ID A8PX80_MALGO Unreviewed; 533 AA.
AC A8PX80;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGL_1356 {ECO:0000313|EMBL:EDP43959.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP43959.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP43959.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP43959.1}.
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DR EMBL; AAYY01000004; EDP43959.1; -; Genomic_DNA.
DR RefSeq; XP_001731173.1; XM_001731121.1.
DR AlphaFoldDB; A8PX80; -.
DR STRING; 425265.A8PX80; -.
DR GeneID; 5855480; -.
DR KEGG; mgl:MGL_1356; -.
DR VEuPathDB; FungiDB:MGL_1356; -.
DR InParanoid; A8PX80; -.
DR OMA; QRECVIS; -.
DR OrthoDB; 3904425at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
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; IPR004331; SPX_dom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR PANTHER; PTHR23327:SF50; TRANSCRIPTIONAL REGULATOR OF YEAST FORM ADHERENCE 3; 1.
DR Pfam; PF03105; SPX; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51382; SPX; 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:UP000008837};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..341
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT DOMAIN 418..457
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 60925 MW; 6613FF117D7D5728 CRC64;
MQEKQPELFP DDETIDTDTI DPEESSHSGA KKQWIEAKSG RRAWGEYELF DDSFGVHPQI
VLHVESPNAL TPVDSPDTPG SDHMSSSTSS SPGTFTRTPR KNSMASRSLR HSIQQLDLGK
PAQEIPTIAS RDYKGAEEMN EVAPGFHHRR IVIPLKADER FFDLLILAIR RLLQLHVSQQ
RTLTMHVESL CSTIAEVASP VNSHNDMYVW REIFSLWLEF DIFEGTREKD RGEMSVAASE
SRLHKYLEAL EKRGLLTPHQ SIEQRGKTLA GTLDSWALQA FSPTNPLTDP RSIATLEHFL
RLNVALVTIK RFERLNIETI RKLFKKHAKK TSLHIRENIN RISSSSKAQQ LLRAASFDSP
IPELDWSHAS VGDVLKSLTA LAPSKFQASF QLSLPRIVSC LLTKALMPVL PSVDDYSCSV
CTSIAWHPIR LCCGHLFCIR CLVKLQKQGM NECPLCRAPN AVRDADENNL DCDMMKYLQE
WFPREVEEKI KENKSDRSVE QRHEKQVRRK NRWARFRTRY HPENEPQREC VIS
//