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Database: UniProt
Entry: A5K8R0_PLAVS
LinkDB: A5K8R0_PLAVS
Original site: A5K8R0_PLAVS 
ID   A5K8R0_PLAVS            Unreviewed;       896 AA.
AC   A5K8R0;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Cell division protein FtsH, putative {ECO:0000313|EMBL:EDL44206.1};
GN   ORFNames=PVX_100935 {ECO:0000313|EMBL:EDL44206.1};
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:EDL44206.1, ECO:0000313|Proteomes:UP000008333};
RN   [1] {ECO:0000313|EMBL:EDL44206.1, ECO:0000313|Proteomes:UP000008333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Salvador I {ECO:0000313|EMBL:EDL44206.1,
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000256|ARBA:ARBA00010044}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000256|ARBA:ARBA00010550}.
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:EDL44206.1}.
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DR   EMBL; AAKM01000010; EDL44206.1; -; Genomic_DNA.
DR   RefSeq; XP_001613933.1; XM_001613883.1.
DR   AlphaFoldDB; A5K8R0; -.
DR   STRING; 126793.A5K8R0; -.
DR   EnsemblProtists; EDL44206; EDL44206; PVX_100935.
DR   GeneID; 5473214; -.
DR   KEGG; pvx:PVX_100935; -.
DR   VEuPathDB; PlasmoDB:PVX_100935; -.
DR   InParanoid; A5K8R0; -.
DR   OMA; CFGFAIW; -.
DR   PhylomeDB; A5K8R0; -.
DR   Proteomes; UP000008333; Chromosome 14.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:EDL44206.1};
KW   Cell division {ECO:0000313|EMBL:EDL44206.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008333};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        79..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          193..334
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          122..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..720
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   896 AA;  99691 MW;  AF0D1AB5F37A15C6 CRC64;
     MFKHYENAVK RIMNAKYENE SLASTGSEKN GDEENSALLQ NNEATGMNKK KSKKTNNDNR
     KYKYYENFFN KKRNKKWNYF MIFFLGICFG FAIWPFFMTI ITYKLFYKDN FNSSNFNTSN
     TSASLKPYGN DRSKKGENGK VSVKDQSQKN SSPHFRPIRF EEIAGIDESK LELLEVVDFI
     RNREKYQEMG ARMPKGVLLV GPPGSGKTML ARAVATEANV PYIYTSGPEF IEIYVGQGAK
     RIRQLFAHAR SVAPSIVFID EIDAIGGKRS SGSVNGAGQR EHDQTLNQLL VEMDGFSNSI
     HIMVIGATNR IDTLDSALLR PGRFDRIVYV PLPDVNGRKR ILEIYIKKIK SDLKAEDIDK
     IARLTPGFSG ADLENVVNEA TILATRNKKS VVTIGELFEA RDKVSMGPER KSLRQSDHQR
     RITAYHEAGH AIVAYFLQPK TDPIHKATII SRGNALGYVE QIPVDDRHNY FKSQMEAKLA
     VCMGGRTAEE IVFGKSETSS GASSDISRAT EIAYKMVTEW GMSDKLGPLN YKKRMGDGYS
     SNRLSAQTIS TIEVEVKALV EKGKSLSEEI LRRHRKELDN LAFALLDRET LSGEEIKKII
     DPNNTRDYSG KVPVLSKGSK SDGAASGPEN EKREGNSTRG GGGSANGSQP NESRSNEGLP
     NEGLPNVGLP NVGLPNDRQE VKQADKGTPA EELKRASSDH VLKKKGKRGE REKHGHAPTT
     DNGKIEIVRK SAKNAVKKIR KKYAKDPNVK NKKILKVVNE HKPYDADRKA AGGNFQNEHG
     RNGKNGLNGA NDPNGPNDPL GKLDKRSYPK GPSPDGGNNN SVVKNMSEVL SKEFAPPYEQ
     NGDNESPDFV KAKELTLNNF KEAVDTSHIK NVGEMKKFNI FEHNLGKLFL FDIFGS
//
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