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Database: UniProt
Entry: M2QVX9_CERS8
LinkDB: M2QVX9_CERS8
Original site: M2QVX9_CERS8 
ID   M2QVX9_CERS8            Unreviewed;       599 AA.
AC   M2QVX9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CERSUDRAFT_52549 {ECO:0000313|EMBL:EMD36255.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD36255.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD36255.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD36255.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445798; EMD36255.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2QVX9; -.
DR   STRING; 914234.M2QVX9; -.
DR   HOGENOM; CLU_018598_1_0_1; -.
DR   OrthoDB; 2881303at2759; -.
DR   Proteomes; UP000016930; 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; 1.10.8.60; -; 1.
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:UP000016930}.
FT   REGION          125..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   599 AA;  66205 MW;  4BCE8E0F5AE2EEAF CRC64;
     MSEIATAADD QLWVDKYEPT SEEDLAVHKK KVQGVRQWLL ESLEGGSNGK LRKYRRILAL
     TGPAGVGKTA TIRVLARELG FDILEWRNTM DEQYSLDDDY GEYEGLSEKF QAFLARAGRC
     HSIFSASTQS QPPSSAVSGG SSVSSASQPK RQIILLEDLP NILHPGTRDA FHDSLNAFVG
     AGEFGVAPMI IIISDTGVRG EGGDGDVGSS TNAWRARREA VDVRSVLPPN LLASPFNPIA
     PKILRKALQT LLRSRFAKST GVSASKEVID LIVDSSNGDI RSAIMALQFA CIHDADAQSE
     RGSRKGSKGV IPRALLEAVT RREQSLALFH LLGKLLYNKR KDDPPAPSAS AKDIQRDRDF
     DSRLQNPPPL PPHLGEHHRR TSRVDALYAD TPIDASLLSL YVHQNYSQYC ETMEQCDTLA
     EWLSWIDASG GETWQQANPH HFHLLALSTL HSLPSPVVRR SQKPYKPVFF DTLRRARNAE
     DALGDVRNWL LHCPDQTEEG RAGGWTKGDI ALRSGGVLKA RTLSGMRAYV PPAHKLFSRL
     EWNKGAGDLS QLAEGDDVDV PDAEPFDDPE WADGRERRSE SEGAWQDDDE IEDIEDFED
//
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