RAD3_SCHPO
ID RAD3_SCHPO Reviewed; 2386 AA.
AC Q02099; Q92391; Q9UUM1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein kinase rad3;
DE EC=2.7.11.1;
DE AltName: Full=DNA repair protein rad3;
GN Name=rad3; ORFNames=SPBC216.05;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8978690; DOI=10.1002/j.1460-2075.1996.tb01054.x;
RA Bentley N.J., Holtzman D.A., Flaggs G., Keegan K.S., DeMaggio A.,
RA Ford J.C., Hoekstra M., Carr A.M.;
RT "The Schizosaccharomyces pombe rad3 checkpoint gene.";
RL EMBO J. 15:6641-6651(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 711-1781, AND FUNCTION.
RX PubMed=1398093; DOI=10.1016/0378-1119(92)90069-2;
RA Seaton B.L., Yucel J., Sunnerhagen P., Subramani S.;
RT "Isolation and characterization of the Schizosaccharomyces pombe rad3 gene,
RT involved in the DNA damage and DNA synthesis checkpoints.";
RL Gene 119:83-89(1992).
RN [4]
RP INTERACTION WITH CRB2 AND CHK1.
RX PubMed=14739927; DOI=10.1038/sj.emboj.7600018;
RA Mochida S., Esashi F., Aono N., Tamai K., O'Connell M.J., Yanagida M.;
RT "Regulation of checkpoint kinases through dynamic interaction with Crb2.";
RL EMBO J. 23:418-428(2004).
CC -!- FUNCTION: Serine/threonine kinase which activates checkpoint signaling
CC upon genotoxic stresses. Involved in G2 arrest following DNA damage
CC where it phosphorylates chk1 (PubMed:8978690, PubMed:1398093).
CC Phosphorylation of 'Thr-73' and 'Ser-80' of checkpoint mediator crb2
CC promotes its interaction with chk1 (PubMed:14739927). It is also
CC involved in the dependence of mitosis on the completion of DNA
CC replication (PubMed:1398093). {ECO:0000269|PubMed:1398093,
CC ECO:0000269|PubMed:14739927, ECO:0000269|PubMed:8978690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with crb2 (via BRCT domain). Interacts with chk1.
CC {ECO:0000269|PubMed:14739927}.
CC -!- INTERACTION:
CC Q02099; P87074: crb2; NbExp=3; IntAct=EBI-768555, EBI-768448;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
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DR EMBL; Y09076; CAA70297.1; -; Genomic_DNA.
DR EMBL; U76307; AAC49607.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB40165.1; -; Genomic_DNA.
DR EMBL; X63544; CAA45106.1; -; Genomic_DNA.
DR PIR; T39911; T39911.
DR RefSeq; NP_595357.1; NM_001021264.2.
DR AlphaFoldDB; Q02099; -.
DR SMR; Q02099; -.
DR BioGRID; 277242; 137.
DR IntAct; Q02099; 5.
DR STRING; 4896.SPBC216.05.1; -.
DR iPTMnet; Q02099; -.
DR MaxQB; Q02099; -.
DR PaxDb; Q02099; -.
DR PRIDE; Q02099; -.
DR EnsemblFungi; SPBC216.05.1; SPBC216.05.1:pep; SPBC216.05.
DR GeneID; 2540719; -.
DR KEGG; spo:SPBC216.05; -.
DR PomBase; SPBC216.05; rad3.
DR VEuPathDB; FungiDB:SPBC216.05; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_1_1; -.
DR InParanoid; Q02099; -.
DR OMA; YTVYSQM; -.
DR PhylomeDB; Q02099; -.
DR PRO; PR:Q02099; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0070310; C:ATR-ATRIP complex; IDA:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072371; F:histone kinase activity (H2A-S121 specific); EXP:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:PomBase.
DR GO; GO:0033315; P:meiotic G2/MI DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:PomBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IMP:PomBase.
