RAD17_SCHPO
ID RAD17_SCHPO Reviewed; 606 AA.
AC P50531;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Checkpoint protein rad17;
GN Name=rad17; ORFNames=SPAC14C4.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8846774; DOI=10.1002/j.1460-2075.1995.tb00269.x;
RA Griffiths D.J.F., Barbet N.C., McCready S., Lehmann A.R., Carr A.M.;
RT "Fission yeast rad17: a homologue of budding yeast RAD24 that shares
RT regions of sequence similarity with DNA polymerase accessory proteins.";
RL EMBO J. 14:5812-5823(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INTERACTION WITH MUG40.
RX PubMed=12514100; DOI=10.1101/gad.1043203;
RA Kai M., Wang T.S.-F.;
RT "Checkpoint activation regulates mutagenic translesion synthesis.";
RL Genes Dev. 17:64-76(2003).
CC -!- FUNCTION: Participates in checkpoint pathways arrest of the cell cycle.
CC A mechanism that allows the DNA repair pathways to act to restore the
CC integrity of the DNA prior to DNA synthesis or separation of the
CC replicated chromosomes. {ECO:0000269|PubMed:8846774}.
CC -!- SUBUNIT: Interacts with mug40. {ECO:0000269|PubMed:12514100}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8846774}.
CC -!- SIMILARITY: Belongs to the rad17/RAD24 family. {ECO:0000305}.
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DR EMBL; X91889; CAA62993.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11206.1; -; Genomic_DNA.
DR PIR; S60090; S60090.
DR RefSeq; NP_594918.1; NM_001020350.2.
DR AlphaFoldDB; P50531; -.
DR BioGRID; 278139; 100.
DR STRING; 4896.SPAC14C4.13.1; -.
DR iPTMnet; P50531; -.
DR SwissPalm; P50531; -.
DR MaxQB; P50531; -.
DR PaxDb; P50531; -.
DR EnsemblFungi; SPAC14C4.13.1; SPAC14C4.13.1:pep; SPAC14C4.13.
DR GeneID; 2541643; -.
DR KEGG; spo:SPAC14C4.13; -.
DR PomBase; SPAC14C4.13; rad17.
DR VEuPathDB; FungiDB:SPAC14C4.13; -.
DR eggNOG; KOG1970; Eukaryota.
DR HOGENOM; CLU_450679_0_0_1; -.
DR InParanoid; P50531; -.
DR PhylomeDB; P50531; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR PRO; PR:P50531; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031389; C:Rad17 RFC-like complex; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR018324; Rad17/Rad24_fun/met.
DR PANTHER; PTHR12172; PTHR12172; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00602; rad24; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA damage; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..606
FT /note="Checkpoint protein rad17"
FT /id="PRO_0000209952"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 606 AA; 68882 MW; 7D2A31E4F27D455C CRC64;
MRRQLSFHES TKRSLKKKKI RKIEKPSLVS KTSRDKNASI TDIHEEDIEA FSDEENKIVH
LNNLKEDRFQ LWFEKYIPQK AADLAVHKSK ISAIKQWMLT DSLESRLLLI CGPSGCGKST
AVQVLAKELG YSLIEWLNPM NLKEPSNQES DTLSLTEKFS RFMSLCETYP ELELMDSNNI
QKRGKNAQGK KKFIFLDEIP HLSKFNGSLD AFRNVIRTAL TSRGAFSIIM VLTEIQLNNL
EGINSQDRNS FNSVQIMGND LLQDPRVTVL QFNPIAPTYM KKCLGSILRK EGVPKSPKLL
SLVENICSAS EGDLRSAINS LQLSISQSFE KKGTKNIREV KEGKGKGNDF SLEAAQVLER
LSKSDSEAYA RFKNYKSAYI PKSDKNENSF FKKDVGLGMM HAIGKVVWNK REGDDEVLKA
SSQQTGNSER IKGVKVSKSQ ENKNCISLKS DQRERMLNVD QCFTSKRRSL VDIESTINQS
GLSGSVFRYG LFENYVDSCV TTDEAFNVCD LLSISDCLSH DFPYSYTGDE ISTWFSVQGT
LFYLPSPVPR KWRQLRFQQW NNEGIVRGIF DDYMVIYGKR SVSDPVIEAH EDQVLEDIDD
PIEDED