ID B3L0U1_PLAKH Unreviewed; 1431 AA.
AC B3L0U1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=DNA repair protein RAD2, putative {ECO:0000313|EMBL:CAA9986789.1};
GN ORFNames=PKNH_0414900 {ECO:0000313|EMBL:CAA9986789.1};
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9986789.1, ECO:0000313|Proteomes:UP000031513};
RN [1] {ECO:0000313|EMBL:CAA9986789.1, ECO:0000313|Proteomes:UP000031513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H {ECO:0000313|EMBL:CAA9986789.1,
RC ECO:0000313|Proteomes:UP000031513};
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S.,
RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M.,
RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S.,
RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A.,
RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W.,
RA Newbold C.I., Barrell B.G., Berriman M.;
RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite
RT with host range from monkey to man.";
RL Nature 455:799-803(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AM910986; CAA9986789.1; -; Genomic_DNA.
DR RefSeq; XP_002257973.1; XM_002257937.1.
DR STRING; 5851.B3L0U1; -.
DR EnsemblProtists; CAQ38510; CAQ38510; PKH_041380.
DR GeneID; 7319279; -.
DR KEGG; pkn:PKNH_0414900; -.
DR VEuPathDB; PlasmoDB:PKNH_0414900; -.
DR HOGENOM; CLU_003018_1_0_1; -.
DR InParanoid; B3L0U1; -.
DR OMA; AKDDMDI; -.
DR OrthoDB; 26655at2759; -.
DR PhylomeDB; B3L0U1; -.
DR Proteomes; UP000031513; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00841; XPG_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031513}.
FT DOMAIN 1..126
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1112..1181
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 394..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1068..1102
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 395..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1431 AA; 164829 MW; 6534B13F9AD961EF CRC64;
MGVKGLWSIV APVGVRVNPE IFTGKRIAID VSIWLYELTY ANNMKVLRNG GVDNMSMFND
LWMDFSENMN TDMRTENLRK VHLYFFFLRI CKLLYYNIRP IFIFDGTPPE LKRKTIFQRN
MKRRNDEERF QKTAEKLIYN YYQRSLLKTL KGKRSTSKKK IENEEGVISQ GQSSSFVGLN
TIVGRNPPPS SSSPLTLSPA QHTYGLIEIY DSIRENEASL GSMVENIGNV AVSVKDILNI
CNDEDLNKIQ NKVLMISNLE VPIGGVSENM KDKHVQSDLK ETAEKDNRMD EAVQRGITND
ENEYAVILAG EYPTPNEQIN HMDNEIDEEI VRKKHMARKK YYESIPKNFK GFLCMRRPVD
IIDISNYSTD ILEFTRKLGE TQSPSRMAQM DELVEGDTPG KDPTKGDICD KGEGVGTPLA
IENKEHDSAE KKGGEDNAYV LHSGGDTLEK ELPDEESPNK EPPHPEQINV LELPSTLDPA
ELFREGKDEY KVYYVNNEEI RIPLFKELNK EVFEKLPIKL QYQILQDIKE EWYVDNRVKA
IKAKDDMDIF SQVQLETYVR MIKTDFEIEK LKIKMAENIQ NAEGELIVNK ELSKHFDNLS
IRDYNDMDKK KKKKKKKKYI NEILNQCYFE GKNDQYQELY IKEEEEDEKG LVMNAMLRGE
RITEKEEEGG LLHDQRTSIE AYGQVELARR RDVTRPKRER HGEDNEPEKE KKALIKMEEE
FKQDLLLDDE ELFGEDLLRG VEGDGRKLDD DRLDDDKSVE EHPPNGETTV GAKDDNAEEQ
IPLSRDIDIH ENRNFTLNVH SSGDDFENCS VEEKGQIIEM EEVQITQDII DLTSHDEQME
ISIQINDEQE VCEASNESNI DNEEEVHDEQ VQIVLPSIPG GKNAQVVSPP LHDKLQRLID
NYSSGEDIAD GGHFAEGKFS ASGQPSPEIP LSASVEVAAE GENTTLQQAP QEPQPKERER
EHDPIRGEEE EISEAMKKVK QKVRRFITKE KINQLLLNKV DLDTIGKDTY LENVLSNKVL
LDGFGLGGEE EKDEDKQMDG EVPDGGILEG MFLHEDVTPN DREKVRDSRA LDDYMEKANK
ENEELVKEYR KLKKNNIEIN EEMNEDIKIL LNMFGIPYVQ SPCEAEAQCS YLNCKNYCDA
IISDDSDVLV FNGKTVIKNF FNKKKTVEVY ERKLIEDKLG LYQDELINLS LLCGCDYTIG
VHGVGIVNAL EIIKAFPTFE DLKKLKEIVS NPFRDLSKDD KYFNNEEVQR FLKTHKNYKL
NWIFPKNFPD REVYKCFKYP KVCTDIEKFQ WHLPNLTHIS RFLQKETNIA EEKIYNVLNP
ILQKYDVKVR SYQLKIHDFF PMIERKRKSV DNLIDIIRDN QKGKRRSTNS GKRGKDAKSN
KATSGRSSTL GRDITSLIDL NPAGVIRSKR MTTALDHIKG RGRSRKRASQ G
//
