ID A5KBK9_PLAVS Unreviewed; 1473 AA.
AC A5KBK9;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=DNA repair endonuclease, putative {ECO:0000313|EMBL:EDL43259.1};
GN ORFNames=PVX_003735 {ECO:0000313|EMBL:EDL43259.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL43259.1, ECO:0000313|Proteomes:UP000008333};
RN [1] {ECO:0000313|EMBL:EDL43259.1, ECO:0000313|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL43259.1,
RC ECO:0000313|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL43259.1}.
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DR EMBL; AAKM01000018; EDL43259.1; -; Genomic_DNA.
DR RefSeq; XP_001612986.1; XM_001612936.1.
DR STRING; 126793.A5KBK9; -.
DR EnsemblProtists; EDL43259; EDL43259; PVX_003735.
DR GeneID; 5472238; -.
DR KEGG; pvx:PVX_003735; -.
DR VEuPathDB; PlasmoDB:PVX_003735; -.
DR InParanoid; A5KBK9; -.
DR OMA; AKDDMDI; -.
DR PhylomeDB; A5KBK9; -.
DR Proteomes; UP000008333; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Endonuclease {ECO:0000313|EMBL:EDL43259.1};
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:UP000008333}.
FT DOMAIN 1..126
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1143..1212
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 150..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1106..1133
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 161..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1473 AA; 164937 MW; D17DFA1D6102DD6A CRC64;
MGVKGLWSIV APVGVRVNPE IFTGKRIAID VSIWLYELTY ANNLKVLRNG AVDNMSIFND
LWMDFSEQMN TDMRTDNLKK VHLYFFFLRI CKLLYYNIRP IFIFDGTPPE LKRKTIFQRN
VKRRNHEEKF KKTAEKLIYN YYQRSLLASM KSRRSSSKRK SPNEGGPSQG GPSASVGVST
KGEGSPSGDA TTTPPPAAAP AQPPCELIEI YDSIRENDAS LGSMVEHIGN VPVSVKDVLN
ICNDEDLKKI QNKVLMITDL EVQAGGKTAE TKGKELPSER KQSGERGSGG DNAVDGERTN
DEDEYAATLG GEYPEEGEHL NRIDNEMDEE IVRKKHMARK KYYESIPKNF KGFLCMRRPV
DIIDISNYST DILEFTRKLG GEAEEAEKAE KAVGVEGVND ADEATERGSP EKAPHKGEAA
TSIEVGNEKQ GSVGKMGGPD NMYLLPNEED PDGESPHEED PQRNPRKEEI NVLELPPTLD
RADLFHEGKD EYKVYYVNNE EIKIPLFKEL NKEVFEKLPI KLQYQILQDI KEEWYVDNRV
KAIKAKDDMD IFSQVQLETY VRMIKTDFEI EKLKIKMAEN IQNVEGEVII NKELSKHFDS
LSIRDYNDVN GKKKKKKKKK YINEILNQCY FEGKSDQYQE LYIKGEEDEE GGLALNAPLG
ERLSAGEEGS VRCDQRTCIE AYGQVELARR RDVTRPKREL PKGERLGGDS EPDNEPENEQ
KALVKMEKEF KQDLLLDDEQ LFGEDLLRVV EEGGRQGEAN QVEAYQGEVD QVKDNQVKAD
QVQGHPPQGV FPPGAKKAET HASGESASNV HSSGDDFENC SVDEKEQGED AVEEPIAQDV
IDLTSSDEQR ETPIRMNDIE EICETSSEPR IRGEKELRDE VAKILRAAPP GGENTQVEPP
PLNDKAPILI ANSSSAHDSG EDPLEGESSA YGDLSSEVPP STSIELAAET EYSSAPQPIS
GDEQKIAEAL KKVKAKVRRF ISKEEINKLL LNKVDLGSVG KESYLENVLS NKVLLDGFGA
GEEAPNGGPP NGESLNGGPP NGESLNGGPP NGESLNGGPP NGESLNGGPP NGESLNGGHL
TGESLDGPPP DDRPHLRDSR ALDAYLDRTN RENEHLMKEY KKLKKNNIEI NEEMNEDIKI
LLNMFGIPYV QSPCEAEAQC SYLNCKNYCD AIISDDSDVL VFNGKTVIKN FFNRKKTVEV
YERKLIEDKL GLYQDELINL SLLCGCDYTI GVHGVGIVNA LEIIKAFPTF EDLKKLKEIV
SNPFRDLSQD DKYFHNEEVK RFLQTHKNYK LNWIFPNNFP DREVYRCFKY PKVCTDIQKF
QWHLPNLSHI TKFLNKATNI AEEKISNVLN PILQKYDVRV RSYQLKIDDF FPIIERKRKS
VDDLIGIIRD NQKGKRRENG SGGRANASNT RKSSSACKSG NAGGSSPLGR DITSLIDLNP
AGVIRSKRMS TALDHIKGRG RSRKRGSPGE ARG
//
