ID A0A0K9P2Q7_ZOSMR Unreviewed; 625 AA.
AC A0A0K9P2Q7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN ORFNames=ZOSMA_45G00360 {ECO:0000313|EMBL:KMZ62495.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ62495.1, 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the SELO family.
CC {ECO:0000256|ARBA:ARBA00009747}.
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:KMZ62495.1}.
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DR EMBL; LFYR01001351; KMZ62495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9P2Q7; -.
DR STRING; 29655.A0A0K9P2Q7; -.
DR OMA; YGPYGWL; -.
DR OrthoDB; 5487961at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
DR GO; GO:0070733; F:AMPylase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00692; SelO; 1.
DR InterPro; IPR003846; SelO.
DR PANTHER; PTHR32057; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR PANTHER; PTHR32057:SF14; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR Pfam; PF02696; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..625
FT /note="Selenoprotein O"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005527363"
SQ SEQUENCE 625 AA; 69629 MW; 91E777BBA16AE9D7 CRC64;
MLCNFHILLS CSPATSSVTT TSAVLRRFRS PGHPSFGFFS RRVWHRVIAP PLHLCRSSEF
GTVSLGPKQG EGIVKGQRKM GTSLEDLNWD QTFIRELPGD LRTDSIPRQV LHACYTRIAP
SVEVDKPELV VSSESVAELL GLDKKEFERP DFPLIFSGAS PLVGGLPYAQ CYGGHQFGSW
AGQLGDGRAI TLGELVNFNG ERWDLQLKGA GKTPYSRFAD GLAVLRSSIR EFLCSEAMNG
LGIPTTRALC LVTTGKTVVR DMFYNGNSKA EPGAIVCRVA QSFLRFGSYQ IHVNRVKEDV
GIVRNLADYT IRHHFPHIDK MNKSDKLSSE ADQEGSSLGN LSSNKYAAWS VEVAERTASL
VARWQGVGFT HGVLNTDNMS VLGLTIDYGP FGFLDVFDPN YTPNTTDLPG RRYCFANQPD
IGLWNVAQFA TTLAAADLIS KEEADYSMER YGVKFMDEYR SIMTQKLGLS KYNKELIGKL
LNNLAVDKVD YTNFFRLLSN VKADPTIEEG SLLVPFKDVL LNIKDERREA WSSWIKVYIS
ELISSGISDE ARKTAMNSVN PKYILRNYLC QIAIDAAEQG DYGEVRQLFK VMEHPFDEQE
GMEKYARLPP EWASRPGVCM LSCSS
//
