ID C5MIR8_CANTT Unreviewed; 402 AA.
AC C5MIR8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=CTRG_05961 {ECO:0000313|EMBL:EER30562.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER30562.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER30562.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; GG692404; EER30562.1; -; Genomic_DNA.
DR RefSeq; XP_002546483.1; XM_002546437.1.
DR AlphaFoldDB; C5MIR8; -.
DR STRING; 294747.C5MIR8; -.
DR EnsemblFungi; CTRG_05961-t43_1; CTRG_05961-t43_1-p1; CTRG_05961.
DR GeneID; 8296078; -.
DR KEGG; ctp:CTRG_05961; -.
DR VEuPathDB; FungiDB:CTRG_05961; -.
DR eggNOG; ENOG502SW0H; Eukaryota.
DR HOGENOM; CLU_051223_0_0_1; -.
DR OrthoDB; 50771at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF2; RING FINGER PROTEIN 150 ISOFORM X1; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 177..201
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 298..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 46183 MW; C0D12EAAD19E0C3F CRC64;
MGDFMINLEF MDENTYIRPF LETIFNSKKK KPASEEAIAS LEKVDVSKLN DKFCSICYEA
FDTTKKANEN NKTTNSSNFG DRPDVAIEND KVLSEKLALY GIYHEPMAKT GKFNDPSVFF
PTDPGSAYYS RFPQRNLSTL EDVTMEDQFP GYEDKSFTDK KLNKYQNEGH IAVKMPECEH
VFGLPCIVEW LKSNVSCPLC RKEVEAKNEN SKKSKREAIE QRTLSNFNSR DDMIDHIENH
STDIFNPFRR PFNPRITPIT DSYMRQEWSS PHSQSRVGAM DPELVMPRKF PFGDPIVSRR
TNTFRPVSRT INRFSTNVAN PRYRNPNNNG NSTSTSTSAS NTAESDTTGD VENRTARFAD
NDDDDRSEER RRRRRSASND SSRSARRVNF SPHTTNIDDL HD
//
