ID   KIN1_ENCCU              Reviewed;         566 AA.
AC   Q8SW31;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable serine/threonine-protein kinase KIN1 homolog;
DE            EC=2.7.11.1;
GN   Name=KIN1; OrderedLocusNames=ECU03_0980;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA   Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA   Barton G.J.;
RT   "The complement of protein kinases of the microsporidium Encephalitozoon
RT   cuniculi in relation to those of Saccharomyces cerevisiae and
RT   Schizosaccharomyces pombe.";
RL   BMC Genomics 8:309-309(2007).
CC   -!- FUNCTION: Serine/threonine protein kinase involved in regulation of
CC       exocytosis. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR   EMBL; AL590443; CAD26242.1; -; Genomic_DNA.
DR   RefSeq; NP_597607.1; NM_001040971.1.
DR   AlphaFoldDB; Q8SW31; -.
DR   SMR; Q8SW31; -.
DR   STRING; 284813.Q8SW31; -.
DR   GeneID; 858769; -.
DR   KEGG; ecu:ECU03_0980; -.
DR   VEuPathDB; MicrosporidiaDB:ECU03_0980; -.
DR   HOGENOM; CLU_000288_59_11_1; -.
DR   InParanoid; Q8SW31; -.
DR   OMA; CIRENGV; -.
DR   OrthoDB; 1127668at2759; -.
DR   Proteomes; UP000000819; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006887; P:exocytosis; 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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Exocytosis; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..566
FT                   /note="Probable serine/threonine-protein kinase KIN1
FT                   homolog"
FT                   /id="PRO_0000385508"
FT   DOMAIN          58..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         64..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   566 AA;  65455 MW;  1DB7C5C66B846200 CRC64;
     MRSEEEMQSC TDSEMEGGED ETSGFMDESA ISNPFREREM RGMIGDFEYI EGKWIGSYRF
     VKQLGTGSSS KVVLGRDVRS GEKVAIKIIP RRVNGGETGD MEMRCDQRVF REVIISSVLN
     HPHIARLKNF LYSPTHYFLI FEYVKGRQLY DIIISSGPLK EKEGQRYFRQ LLSAIDYIHR
     NSVVHRDLKI ENILIDENDN VKLIDFGLSN FYDNKTLLNT FCGSLYFAAP ELLQGQRYCG
     PEIDVWSLGV VLYAILCGCV PFDDEDVQGL QAKIMDADFK FCKTISREAM ELIRGMIVAQ
     PSSRMGLSQV IGSEWVNKGQ KSRINSYAAK RYPIMKLNEK YIRPISRAIR FQFPNMEREI
     RRFHKICREE IGTLEQIYWS RRPVVSLYYL VSENLGGDDE NEAYTDDGEE EPPQELPEAV
     HDFVRFMFSK EKGCGPRHVK KEVFLTSTSQ DSLCSVKGKD CGLPQVRQTY LKGFFKGIRV
     KHIGSHNALK KVLLDIFNAN NIIYEITEKS YFCSAYHEDL ECLFKVSMYF NVLLNEYYLT
     VTPLNSERKV FRNVYEWISS GLRNRV