SRK2A_PHYPA
ID SRK2A_PHYPA Reviewed; 349 AA.
AC A9TF79;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein kinase SRK2A {ECO:0000303|PubMed:27268428};
DE EC=2.7.11.1 {ECO:0000269|PubMed:27268428};
DE AltName: Full=SNF1-related kinase 2A {ECO:0000305};
DE Short=PpSnRK2A {ECO:0000303|PubMed:27268428};
GN Name=SRK2A {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_194508 {ECO:0000312|EMBL:EDQ57933.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1] {ECO:0000312|EMBL:EDQ57933.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27268428; DOI=10.1105/tpc.15.00774;
RA Bressendorff S., Azevedo R., Kenchappa C.S., Ponce de Leon I., Olsen J.V.,
RA Rasmussen M.W., Erbs G., Newman M.A., Petersen M., Mundy J.;
RT "An innate immunity pathway in the Moss Physcomitrella patens.";
RL Plant Cell 28:1328-1342(2016).
CC -!- FUNCTION: Involved in early responses to osmotic stress.
CC {ECO:0000269|PubMed:27268428}.
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:0000269|PubMed:27268428};
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:0000269|PubMed:27268428};
CC -!- ACTIVITY REGULATION: Activated by osmotic stress and by abscisic acid
CC (ABA). Activation by NaCl is dependent on ABA.
CC {ECO:0000269|PubMed:27268428}.
CC -!- INDUCTION: Up-regulated in response to NaCl treatment.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DISRUPTION PHENOTYPE: Significantly reduced levels of SnRK2 proteins
CC activated by NaCl or abscisic acid (ABA) compared with wild-type.
CC {ECO:0000269|PubMed:27268428}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; DS545107; EDQ57933.1; -; Genomic_DNA.
DR RefSeq; XP_001777278.1; XM_001777226.1.
DR AlphaFoldDB; A9TF79; -.
DR SMR; A9TF79; -.
DR STRING; 3218.PP1S218_59V6.1; -.
DR EnsemblPlants; Pp3c5_21160V3.1; Pp3c5_21160V3.1; Pp3c5_21160.
DR EnsemblPlants; Pp3c5_21160V3.3; Pp3c5_21160V3.3; Pp3c5_21160.
DR Gramene; Pp3c5_21160V3.1; Pp3c5_21160V3.1; Pp3c5_21160.
DR Gramene; Pp3c5_21160V3.3; Pp3c5_21160V3.3; Pp3c5_21160.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; A9TF79; -.
DR OMA; TISNQCD; -.
DR OrthoDB; 1017936at2759; -.
DR Proteomes; UP000006727; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..349
FT /note="Serine/threonine-protein kinase SRK2A"
FT /id="PRO_0000443380"
FT DOMAIN 12..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 151..177
FT /note="Activation loop"
FT /evidence="ECO:0000250|UniProtKB:Q940H6"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 349 AA; 39617 MW; D4DF8DB7443D7881 CRC64;
MDIPSMHDHD RYELVKDIGS GNFGVARLMR DKKTRELVAV KYIERGEKID ENVQREIINH
RSLRHPNIVR FKEVMLTPTH LAIVMEYAAG GELFERICNA GRFSEDEARF FFQQLISGVS
YCHSMQICHR DLKLENTLLD GSPAPRLKIC DFGYSKSSLL HSQPKSTVGT PAYIAPEVLS
KKEYDGKIAD VWSCGVTLYV MLVGAYPFED PEDPRNFRKT IGRILSVQYS IPDYVHISVE
CRHLLSRIFV ANPAKRINIQ EIKNHEWFLK NLPADLVDLA DRSYDFEDPN HPPQSIEEIM
RIISEARVLG TGATGDYFGD SVDDMDLEND VDPDADPDVG SSGEFVCAM
