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Database: UniProt
Entry: A0A165DE40_9BASI
LinkDB: A0A165DE40_9BASI
Original site: A0A165DE40_9BASI 
ID   A0A165DE40_9BASI        Unreviewed;       561 AA.
AC   A0A165DE40;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Rad17-domain-containing protein {ECO:0000313|EMBL:KZT52615.1};
GN   ORFNames=CALCODRAFT_511962 {ECO:0000313|EMBL:KZT52615.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT52615.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT52615.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT52615.1,
RC   ECO:0000313|Proteomes:UP000076842};
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 rad17/RAD24 family.
CC       {ECO:0000256|ARBA:ARBA00006168}.
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DR   EMBL; KV424061; KZT52615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165DE40; -.
DR   STRING; 1353952.A0A165DE40; -.
DR   InParanoid; A0A165DE40; -.
DR   OrthoDB; 2881303at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12172; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR   PANTHER; PTHR12172:SF0; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR   Pfam; PF03215; Rad17; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT   REGION          537..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  62228 MW;  36F2712791970552 CRC64;
     MAPSKTPIKK SRRGKELIKH VQLGVTPVNG SIKPLRASSK TRFLLNIPSP PSSEDLLSVQ
     SVGSSQARVS TNEGNRGTRS ANDSGLWIDL YSPRSSSDLA VHKRKVDAVR HWIEEALDGG
     LNKQLKKYRK LLALTGPAGS GKTATVQALA REMGFEIVEW QNFRTTPSRF AESDQETLSD
     KFSNFLSHIS EIPQQLDMVR QSSEAATLSS TPRHTVVLLE DLPNLLHSGT KEAFQLDVED
     FITTPGSPPL LLIVSESGRR GMEPESFHRD MTWDIRSILG SRLLQNPSVA EIQCIQPTLI
     DHRMLPHTLN AIVEGSMGDV RSAINALQFA CRLPIREIVK GKARVVEKNG RREDPAEAVK
     QIIQGITRNE QVLALFHMLG KILYNKHSPV DVSLLLPYLH HNYPLFCLDL EDLEAASARL
     SDGDTGEVFH FDSEMGQKLG KSPYWDFGQS ERDARQSLRS WARHDIFATR DAKPVDMIER
     AWLVGRTGGL QHPGILDLAS MPWGIQKIST SMQLLDETAA ACLEDDTTLS QTYGMESEAN
     EDQGAGTSLT GWIEEDDIEE A
//
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