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:1904514; P:positive regulation of initiation of premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IGI:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA synthesis; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2386
FT /note="Protein kinase rad3"
FT /id="PRO_0000088837"
FT DOMAIN 1386..1943
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2052..2370
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2354..2386
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2058..2064
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2227..2235
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2247..2271
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT CONFLICT 198
FT /note="T -> S (in Ref. 1; CAA70297/AAC49607)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="L -> P (in Ref. 1; CAA70297/AAC49607)"
FT /evidence="ECO:0000305"
FT CONFLICT 1779..1781
FT /note="SEC -> LRM (in Ref. 3; CAA45106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2386 AA; 273529 MW; DDEA343FFA3872D3 CRC64;
MSQHAKRKAG SLDLSPRGLD DRQAFGQLLK EVLALDKEHE LGRSNSLPSM TSELVEVLIE
VGLLAFKHDD SKSEFISPKM LKEAHLSLQA LMLILKRSPT VLREIKSSVT LLDWILPRTI
SLFADIRFIK LFDSLKEFHK LIYQLISEKS FLWDLYASFM RYWKYYITNV SSIVLQITNA
TFPYKMPSPN SQPLQSITPN YPTHREDKFD LLIINIEEAC TFFFESAHFF AQCSYLKKSN
FPSPPLFTAW TWIKPCFFNF VILLKRISIG DSQLFLHLHS RIVQTLCCFS LNFIYHGLPI
CEKSKHILMS SINLTLGSLK KTYTVANTAI SLFFLSLFVL PKTVAGLFYP FGVSLLSDFK
VLEQLEPDSD LKKAIILFKC RYQSSEIDQT TLRAFGEICT GKLENTLFSN SELNLFLLHY
LSLDNDLSNI LKVDFQNGHN ICTFAKWCIN NNLDEPSNLK HFREMLDYYS SHNVTISEDD
LKNFSLVLCT HVAKVNEKTN SIFRTYEVHG CEVCNSFCLL FDERSLFKIP YHELFCALLK
NPDIISSSVK QSLLLDGFFR WSQHCSNFNK ESMLSLREFI MKALASTSRC LRVVAAKVLP
IFIKGPNNLD IVEFHKESKA LIFNTLKILA VENTAILETV ILSWISLSRV VEEEELHFVL
LEVISSVINS GIFYQGIGLS ALQQIASTRH ISVWQLLSPY WPTVSVAIVQ GMGKKPNIAS
LFAQLMNISE GDFLIRTQAY TLPFLVLTKN KALIVRIAEL SQSDVATLCL TNMHKILASL
LTTDHPNLEE SVMLLLSLAT SDFEKVDLTS LLRSDPISIT VELLQLYQND VPHEKIENAL
RKVAMIVSQV VNDEDLSNKE LLYDFFNNHI LGILAEFSNI LNDLKGKTSI NEKIKTIVGI
EKMLSLCGGA VKLGLPQILS NLQSAFQNEH LRFYAIKAWF SLILATKEPE YSSIAGLSLV
ILPPLFPYLE PQEAELVIQI FDFISSDTHK CLQGLKWAIP TSLDSACFSL KAKEIFCSLQ
NEDFYSELQS IIKCLTNENE PVCYLGLQKL ELFFQAKVDE LHDTLNLDIS NEVLDQLLRC
LLDCCVKYAS TNMQISYLAA KNLGELGAID PSRAKAQHII KETVVLDNFE NGEESLKFIL
DFMQSQLIPA FLVTTDTKAQ GFLAYALQEF LKLGGFKSAV INKKKGLTVV TEHWMSLPDL
SKRVLIPFLT SKYHLTPIPK IDIRYPIYKE NVTIHTWMQL FSLKLMEYAH SQNAEKIFGI
CSKVVKDQEV NIPCFLLPFL VLNVILTESE LEVNKVIEEF QLVINQPGPD GLNSVGQQRY
TSFVDVFFKI VDYLNKWLRM RKKRNWDRRS AIARKENRYM SVEDATSRES SISKVESFLS
RFPSKTLGIV SLNCGFHARA LFYWEQHIRN ATAPYAALES DYRVLQEIYA GIDDPDEIEA
VSLNFHDYSF DQQLLLHENS GTWDSALSCY EIIIQKDPEN KKAKIGLLNS MLQSGHYESL
VLSLDSFIIN DNHEYSKMLN LGIEASWRSL SIDSLKKCLS KSNLESFEAK LGSIFYQYLR
KDSFAELTER LQPLYVDAAT AIANTGAHSA YDCYDILSKL HAINDFSRIA ETDGIVSDNL
DIVLRRRLSQ VAPYGKFKHQ ILSTHLVGYE KFENTKKTAE IYLEIARISR KNGQFQRAFN
AILKAMDLDK PLATIEHAQW WWHQGQHRKA ISELNFSLNN NMFDLVDEHE ERPKNRKETL
GNPLKGKVFL KLTKWLGKAG QLGLKDLETY YHKAVEIYSE CENTHYYLGH HRVLMYEEEQ
KLPVNEQSER FLSGELVTRI INEFGRSLYY GTNHIYESMP KLLTLWLDFG AEELRLSKDD
GEKYFREHII SSRKKSLELM NSNVCRLSMK IPQYFFLVAL SQMISRVCHP NNKVYKILEH
IIANVVASYP GETLWQLMAT IKSTSQKRSL RGKSILNVLH SRKLSMSSKV DIKALSQSAI
LITEKLINLC NTRINSKSVK MSLKDHFRLS FDDPVDLVIP AKSFLDITLP AKDANRASHY
PFPKTQPTLL KFEDEVDIMN SLQKPRKVYV RGTDGNLYPF LCKPKDDLRK DARLMEFNNL
ICKILRKDQE ANRRNLCIRT YVVIPLNEEC GFIEWVNHTR PFREILLKSY RQKNIPISYQ
EIKVDLDFAL RSPNPGDIFE KKILPKFPPV FYEWFVESFP EPNNWVTSRQ NYCRTLAVMS
IVGYVLGLGD RHGENILFDE FTGEAIHVDF NCLFDKGLTF EKPEKVPFRL THNMVDAMGP
TGYEGGFRKA SEITMRLLRS NQDTLMSVLE SFLHDPLVEW NRKKSSSKYP NNEANEVLDI
IRKKFQGFMP GETIPLSIEG QIQELIKSAV NPKNLVEMYI GWAAYF
