ID A0A166I9V1_9AGAM Unreviewed; 279 AA.
AC A0A166I9V1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=DNA repair protein rad10 {ECO:0000313|EMBL:KZT43549.1};
GN ORFNames=SISSUDRAFT_1112027 {ECO:0000313|EMBL:KZT43549.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT43549.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT43549.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT43549.1,
RC ECO:0000313|Proteomes:UP000076798};
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family.
CC {ECO:0000256|ARBA:ARBA00008283}.
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DR EMBL; KV428007; KZT43549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166I9V1; -.
DR STRING; 1314776.A0A166I9V1; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProt.
DR GO; GO:0006302; P:double-strand break repair; IEA:UniProt.
DR CDD; cd22325; ERCC1_C-like; 1.
DR Gene3D; 3.40.50.10130; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR InterPro; IPR047260; ERCC1-like_central_dom.
DR InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR NCBIfam; TIGR00597; rad10; 1.
DR PANTHER; PTHR12749:SF0; DNA EXCISION REPAIR PROTEIN ERCC-1; 1.
DR PANTHER; PTHR12749; EXCISION REPAIR CROSS-COMPLEMENTING 1 ERCC1; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF03834; Rad10; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798}.
FT DOMAIN 17..130
FT /note="ERCC1-like central"
FT /evidence="ECO:0000259|Pfam:PF03834"
FT REGION 213..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 31280 MW; C52FD3C333A0D94E CRC64;
MAAAPKPPVV QAGTGNSIIV NPCQRLNPLL DCIRNVSKEF GDIIPDFQLG RTTCALFLSL
KYHRLHPEYI HQRIEKLGNM FSLRILMLLC DVTQHQDAIR EITKTCLINN ITVMVAWSNE
EAGAYLSSFK AFEHKPPDMI KERLEKDFNS MYRTSLTTIP KVNKTDVETL RSHIGSIASV
ATASAEQMHN LPGLGQVKVR RIKDAFEKPF WNNSTNSTFK TRESADITRP QIKENQPMES
ESESATTNPQ QDGRGRATSP TWDIELDPSA SLPDSDVPV
//