ID   PCK1_SCHPO              Reviewed;         988 AA.
AC   P36582; Q9UTU9;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 210.
DE   RecName: Full=Protein kinase C-like 1;
DE            EC=2.7.11.13;
GN   Name=pck1; ORFNames=SPAC17G8.14c, SPAC22H10.01c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8491190; DOI=10.1002/j.1460-2075.1993.tb05848.x;
RA   Toda T., Shimanuki M., Yanagida M.;
RT   "Two novel protein kinase C-related genes of fission yeast are essential
RT   for cell viability and implicated in cell shape control.";
RL   EMBO J. 12:1987-1995(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 318-535.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Involved in the control of the cell shape. Target of the
CC       inhibitor staurosporine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=2.7.11.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000305}.
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DR   EMBL; D14337; BAA03267.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA93697.2; -; Genomic_DNA.
DR   EMBL; AB027982; BAA87286.1; -; Genomic_DNA.
DR   PIR; S35362; S35362.
DR   RefSeq; NP_593737.2; NM_001019168.3.
DR   AlphaFoldDB; P36582; -.
DR   SMR; P36582; -.
DR   BioGRID; 278761; 112.
DR   FunCoup; P36582; 268.
DR   STRING; 284812.P36582; -.
DR   iPTMnet; P36582; -.
DR   PaxDb; 284812-P36582; -.
DR   GeneID; 2542293; -.
DR   KEGG; spo:2542293; -.
DR   PomBase; SPAC17G8.14c; pck1.
DR   VEuPathDB; FungiDB:SPAC17G8.14c; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   HOGENOM; CLU_000288_54_0_1; -.
DR   InParanoid; P36582; -.
DR   OMA; QIMRCAV; -.
DR   PhylomeDB; P36582; -.
DR   BRENDA; 2.7.11.13; 5613.
DR   Reactome; R-SPO-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-SPO-114516; Disinhibition of SNARE formation.
DR   Reactome; R-SPO-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-SPO-1489509; DAG and IP3 signaling.
DR   Reactome; R-SPO-202424; Downstream TCR signaling.
DR   Reactome; R-SPO-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-SPO-2179392; EGFR Transactivation by Gastrin.
DR   Reactome; R-SPO-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-SPO-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-SPO-4419969; Depolymerization of the Nuclear Lamina.
DR   Reactome; R-SPO-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-SPO-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-SPO-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-76005; Response to elevated platelet cytosolic Ca2+.
DR   Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR   Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR   Reactome; R-SPO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR   Reactome; R-SPO-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells.
DR   PRO; PR:P36582; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0051285; C:cell cortex of cell tip; EXP:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000935; C:division septum; IDA:PomBase.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; EXP:PomBase.
DR   GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004699; F:diacylglycerol-dependent, calcium-independent serine/threonine kinase activity; EXP:PomBase.
DR   GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:1903500; P:negative regulation of mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR   GO; GO:1903139; P:positive regulation of cell integrity MAPK cascade; IMP:PomBase.
DR   GO; GO:1903617; P:positive regulation of mitotic cytokinesis, division site positioning; EXP:PomBase.
DR   GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR   CDD; cd20822; C1_ScPKC1-like_rpt1; 1.
DR   CDD; cd20823; C1_ScPKC1-like_rpt2; 1.
DR   CDD; cd11621; HR1_PKC-like_1_fungi; 1.
DR   CDD; cd05570; STKc_PKC; 1.
DR   FunFam; 1.10.510.10:FF:000101; Protein kinase C; 1.
DR   FunFam; 3.30.200.20:FF:000103; Protein kinase C; 1.
DR   FunFam; 3.30.60.20:FF:000064; Protein kinase C; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PKC_DAG/PE.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF02185; HR1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00742; Hr1; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF46585; HR1 repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51860; REM_1; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell shape; Coiled coil; Cytoplasm; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..988
FT                   /note="Protein kinase C-like 1"
FT                   /id="PRO_0000055740"
FT   DOMAIN          1..68
FT                   /note="REM-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          107..182
FT                   /note="REM-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          189..315
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          664..923
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          924..988
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ZN_FING         413..461
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         480..530
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          64..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..348
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..640
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        789
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         670..678
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         693
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        27..35
FT                   /note="AMVASTKNP -> SNGGFDGES (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   988 AA;  111784 MW;  0969BDEC1AB43C4E CRC64;
     MVQLDDALQD AYKKVEREES LILGAKAMVA STKNPEVKRR LESNIAVSEN NIKYLRERID
     ALKVESGSER ESQSDKDSSK KYSDSAKSTN SDDHLLSYNR SAFDLFNSEK PLSPEKISTM
     LQHLQMRLSI EQQCVSGIEK IMSLYSKEQK DKTDVIIKLK EGKQKVNLLK RSLKRYNELH
     IPFDISTPSS EEKQQASGLN FRGLAKPISG TLKVTIHSLR NIEHTSFLQT HSFTMPSYAV
     LYVDDAQVAK SRISQTDTWD ETFIFDVHRA KEFQIIIYEK KKDFDIPIAL ILIPTTIIAE
     ELRRKRNIQE MSETSWKPSI AESASRSDEK GSKSDPINAP NSSSSISTNS PLAPTAYYKL
     LSKSWLSLEP VGQICISLSF SKRTTKRQFP ETGLGRQGAI RQKKEDVVAS QVGHQFVQRQ
     FYQIMRCAVC AELFSYSPGL QCENCSFVCH KKCVTKVLAS CIAQSNSEKS DFGGLRYRIP
     HRFEPFNSLG AQWCAHCGFF LPLRRKDCFK CVECGITCHG QCAHLIPDYC GMSNDLKHQL
     LTELEVSKRP KKPELPNQEN KTTNEKVYRK PLSSQNTFDT LPTISQGLLA ATQPVTSVLN
     TSPLPKTPEK DRSLNVTPSS STPTPASVLA PPSSASLSSS KDANRSVPES PRREKKNRVT
     LDDFTFLAVL GKGNFGKVML AEYKVNKKFY AIKVLKKEAI LKNEELESLK TEKHVFEVAN
     KEKHPFLLNL FASFQTSTRV YFVMEYILGG DLMVHIQRQQ FSVKRARFYG AEVCLALKYF
     HENGIAYRDL KLDNILLCPD GHIRIADYGL CKENMLLGNT TSTFCGTPEF MAPEILLEQQ
     YSKDVDWWAF GVLMYQMLLG QSPFKGEDEE EIFDAILSDE PLFPINMPAD AVSLLRGLLT
     RDPNQRLGSG PKDANEVMAH PFFASIVWDD LYNKLYEPSY KPLINDPRDL NNFDEEFTSA
     CPTLTPVNTV LTRQQQECFR GFSSFATE
//