ID   H2ANP7_KAZAF            Unreviewed;       649 AA.
AC   H2ANP7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   Name=KAFR0A05620 {ECO:0000313|EMBL:CCF55997.1};
GN   ORFNames=KAFR_0A05620 {ECO:0000313|EMBL:CCF55997.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF55997.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF55997.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR   EMBL; HE650821; CCF55997.1; -; Genomic_DNA.
DR   RefSeq; XP_003955132.1; XM_003955083.1.
DR   AlphaFoldDB; H2ANP7; -.
DR   STRING; 1071382.H2ANP7; -.
DR   GeneID; 13885961; -.
DR   KEGG; kaf:KAFR_0A05620; -.
DR   eggNOG; KOG2164; Eukaryota.
DR   HOGENOM; CLU_011811_0_0_1; -.
DR   InParanoid; H2ANP7; -.
DR   OrthoDB; 125113at2759; -.
DR   Proteomes; UP000005220; Chromosome 1.
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; 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   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:UP000005220};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          193..247
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..649
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  74816 MW;  FA68DA03B12819F6 CRC64;
     MSSTNSRPDA NFPKKNEVED KKDGPMHNSS IEKRNSKKEK SSSNRARGGQ KSTNNHGRRR
     RMGQHRRQQN YARAENLKNE HGYDLDLSIQ EELTSGDFKL RGRRTQVSIN HLLDFQLPEI
     ERSKDLDVKA RRNLRRNERG REHINLVGDS FINVNYRMLV NGRYDYEEQS CDPNIPIPDE
     KVVGVIVPKG QNCPICLCEE PVAPRMVTCG HIFCCSCLIN FFSIDETITN KETGYTKKKK
     YKDCPLCGSI IRPQRVKPVV YEEENTIPVF KQSPSPGIVS TFYLMCKPLE SMLPLPVTLK
     RDPRKIGNFP PVHLKEVASF GRIVKCDTQY SLELLQQDID AIKVQLDIDK ALYNQDEKYS
     KLAIEDVNTK IASVLSEEAD NLTNTITEAL DRLDLDTDVK SIYDDSTAHF FLQTTFHSPT
     KFFLSPLDIK ILLTVFHNYS KFPDILEAIV ENVHYGSIVT EQLIRRHKYI SYLPIGTEIA
     FVDIDWRNVP FVTKEIYSQF ASELNSRRRE FKIKKQKEDK RKKLYQQKLE EEQAEFYRRD
     YSNYTPTSDM IHLNTVGDSN LALTSLPPSK TPLGTASENE DSSKKKSYEE RTIWGTSISV
     IPDEKTSREN QDFEDMLLQR MQQETDNSQS SGKSKGRKKK KGKVLLFST
//