ID A5DDM0_PICGU Unreviewed; 625 AA.
AC A5DDM0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PGUG_01371 {ECO:0000313|EMBL:EDK37273.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK37273.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK37273.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the RNF10 family.
CC {ECO:0000256|ARBA:ARBA00008117}.
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DR EMBL; CH408156; EDK37273.2; -; Genomic_DNA.
DR RefSeq; XP_001485700.1; XM_001485650.1.
DR AlphaFoldDB; A5DDM0; -.
DR STRING; 294746.A5DDM0; -.
DR GeneID; 5128251; -.
DR KEGG; pgu:PGUG_01371; -.
DR VEuPathDB; FungiDB:PGUG_01371; -.
DR eggNOG; KOG2164; Eukaryota.
DR HOGENOM; CLU_011811_0_0_1; -.
DR InParanoid; A5DDM0; -.
DR OMA; PKQELWP; -.
DR OrthoDB; 125113at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039739; MAG2/RNF10.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 194..250
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 22..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 489..517
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 71455 MW; 593B8258D2D93B05 CRC64;
MRTGAPTSAA GPHEFLACNR FDVPSTMSGN TTELNRGLEN GNLTDAGGAG SKASALDSRN
RKKKGPKSNK TTAAKPPKRD IFNDNISDLE QQLRNGKRVN GSSKKNQISI NHLLDFSSYR
DSEEYHMNRS RKHTKKERRP SRSHQSLRGM AFVNVNYKFV VDCNGNYASQ QIDPNIPFAL
EDIFQIIAHR GNQCPICLTD ELVAPRMLTA CGHILCLRCL LRLLESELPQ AQKRQGAAVV
EKYRECPLCS SIIRKKEVKP VRISSVDERF EIPQVNQETV LTLMYRPHAS LVALPVSMEE
LRPLVEPFPW INSDHEFDSY SRVFRGGSEY LEEMFAAERA QITALQEEER TAYGEDIFTQ
RALDDIDAQL EAWKTFRKDK APVVPEKKTI EVDPEPFRYY QTGFHSNTIY VLSPLDMKVL
RTSYGNYSAM PTSIVAPIET IRYDELSPET ALTKFKYLSH LPIGTTIGFM ECNWRGSPYV
NSEAWTMFKN DLTKRSQSTA RKLRKEEQDR IRALNEEELR TRAFYERENG TNSDEMVSQF
KALDVAYTDL PVLTSESMGD SEESDSEYRS TPWGTKIRKS ELEAAMEEHE SWEASEMIRR
AREDMNKENG KKKKKKRILL SSNAW
//
