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Database: UniProt
Entry: A0A0K9P257_ZOSMR
LinkDB: A0A0K9P257_ZOSMR
Original site: A0A0K9P257_ZOSMR 
ID   A0A0K9P257_ZOSMR        Unreviewed;       534 AA.
AC   A0A0K9P257;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolases superfamilyprotein {ECO:0000313|EMBL:KMZ62295.1};
GN   ORFNames=ZOSMA_477G00090 {ECO:0000313|EMBL:KMZ62295.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ62295.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001836};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007448}.
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:KMZ62295.1}.
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DR   EMBL; LFYR01001385; KMZ62295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9P257; -.
DR   STRING; 29655.A0A0K9P257; -.
DR   OMA; WTHHVDT; -.
DR   OrthoDB; 819832at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   CDD; cd19510; RecA-like_BCS1; 1.
DR   Gene3D; 6.10.280.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR025753; AAA_N_dom.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR   PANTHER; PTHR23070:SF43; OS09G0445700 PROTEIN; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF14363; AAA_assoc; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Hydrolase {ECO:0000313|EMBL:KMZ62295.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..534
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005527349"
FT   DOMAIN          239..388
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          453..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  59526 MW;  06FE89B57C97D2AB CRC64;
     MEILSQMWSL LGLLTVLQNV LPSQLLHLLH TLWQSLQDSL TPFSYFDVPE FIGYCGVDPN
     DLYRHVHLYL HASLLPSTST TSTSSTTATS PPRLTLSLPR NSHNLSLTVA PNHAVEDYYN
     GNRLLWTHHV DTLQDSLDER RSFSLRTPKQ LARSPTLLTS YLSHVSRKAE EFERLSRDRR
     LHTNIPGRSE SGCWASVPFR HPATFDTLAL DQGLKRRIIA DLSAFADGKD FYKRIGRAWK
     RGYLLHGPPG SGKSSLIAAM ANYLRYDVYD LELTKVTDNS ELRALLIQTT NRSVIVIEDI
     DCSLELTGDR DSKVHKLRSG INNNTNGGND HEDGHVTLSG LLNFTDGLWS CCGEERIIVF
     TTNHKDGVDP ALVRAGRMDV HVRLGTCGIH AFKELVKGYL GVEEHDLFHV AESCIRAGGA
     LTPAEVGEVL LRNRDNVDVA VREVVAEMQG RVLRGGGSKD CNGEESNTGD SDLDEETSPT
     GSWELGLSTT TAYTRESERK RKTRSTSAST WEKKVKFLTR LRSLTKSESG RRGV
//
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