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Database: UniProt
Entry: A0A165C4K6_9APHY
LinkDB: A0A165C4K6_9APHY
Original site: A0A165C4K6_9APHY 
ID   A0A165C4K6_9APHY        Unreviewed;       366 AA.
AC   A0A165C4K6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN   ORFNames=LAESUDRAFT_762962 {ECO:0000313|EMBL:KZT02195.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT02195.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT02195.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT02195.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV427654; KZT02195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165C4K6; -.
DR   STRING; 1314785.A0A165C4K6; -.
DR   InParanoid; A0A165C4K6; -.
DR   OrthoDB; 1608098at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR032567; LDOC1-rel.
DR   InterPro; IPR005162; Retrotrans_gag_dom.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR15503:SF29; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR   Pfam; PF03732; Retrotrans_gag; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          246..261
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          210..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..353
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  41111 MW;  8171F327CE1E0703 CRC64;
     MTRLSDHQSI PELGAIPKPP VAREKKMGKI KEFRGDKREY ASFLRNVERY LQANTGVYND
     DFSKIAFVLS QIDSSSMAGK WAESWEANQM AKHSNLGTYQ DFKTTLTEKY GGVATKDQAW
     QVLLEGKYKQ DKQTVDEYIG NLDILYRYAE IDDEYAKLIH FKRGLNEKLA EKVFITENPP
     TTYATACKAA RKVTDLQDIH SGKTNIFKFI SGSSGSGRRT EKDPDAMDVD RISPETHQKR
     SVGGLCYNCG KAGHVAADCT SPEYDPAPNR SGKTTSYAKT KTSNPRTKKY SGSGRRRKTS
     KPTKSYSKGT EKKCRRVKRV EESDSEDNSE ESEQEESESS SSEESESSSS ESEEVSEQET
     VVHRAN
//
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