ID   RAD50_PLAF7             Reviewed;        2236 AA.
AC   C6KSQ6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable DNA repair protein RAD50;
GN   ORFNames=PFF0285c;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA   Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
RN   [3]
RP   SYNTHESIS OF 966-1002, AND POSSIBLE CANDIDATE MALARIA EPITOPE.
RX   PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA   Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA   Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA   Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT   "Rapid identification of malaria vaccine candidates based on alpha-helical
RT   coiled coil protein motif.";
RL   PLoS ONE 2:E645-E645(2007).
CC   -!- FUNCTION: Essential component of the MRN complex, a complex that
CC       possesses single-stranded DNA endonuclease and 3' to 5' exonuclease
CC       activities, and plays a central role in double-strand break (DSB)
CC       repair, chromosome morphogenesis, DNA repair and meiosis. In the
CC       complex, it mediates the ATP-binding and is probably required to bind
CC       DNA ends and hold them in close proximity (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Probable component of the MRN complex with MRE11.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}.
CC   -!- DOMAIN: The zinc-hook, which separates the large intramolecular coiled
CC       coil regions, contains 2 Cys residues that coordinate one molecule of
CC       zinc with the help of the 2 Cys residues of the zinc-hook of another
CC       RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of
CC       the homodimer, which constitute the ATP-binding domain, interact with
CC       the MRE11 homodimer (By similarity). {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC       determined by epitope response in sera.
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR   EMBL; AL844505; CAG25228.1; -; Genomic_DNA.
DR   RefSeq; XP_966048.1; XM_960955.1.
DR   AlphaFoldDB; C6KSQ6; -.
DR   SMR; C6KSQ6; -.
DR   BioGRID; 1210379; 2.
DR   IntAct; C6KSQ6; 3.
DR   STRING; 5833.PFF0285c; -.
DR   PRIDE; C6KSQ6; -.
DR   EnsemblProtists; CAG25228; CAG25228; PF3D7_0605800.
DR   GeneID; 3885706; -.
DR   KEGG; pfa:PF3D7_0605800; -.
DR   VEuPathDB; PlasmoDB:PF3D7_0605800; -.
DR   HOGENOM; CLU_002217_0_0_1; -.
DR   InParanoid; C6KSQ6; -.
DR   OMA; NVILCHH; -.
DR   PhylomeDB; C6KSQ6; -.
DR   Proteomes; UP000001450; Chromosome 6.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR   GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR   GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISS:GeneDB.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR   GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; ISS:GeneDB.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR   CDD; cd03240; ABC_Rad50; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR045171; ABC_Rad50.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Chromosome; Coiled coil; DNA damage; DNA repair;
KW   Hydrolase; Meiosis; Merozoite; Metal-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome; Telomere; Zinc.
FT   CHAIN           1..2236
FT                   /note="Probable DNA repair protein RAD50"
FT                   /id="PRO_0000371500"
FT   DOMAIN          3..2230
FT                   /note="Zinc-hook"
FT   REGION          489..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1900..1929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..244
