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Database: UniProt
Entry: A0A1E3IZ68_9TREE
LinkDB: A0A1E3IZ68_9TREE
Original site: A0A1E3IZ68_9TREE 
ID   A0A1E3IZ68_9TREE        Unreviewed;       906 AA.
AC   A0A1E3IZ68;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L203_00085 {ECO:0000313|EMBL:ODN93917.1};
OS   Cryptococcus depauperatus CBS 7841.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN93917.1, ECO:0000313|Proteomes:UP000094043};
RN   [1] {ECO:0000313|EMBL:ODN93917.1, ECO:0000313|Proteomes:UP000094043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN93917.1,
RC   ECO:0000313|Proteomes:UP000094043};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:ODN93917.1}.
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DR   EMBL; AWGK01000001; ODN93917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3IZ68; -.
DR   STRING; 1295531.A0A1E3IZ68; -.
DR   VEuPathDB; FungiDB:L203_00085; -.
DR   OrthoDB; 3088759at2759; -.
DR   Proteomes; UP000094043; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16514; RING-HC_LONFs_rpt2; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 2.30.130.40; LON domain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003111; Lon_prtase_N.
DR   InterPro; IPR046336; Lon_prtase_N_sf.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23327:SF42; LON PEPTIDASE N-TERMINAL DOMAIN AND RING FINGER PROTEIN C14F5.10C; 1.
DR   PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00464; LON; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51787; LON_N; 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:UP000094043};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          517..555
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          600..892
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  100136 MW;  91855518FA7874C7 CRC64;
     MANSHPHTAN AQSSPPPPYR LSPSPACDAR ESAAVVVGQT SQAMSLDTPV VATPTCRLVH
     RRSTSFSERD DPRWLSEGEG SATAIDQPNR MHIRNEEQCS RRPEADDVGP STRAYRGSAD
     RSQAEDRSWI DGADGQESPS GDGSHSHTSG RKTLTLARAR SPVLATTEQR VRSDFGWQPE
     SEPHDRPLAS PSGFLDSVGP GAPSIVSNGK QNNGNVTAAA LGTTLVAQQP RDASAEGNVT
     RNEGRETIMQ ALQSIFTCPN CPIQKNKNCP LYLHHPVTLP CGHTLSLAHL DFPSLPLLPP
     VQFTTDPAEL WSSQQRRHQQ NLSLWASVSC KIPSCKRYLG QETTISNPTS QAQEADGGSS
     RSMGVPVFPP PPLPTPILTA SQQTPAFSLD LANDALPPAY SVDDNQRATL GVGLLDTRVE
     KMLEIFRAEK EKIRLNKRQG RRRNVDATWS DLSSSSDDEA DGENEQRHLG STSDSPTSPS
     ARRPMKRRRR HQSLVLHFAQ NEEEWPFKKE LMATLECGVC AQMLYQPVTT PCQHSFCTKC
     LSRSLDHSPR CPVCRQDLPS FTYFQDHPQS KVLLFVLTTV FPEEYAERRA SLDAEERNSL
     LSTPIFVCTL AFPGMPTILH VFEPRYRLMI RRCIESDSPR FGMVLPARGA GLQSISRVME
     YGTMLEIQSV QMLPDGRSIV ETVGTHRFKL LEKGSLDGYT VGRIERMDDI SPEEEAEMER
     EAVERRSRTL NATLPAAPVS TPISRTPSHQ APAMEASASA PGILNPDFSS SILQGMDFAS
     LAAQSHNPSA APSQSSNRSR QSSNAPSPEN TPESTEELMS ICRAFIEQLR SGFAPWLLQR
     LNNTYGTMPD NPSEFSYWMA LVMPIDEYEK ARLLPIRSPR LRLKLIVHWV ESFRLSWWFS
     NGCVVG
//
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