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Database: UniProt
Entry: A0A0K9NY81_ZOSMR
LinkDB: A0A0K9NY81_ZOSMR
Original site: A0A0K9NY81_ZOSMR 
ID   A0A0K9NY81_ZOSMR        Unreviewed;       647 AA.
AC   A0A0K9NY81;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=ZOSMA_56G01260 {ECO:0000313|EMBL:KMZ60895.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ60895.1, 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 + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:KMZ60895.1}.
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DR   EMBL; LFYR01001565; KMZ60895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9NY81; -.
DR   STRING; 29655.A0A0K9NY81; -.
DR   OMA; GWRYEEE; -.
DR   OrthoDB; 53548at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13983; STKc_WNK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   PANTHER; PTHR13902:SF132; SERINE_THREONINE-PROTEIN KINASE WNK4-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KMZ60895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Transferase {ECO:0000313|EMBL:KMZ60895.1}.
FT   DOMAIN          33..291
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          408..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  73597 MW;  9D226B4E12C7CCE8 CRC64;
     MSCSNLFEMP RCGGGEDSDE SYYAEIDPTG RYGRFNQVLG KGAMKTVYRA FDEVNGIEVA
     WNQARVCNVL RSPLALEHLY SEVNLLSILK HDSIMQFHST WTDPVKGTFN FITEMFTSGS
     LREYRQKYKR VNIKAVKNWA RQILHGLVYL HEHDPPVIHR DLKCDNIFVN GNLGQVKIGD
     LGLAAFLRNS QPAHSVIGTP EFMAPELYEE EYNELVDIYS FGMCVLEMLT SEYPYSECSN
     PAQIYKKVTS GKLPSAFYKI QDEESRIFIG RCLESASRRS SAKDLLFDPF LQDSNLPNDL
     APSHSLLSDQ EDQQEQEDII NTDMKITGKM NPDDDAIFLR VHFADKTGHT RNIYFPFDII
     RDTPIDVADE MVKELDIVDH DPSHIAEMID VEISALVPDW KDRRNHITNN VSDDDYNDED
     NDGDNNHHPG GDDDASSHHH FFYLSSSASS HSSGVSQQAR THSSTHGNHH GTYHSQEYIQ
     ARKIFHDEGD EITSQNSIYY DKHSDVNSNM KNEVVGTESS QWRDHLQHNQ KVTRFGPEEN
     NHTDHAKYAD SNSTEDGSDH SHSKNRRSKK VSARGELTRN RSLVNIRSQM LHRTIVEEVN
     KRMFNSVGSM EDIGFQNPCQ SSSVGKTKRD SCRLGKKNVG LTWGTSQ
//
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