSALSSLVAI GTMNGLTLVF DLRENLKHVL GGKKSAIHLG
SVTAVDFNTD GSRLLTGYQN GQIFMWDTQK GEIIRNLTSA HPPLTVLQLK VDSIYYYYCF
TDDPTLAIFS DASGSAYTLS FTRKMGIRGY NKRIIVDGSD ATVCSLEPLH IEEKRKNHRA
SNLQIVAMTT LLRIVFVALK PEPKVLLTIP IKANEDDIPA LSWQFSLIKT DGNSEVMEPV
LAVGRGQMIV FYQWMTPHLL VIVDVNRKAR VIYIKSEEQL EIIDTAAIEL VTPSYLRSST
SVEGISERLI ACHRRAFFST VVSFRGEIAL AGTKAIYVLR LRTWKERIDY FVELNKYSEA
LAQALAFYDD RAKCTIGLPS NDEQRQAIIA DEIIKLLSQF VDSALQFIHQ ETVEGTDTEL
YFAVEYYQNR EMLDRVEQCI LHLQVTSMDF HQIVNLCWTY GLYDAIIYVY AQGLKDYMTP
VEELYKIIRN KLNSGVPILT ERKSYPRFRT FLKFDSREFL NVLALAFEDE DFGINESGFV
AIDGRQLVID ILLEVMLEPT QSNVEEIRNL FTFIARQVAK PQSNIIISSH LIDQVLEYLC
NAMDKTRMEE RQQVCQVIYE QKGQLANVLS CYWRDDSRKD LVFDYINGFL QDEKIIEFDR
VEMKKIVLAH IEDLLSVDNI AAARLLAVDF KIDLPTLMIQ LMGESKVLFS LLDGIYNGNT
GVLATKSDIV SDPESHEKYI ELLCRYNPGD VYPHLKAIEG YRPEVALKIC RQFKVMNATA
YLLELIGEIE EAFHLIIKDF NEKFSELTKA CRVGNLSREN MDQSITQTES MLHAIVKFCK
RGSNKIVQAR REAIWFELLD VVLVPQAIKE NFSQDSIEVF MNMANIVLNN MMGFISIPQV
LRKIMMDSSY NSKFGDIKSL ILGLLDTYIY EETLLTSTIK LLSQDLYTSL RSFEVNNKKG
IQPGRFFCEI CRRTLLSDKE RLDDEAAVFN CGHMFHIKCL EISLPSRQFV CILCAGIRST
STGSISLSRQ QSTTNSVGFE SNSKRSSKSL GLAEAFHNTV DNQKLKKYEH FIRTTKTSSK
IAMLAELSKA RDGVESFSDE SRLISEDFKL KSMPQGSFDL SRC
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