ID   KIN1_ENTBH              Reviewed;         595 AA.
AC   B7XHR6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable serine/threonine-protein kinase KIN1 homolog;
DE            EC=2.7.11.1;
GN   Name=KIN1; ORFNames=EBI_21713;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA   Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(2009).
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; ABGB01000015; EED44563.1; -; Genomic_DNA.
DR   RefSeq; XP_002649544.1; XM_002649498.1.
DR   AlphaFoldDB; B7XHR6; -.
DR   SMR; B7XHR6; -.
DR   STRING; 481877.B7XHR6; -.
DR   PRIDE; B7XHR6; -.
DR   EnsemblFungi; EED44563; EED44563; EBI_21713.
DR   VEuPathDB; MicrosporidiaDB:EBI_21713; -.
DR   HOGENOM; CLU_000288_59_11_1; -.
DR   InParanoid; B7XHR6; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
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; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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..595
FT                   /note="Probable serine/threonine-protein kinase KIN1
FT                   homolog"
FT                   /id="PRO_0000385509"
FT   DOMAIN          67..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         73..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   595 AA;  69212 MW;  0D521D39117D98FA CRC64;
     MQSTSKYNCD SDYIAGRNYN TKRTNGREEL STGLTNEETG VVNISDENNI FFKKNIDYVK
     GSRIGKYKLI KTLGKGSCAK VVQAEDCETG EYVAIKIIER TPKQLSDIRI YREALICSLF
     NHPHIIKLLD FFHTTEYFFL IFEYVDGQQL YDIILNKGYL DEDEARKYFR QIISAVDYSH
     RNSVVHRDLK IENILIDRND NIKLIDFGLS NFYDADDLLG TFCGSLYFAA PELLLGTRYT
     GPEIDVWSLG VILYVMLVGK VPFDDENIHA LQNKIKSCKF KFEKTISPEA QDLITNMILS
     SDARINLENV KKSKWTNLGY KNLTNNFMTL RKPIIEINKN ILRALQAAMF FQFTDMERVL
     MQYLQICKGD KHSLEQTYWC KKPVVILYYL TMEKFNELNY KSIPIDIDTG MNTKSLIDIT
     IEKQPIIIYN FVRFTNAKKN NNPYNLFFSR SVFEPEMEFL NMTKDVSLDS CNISEDENKK
     HNFPKIKQSI IKGLFKGIKI KNGDKDYVKN AIIKILLDLD ITYEANEKSY FCSYSHSGVE
     CHFKIDLYFN ILLLEHYVVL NCLNRKKDNF KLVTELIKEK LEEIGDTSNY PENAI