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Database: UniProt
Entry: A0A1B7TK70_9ASCO
LinkDB: A0A1B7TK70_9ASCO
Original site: A0A1B7TK70_9ASCO 
ID   A0A1B7TK70_9ASCO        Unreviewed;       198 AA.
AC   A0A1B7TK70;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=HANVADRAFT_51065 {ECO:0000313|EMBL:OBA29136.1};
OS   Hanseniaspora valbyensis NRRL Y-1626.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA29136.1, ECO:0000313|Proteomes:UP000092321};
RN   [1] {ECO:0000313|Proteomes:UP000092321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBA29136.1}.
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DR   EMBL; LXPE01000001; OBA29136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7TK70; -.
DR   OrthoDB; 901818at2759; -.
DR   Proteomes; UP000092321; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140082; F:SUMO-ubiquitin ligase activity; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR049627; SLX8.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR47094; ELFLESS, ISOFORM B; 1.
DR   PANTHER; PTHR47094:SF12; ELFLESS, ISOFORM B; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092321};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          136..175
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          31..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  23060 MW;  86C2C9A6ECEE28BA CRC64;
     MEVINIDEID ESNNDIIVIE QEQIHNKRAL ELTEEEKEKL DKKERKRLKK LGEKEQEKRK
     SKSDGLEQET NDNSIIILDT QNDENQENNL SEEDLAAYEQ IIEDSDIEII ENPSVSKEDL
     NRVRKEQEIA DETPVCIICY GEPTNAVVTE CGHVYCCECL HEYRNKNFTT CAVCRKHCND
     RNNHLVIMKS ILVPKIEQ
//
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