ID   KPC1_NEUCR              Reviewed;        1142 AA.
AC   P87253; Q7RVG4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Protein kinase C-like;
DE            EC=2.7.11.13;
GN   ORFNames=NCU06544;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Arpaia G., Macino G.;
RT   "Molecular cloning of a protein kinase C homologue from Neurospora
RT   crassa.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000305}.
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DR   EMBL; Y12002; CAA72731.1; -; Genomic_DNA.
DR   EMBL; CM002239; EAA33015.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87253; -.
DR   SMR; P87253; -.
DR   BioGRID; 1979838; 1.
DR   FunCoup; P87253; 400.
DR   STRING; 367110.P87253; -.
DR   PaxDb; 367110-P87253; -.
DR   EnsemblFungi; EAA33015; EAA33015; NCU06544.
DR   KEGG; ncr:NCU06544; -.
DR   VEuPathDB; FungiDB:NCU06544; -.
DR   HOGENOM; CLU_000288_54_0_1; -.
DR   InParanoid; P87253; -.
DR   OMA; QCTHLVP; -.
DR   OrthoDB; 63267at2759; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0030428; C:cell septum; IDA:CACAO.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   CDD; cd20822; C1_ScPKC1-like_rpt1; 1.
DR   CDD; cd20823; C1_ScPKC1-like_rpt2; 1.
DR   CDD; cd08689; C2_fungal_Pkc1p; 1.
DR   CDD; cd11620; HR1_PKC-like_2_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:000014; Protein kinase C; 1.
DR   FunFam; 3.30.60.20:FF:000034; Protein kinase C; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 1.10.287.160; HR1 repeat; 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; IPR037778; C2_fungal_PKC.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR037312; PKC-like_HR1.
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; 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; Coiled coil; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1142
FT                   /note="Protein kinase C-like"
FT                   /id="PRO_0000055744"
FT   DOMAIN          1..67
FT                   /note="REM-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          149..226
FT                   /note="REM-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          231..349
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          817..1076
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1077..1142
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ZN_FING         457..505
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         525..576
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          70..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..724
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..765
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        942
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         823..831
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         846
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        914
FT                   /note="F -> L (in Ref. 1; CAA72731)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1055..1056
FT                   /note="EP -> DA (in Ref. 1; CAA72731)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1142 AA;  127972 MW;  A7462CDFD1848DAD CRC64;
     MNDEDKVHDI SKKIEREKAL INAAQAMRQQ TNNEQVRSKL DTQMREGRRN LEFFEEKLRE
     LQMRRLGHGV DNMSLGASPM SGSHRQSVDD FEGYGAPSPP PKEDVRGHSS HQSQGSGPLM
     PASAPYPGGP PDSNVPRARP NYTRLDLIKF DTPHLGPRIQ LMLSQIQFKL NVEEQYLKGI
     EKMVQLYQME GDKKSKLDAA AKRVESKQKI VLLKQALKRY EELHIDIDVD GPDDDSINLP
     ALRKPLSGTL SIRILAVKDV DHAPLGRFAR SPETFIAVKA EDIVVARTKP SRNDKWEAEF
     HTFPVDKTNE IEFTVYDKPA EHPVPIAMLW VRISDIVEEL RRKKIEAEMT SAGWVSADRV
     GSRAPPPQFP MGAQSPQFAA PPTSPGSQEQ NTMIPPQAPP PSQVVSQPVD GWFNLEPYGQ
     IHLSFNFIKG ARPQGMDRLG RKGAVRQRKE EVHEMYGHKF VQKQFYNIMR CALCGDFLKY
     SAGMQCEDCK YTCHTKCYTS VVTKCISKSN AETDPDEEKI NHRIPHRFIP FSNLTANWCC
     HCGYMLPIGS KKNSRKCSEC ALTAHAQCVH LVPDFCGMSM AVANQILEGM RTQKKTHKDK
     ASSMSERTLR PGSKTSISSG SIAQASTYSG STAYTSIASP EATEAAKLMY SQTTPRPGGP
     DRTSTSSTTA SAAAAAAMAP KHSSQPSQAG SIPDFGGSPG YGRPDSRDDE YSAQQQQGYG
     SPQQRKYNPA DYANIDAYSS PQARPQQQQQ QQQQTPQQVS PMYQQNPQTP ISKPQPVAPS
     YDNQVVPSAS GVPVPTKKPL PSATDPGTGM RIGLDHFNFL AVLGKGNFGK VMLAETKKSR
     KLYAIKVLKK EFIIENDEVE SIRSEKRVFL IANRERHPFL TNLHACFQTE TRVYFVMEYI
     SGGDLMLHIQ RGMFGTKRAQ FYAAEVCLAL KYFHENGVIY RDLKLDNILL TLDGHIKIAD
     YGLCKEDMWY GSTTSTFCGT PEFMAPEILL DKKYGRAVDW WAFGVLIYQM LLQQSPFRGE
     DEDEIYDAIL ADEPLYPIHM PRDSVSILQK LLTREPDQRL GSGPTDAQEI MSQPFFRNIN
     WDDIYHKRVQ PPFLPQIKSA TDTSNFDSEF TSVTPVLTPV QSVLSQAMQE EFRGFSYTAD
     FE
//