FT                   /evidence="ECO:0000255"
FT   COILED          288..381
FT                   /evidence="ECO:0000255"
FT   COILED          634..724
FT                   /evidence="ECO:0000255"
FT   COILED          906..930
FT                   /evidence="ECO:0000255"
FT   COILED          968..997
FT                   /evidence="ECO:0000255"
FT   COILED          1089..1170
FT                   /evidence="ECO:0000255"
FT   COILED          1376..1403
FT                   /evidence="ECO:0000255"
FT   COILED          1606..1626
FT                   /evidence="ECO:0000255"
FT   COILED          1778..1839
FT                   /evidence="ECO:0000255"
FT   COILED          1970..2006
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        490..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   2236 AA;  267956 MW;  3ADA116F6716B875 CRC64;
     MTTLEKIGIQ GIRSYNDEDV EILEFATPIT IIYGNNGSGK STIIECLKVS CTGDFPPNAE
     KGKSFLHDPL ISNKMNIRGK IDVLLNNYNN KRIGISRSYN LFYSKDKNKK VKHTFRALDN
     NIIIKKEKGD DLIITNKCVD INNHIPKLMG VSKALLENVI FCHHDENLWP FSESIKIKKK
     FDELFGDDHF SKILEELLKC KKYLNDLLKR KEFDLIHIKE NFEKKKNIYI EIEKNEKEIQ
     SAQICIQLDV EEIEENTIIL NNLIKKKNLL YKLIGNIDSY FLLYTKFKVD AEAYKDLKEV
     YEENYTELLY FQEVFNNDIN KCEICIQKVK QDIQNLQHEK DTCMFNYNES NKYDDNYELS
     KKQLNEYIIK RDDIRNKLKD IFFYNDQIFF SNYKGNSSSD MIKHSSINEG HQKEKLKKKF
     KKHDSVYIKD HLLKEYENLL HMYDIHKEDI ALYNHDVMLS YKNEEHIPSN ARLMEELFLI
     CQNKVQYKTS NKSDDNKRNN NNNHFDDDNK RNNNNNHFDD DNKRNNNNNH FDDDNKRNNN
     NNHFDDDNKR NNNNNHFDDD NKRNNNNNHF DDDNKNKCDD KKFIEIPNVS NILSNVPYLK
     KKHEKKINSI RYILKRHISH IKRNKYKKRN VIYKIKNYKK RLLKIEKNIT LLDIYKNKLN
     KLKSNEIIYE QNLKKIEKLN QLKCLYDNLT TLDNEMDTYN IQKENNYYEE QIEKNMKQIN
     DIQKLKIWIH TFCNIIRNYN IFYEFIQRCK KIHEHCVIFF DILFSLLDVI KTDFYKIVDM
     LKERDMDLYY YIERGMQKKI NVERNVCVER NVCVERNVCV ENNICVEKNI CVEKNICGEK
     NICGEKKKIT KLKSNIEIEE SVEKIKDNKI NECDVNVDTL NKTNSIHHVN NIKINSKSLV
     CMNEHLQRKR ENEKLNDYTC KLKKQKTHLD ISILKNRKYL DILLNIINIF IDKYENKINN
     IKTLIIPLNQ KVLEISKKLN NMNNNINEYK NYLSNFIHML KEKKYKDVKD FVNYVEAIDN
     QIKIKKKNLW MLNGKEDLMN EFKNHLKSDE QNNSDNNKKV GVEKKKKKNC LFCKNTISQN
     NKDIVQIEMY IEEQKRDMLK KIEESEKDIN ILKNKKEENI ILLNYYYYHI KHIHTYTNDS
     NEMIVKLKEE LLSAQDSIEK YNIKIKNIHR KFQLVQKFKE TCVYLINIQK DILDVEKYIK
     DESIKIKGNF QEMKNKIKDN VENNKMSNNT NKCNDTKTCN NTKTCNNTYT CDHLFIEKLY
     HMIENLDISI EVKESNLLKN IKEFVKKFAK YNNKDIINIF YNKICTSNVN DSYSYIPYND
     IINVDLYQQY NYQNNYKNRF KYNLYKINNA NYICKLLSPH QKVSLKDCYS SDQTPQKIYV
     DEEKEKEKEK KKKKKKKTDN DGYYDEIFHC DNMEYDEQFY EDDDHHSYNK SKSLIENYIT
     PCKNKEESVK EPNMCSIKHI YDNGSSNDDI LNNDKTVLLN KINSSYLSFV LNIGTSYYSN
     EEIKENNKND TNKMCDDTNK MCDDTNKMYD DTNKMYDDTN KMYDDTNKMY DDTNKMCDDT
     NKRYDDTNKM CHDTNKMCDD TNQMYDDTNK RYDDTNKRYD DTNKMCDDTN QMYDDTNKRY
     DNINQNTYGT FLKCSDFLHN LPSIILNNKH FEKMYRNFLS YLNVEEYTRK EQNKMIEKMK
     VVIKDRRAYV IKKSKVLEKT INIDKRIRDL IKKMDIYILY YKEKKKKIID EKINVKNLLI
     EQRDTQLKYI KRCIRNNKKS IFLEKRNYYL KMNMIYILIK KLKHTEEEIV NKEKYLKDVK
     EKLNNNEIIK NQVICIDKKI NEKKEHILCL EKEKINIEKM LHNIIMNTNM KKMYEQFLEH
     HQTFILSLNQ LKASFFLYER KNIKNSNMCK LEYKDEINGD KKKENDNTVS SNNDSIINND
     NRNKKNRYND EENGINYIND IVKKLEENYN NNTNIYNFIN KTFDITDCLK NRLKDIIKIE
     EDDLNEQIEK YTKSITALKI KEAEMNGKIC LRKEYLEKLK EDIKSETLIN IDKEYKKKII
     EIFVYKNLIK DLQNFHFSFD QAIIKFHSLK MQEINLSIKN LWRRVYNSAD IDYIYIKSDI
     QTEPTDKSSQ RRSYNYRVVM VKDNCELDMK GRCSSGQKVL SSIIIRLALA ESFSIKCGIL
     ALDEPTTNLD KANSRNLASL LANIVELRKS SSSFQLILIT HDNYFVDILS QYGLTNCFYK
     IKKNNLGYSK IERVNT