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Database: UniProt
Entry: W7B999_PLAVN
LinkDB: W7B999_PLAVN
Original site: W7B999_PLAVN 
ID   W7B999_PLAVN            Unreviewed;      1549 AA.
AC   W7B999;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Adenosinetriphosphatase {ECO:0000313|EMBL:EUD74716.1};
DE   SubName: Full=DNA repair protein rhp16, putative {ECO:0000313|EMBL:CAD2114493.1};
GN   ORFNames=PVPCR_1406700 {ECO:0000313|EMBL:CAD2114493.1}, YYG_00667
GN   {ECO:0000313|EMBL:EUD74716.1};
OS   Plasmodium vinckei petteri.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=138298 {ECO:0000313|EMBL:EUD74716.1, ECO:0000313|Proteomes:UP000030659};
RN   [1] {ECO:0000313|EMBL:EUD74716.1, ECO:0000313|Proteomes:UP000030659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR {ECO:0000313|EMBL:EUD74716.1,
RC   ECO:0000313|Proteomes:UP000030659};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium vinckei petteri CR.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAD2114493.1, ECO:0000313|Proteomes:UP000515268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ramaprasad A.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LR865419; CAD2114493.1; -; Genomic_DNA.
DR   EMBL; KI965394; EUD74716.1; -; Genomic_DNA.
DR   EnsemblProtists; EUD74716; EUD74716; YYG_00667.
DR   VEuPathDB; PlasmoDB:PVPCR_1406700; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   eggNOG; KOG1002; Eukaryota.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000030659; Unassembled WGS sequence.
DR   Proteomes; UP000515268; Chromosome PVPCR_14.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 3.
DR   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR036957; Znf_PARP_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF12; DNA REPAIR PROTEIN RAD16; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 2.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM01336; zf-PARP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          55..103
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          923..1018
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1380..1532
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          354..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1549 AA;  179246 MW;  AA7B2C8C9E07664C CRC64;
     MDNSLDKLFS KQERLYKEII EASCFYVKKL SEWIGDKHIR KLRLKKDDID LTPKLLINRA
     QSKASRCRVC GLCIEKKSLR IGYPSKDPRG NYGYISCWVH LDCSKKILYA VLYVEENKEC
     LKKYLINSEE ITCTNDHNSY EQFIHKNIKW ELFFGHYDEL DDEEKEKLKE ITKPYDAKDY
     EHGKNSFEIF VKKEKDTVFS NNLMKTEKKQ IINYELNVPK ELKFELLKYQ KEGVSWMINQ
     ENSKHKGGIL ADEMGMGKTI QAITLILCQK INRMKSSEMN IKEIEEKIKE EKTDVCIKTE
     QTNMTNYNSS MDDNTNLIKN QVKVKEEDSE RSIILIESDD NKCFGMKRKS KYFTKSEKEK
     KSKKGNSKNN KTGKSSKNNG SEKVLHGQTL IIAPIAAVMQ WKSEIEKFVE KDFLKVYIYH
     GSNKKISSKE LLEYDVVITS YAMVEINFRK IINKHKIACE YCGRLYLPST LIIHQKYFCG
     PNAVRTEKLK KRKKKNKDTA LVAMKKFDDH FVPTPKNVFL EILNENKENV KDHKDIKGKS
     RKGNEKLEKK NTKKNVPFEE NELIVLSSRE SESDSSESKK SIFSPLLRKT SSRVIDLCNV
     GFEKEAIEKS IEDIYKKKKK NVQWNIVIKY VLKNHLYSID MNDKCKDVLV EIYLSNNNLE
     DHELKSLNMG ELKVLLITMG KHVFGTKIEL INRVLVSAKY IRQEIEEEMK KIEDNNKKKT
     KKGNKNSKTM TKKGIKKGSI DLNSHSDSNY EHNSSEGYKN EYSSSKIKKE DSEDTLTKDT
     GRSNRKRRNS VGSCTVSKRE NSSEMNKKIK KEEQNSSKKR KKCNSESSIG EHFSARSSPR
     LTTKSSGGLS SRGSPRLAAK SSGGVSSKGS ARLATKSSGR LSSKRSSKLT IKSSDDSSVN
     YLGSQTGESS ESFYEESENS SDTVMSYDSI IIEKNKIKNK NKKMKRKGSD IFDESLLHLI
     EWNRIILDEA HRIKNRIAST SQSIFNLKCS GYRWCLTGTP LQNRIGELYS LIRFLEFYPY
     AYYFCSKKDC KCSLINFEMK DNKYCTLCDH TRMCHFNYFN KRILKPIQSF GYNGEGVNSM
     FYLKNEILDE ILLRRTKGER EKDIKLKPLI VSIRKDKLSN EEKDFYESLY KKTTTQFDKY
     VKSNTVLHNY AHIFDLLSRL RQAADHPYLI LFGNTFLSDP SGKFIKKNSA IVPAISNDFV
     CGICLENVPR KNNVNTKCNH HFHKDCLKQY IESFELENKG TEGDENFNIK KYNTYNIVSN
     CSDTEKCDNT NMIVFGNDDN NEGKNNSELN RNYKSLSVVK FKDRENSQFV SITNNIENIK
     DHPLGCPVCY VPLTVDFNAF ANEEDKMDDE EIIVCKEEVT HINKSFINRI NTDEYQTSTK
     IEAIYEEVRN VINNTDDKCL IFSQYCSMLD LIEYHLKKNN IICSKLLGYM SMVSRNNILY
     NFNNDKQLRV LLISLKAGGE GLNLQVANRI FIVDPWWNPA AELQAIQRAH RIGQTKTVYA
     IRFIIENTVE EKIIQLQNKK QLVFDCTIGN SGSAMQKLTK EDLAFLFHA
//
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