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Database: UniProt
Entry: G0TRP9_TRYVY
LinkDB: G0TRP9_TRYVY
Original site: G0TRP9_TRYVY 
ID   G0TRP9_TRYVY            Unreviewed;       702 AA.
AC   G0TRP9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-FEB-2023, entry version 39.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=TVY486_0200390 {ECO:0000313|EMBL:CCC46620.1};
OS   Trypanosoma vivax (strain Y486).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX   NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCC46620.1};
RN   [1] {ECO:0000313|EMBL:CCC46620.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y486 {ECO:0000313|EMBL:CCC46620.1};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA   Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA   Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA   Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT   African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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DR   EMBL; HE573018; CCC46620.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0TRP9; -.
DR   VEuPathDB; TriTrypDB:TvY486_0200390; -.
DR   OrthoDB; 152156at2759; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   REPEAT          76..108
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          650..692
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          559..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  76622 MW;  8AE11A3EF395ABA2 CRC64;
     MSSVGRSTLE GQYYAMTGDN NALREWLRAH PDCLNKCTPD APHTLVYMAV VRGHIETVRM
     LVNEFGADLS ISCGALGDTC LHAAVQRSDV ELLSFLMISG APLKANAIGK FPQDMLEGAA
     LQSPEGKQCL GILSTHYRFS GQPAASSGTE NKTLSKSCAK SGAGEMRDLI SKLSISQGDS
     CVVEGEWPKA GPVSTKWPQH VVQEEVVGVP SSSRGQPSVD CGVANAGAAI LRGMRKFSEN
     DRLPYDMEVF RRRYGNGFEY SETTRHYQIR GLLPYSFKGV VYYTPIIFVL AKPRAGGVEE
     SQRSAVLQYR ALIDRNGMAQ FSISRRARYI DPNTAAIIPS ISDTMYRTFI EFVEKVVISN
     FENVPPLTAN AEHSINAQVE GPLFAPSLTT HGRRIRILRD LSLFCDSTFS YDSVTHAITG
     FIPILVDVQL KYQNGECVLL GTENTSNRVV TGEGASQRVL AMDMPVRLPF KMQFGTNGRY
     NTAPCLYLTN ATRCTAESQL NYAFLAEIVS DSATGEVSME SLASLKSWQD HGSVKKVLED
     LQNVALQLLL RYCKKNRIPA NPPARSSERT SSQCERSLGG NRERAVKSSS VASSENVSAV
     VANGANDRPK HSEEASCRAT APPTAGPSRV PTMDGRMPLS TVEANILKKC LVCLEADKTM
     VLLPCMHLLL CHSCADVYKD RLSDGLLCLA CRKPVEGVSR LQ
//
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