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Database: UniProt
Entry: A0A314KV84_NICAT
LinkDB: A0A314KV84_NICAT
Original site: A0A314KV84_NICAT 
ID   A0A314KV84_NICAT        Unreviewed;       813 AA.
AC   A0A314KV84;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Wall-associated receptor kinase 2 {ECO:0000313|EMBL:OIT32887.1};
GN   Name=WAK2_2 {ECO:0000313|EMBL:OIT32887.1};
GN   ORFNames=A4A49_15427 {ECO:0000313|EMBL:OIT32887.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451 {ECO:0000313|EMBL:OIT32887.1, ECO:0000313|Proteomes:UP000187609};
RN   [1] {ECO:0000313|EMBL:OIT32887.1, ECO:0000313|Proteomes:UP000187609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC   TISSUE=Leaves {ECO:0000313|EMBL:OIT32887.1};
RA   Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Baldwin I.T.;
RT   "The genome of Nicotiana attenuata.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000327};
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         Evidence={ECO:0000256|ARBA:ARBA00000671};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:OIT32887.1}.
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DR   EMBL; MJEQ01000977; OIT32887.1; -; Genomic_DNA.
DR   RefSeq; XP_019225113.1; XM_019369568.1.
DR   AlphaFoldDB; A0A314KV84; -.
DR   STRING; 49451.A0A314KV84; -.
DR   EnsemblPlants; OIT32887; OIT32887; A4A49_15427.
DR   GeneID; 109206715; -.
DR   Gramene; OIT32887; OIT32887; A4A49_15427.
DR   KEGG; nau:109206715; -.
DR   OrthoDB; 101939at2759; -.
DR   Proteomes; UP000187609; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005:SF332; WALL-ASSOCIATED RECEPTOR KINASE 2-LIKE; 1.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OIT32887.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:OIT32887.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187609};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..813
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016437678"
FT   DOMAIN          292..336
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          337..371
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          465..742
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          34..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..58
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   813 AA;  89535 MW;  5E7DB9C0857F39FF CRC64;
     MQHKQVPLFS FQLPCFFSFV LILTLATAQI ITISPPPPPP TTSPPPTNTT PPPTNTTSPP
     TNTTITKAAN ITKPGCQKQC GNLTVPYPFG IGIGSGCAID PSFEINCDTI TTGSPTPLLG
     NIKIYDISDS EMRISSVLNR RCYSSTGVLI LDQPAWMTLG SSSPYSFSSL NRFSVVGCDE
     AAIIVGDDFA NGCPTVCTTS SDVIEGRCMG AGCCQITIPK GLKYFNTSMQ SSKLNHTAVW
     SYSKCGYAFL GEASRFEFKG LQDLSDLDFV KKIKNNVPIV LDWAIGNLTC VEAQKRNDYA
     CLDNSQCVDS DNDIGGYRCS CNSGYEGNPY IGSGCQDIDE CADPNTNSCE KTCINMPGSY
     NCTCPKGHTG DGRKNGRGCI APNSNSEFPW IKFSVGMGVG FMSLVVGTTW LYFSIKKSKL
     IKLREKFFQQ NGGLLLKQRI SSDEGGMEAT KVFTAEELKK ATNSYANDRI LGRGGNGIVY
     KGILPDNRIV AIKKSKFVDE DQVEQFINEV LILTQVNHRN VVRLFGCCLE AEVPLLVYEY
     VSHGTLYEHI HNQNGAPWLS WQNRLRVATE TASALAYLHS SALMPIIHRD VKSANLLLDD
     VYTAKVADFG ASRLIPLDQT HLATLVQGTL GYLDPEYFRT SQLTEKSDVY SFGVVLAELL
     TGIKPISRDK NNEDKNLAEY FVLSMRKNQL FQILDRRVVR EGSLEQLQKV AELVKSCLSL
     HGEDRPTMKE VAMELESLRK FTKNNPWPSG HGHHEENEDE SSDLYTIQFD SNTGVNNLSG
     QYNSNSTTNN TSNFSGQYSV DSSSFIFNRN IPR
//
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