ID   RKIN1_SECCE             Reviewed;         502 AA.
AC   Q02723;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Carbon catabolite-derepressing protein kinase;
DE            EC=2.7.11.1;
GN   Name=RKIN1;
OS   Secale cereale (Rye).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX   NCBI_TaxID=4550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endosperm;
RX   PubMed=1924320; DOI=10.1073/pnas.88.19.8602;
RA   Alderson A., Sabelli P.A., Dickinson J.R., Cole D., Richardson M.,
RA   Kreis M., Shewry P.R., Halford N.G.;
RT   "Complementation of snf1, a mutation affecting global regulation of carbon
RT   metabolism in yeast, by a plant protein kinase cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8602-8605(1991).
CC   -!- FUNCTION: Essential for release from glucose repression.
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   -!- 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;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR   EMBL; M74113; AAA33921.1; -; mRNA.
DR   PIR; A41361; A41361.
DR   AlphaFoldDB; Q02723; -.
DR   SMR; Q02723; -.
DR   BRENDA; 2.7.11.1; 5654.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR001772; KA1_dom.
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; IPR015940; UBA.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..502
FT                   /note="Carbon catabolite-derepressing protein kinase"
FT                   /id="PRO_0000086614"
FT   DOMAIN          14..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          290..330
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          453..501
FT                   /note="KA1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  57711 MW;  0C9AF827F8989927 CRC64;
     MDGGGEHSEA LKNYYLGKIL GVGTFAKVII AEHKHTRHKV AIKVLNRRQM RAPEMEEKAK
     REIKILRLFI DLIHPHIIRV YEVIVTPKDI FVVMEYCQNG DLLDYILEKR RLQEDEARRT
     FQQIISAVEY CHRNKVVHRD LKPENLLLDS KYNVKLADFG LSNVMHDGHF LKTSCGSLNY
     AAPEVISGKL YAGPEIDVWS CGVILYALLC GAVPFDDDNI PNLFKKIKGG TYILPIYLSD
     LVRDLISRML IVDPMKRITI GEIRKHSWFQ NRLPRYLAVP PPDMMQQAKM IDEDTLRDVV
     KLGYDKDHVC ESLCNRLQNE ETVAYYLLLD NRFRATSGYL GAHYQQPMES ASPSTRSYLP
     GSNDSQGSGL RPYYRVERKW ALGLQQSRAP PRAIMIEVLK ALKELNVCWK KNGDCYNMKC
     RWCPGFPRVS DMLLDANHSF VDDCAIKDNG DANSRLPAVI KFEIQLYKTK DDKYLLDMQR
     VTGPQLLFLE FCAAFLTNLR VL