KPC1_COCHE
ID KPC1_COCHE Reviewed; 1174 AA.
AC O42632;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein kinase C-like;
DE EC=2.7.11.13;
GN Name=PKC1;
OS Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris
OS maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5016;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 48329 / C2;
RX PubMed=9742699; DOI=10.1111/j.1574-6968.1998.tb13157.x;
RA Oeser B.;
RT "PKC1, encoding a protein kinase C, and FAT1, encoding a fatty acid
RT transporter protein, are neighbors in Cochliobolus heterostrophus.";
RL FEMS Microbiol. Lett. 165:273-280(1998).
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=2.7.11.13;
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=2.7.11.13;
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; Y15839; CAA75801.1; -; Genomic_DNA.
DR PIR; T43051; T43051.
DR AlphaFoldDB; O42632; -.
DR SMR; O42632; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR CDD; cd08689; C2_fungal_Pkc1p; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 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; IPR002219; PE/DAG-bd.
DR InterPro; IPR037312; PKC-like_HR1.
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 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; SSF46585; SSF46585; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
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; Repeat; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1174
FT /note="Protein kinase C-like"
FT /id="PRO_0000055743"
FT DOMAIN 1..68
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 229..349
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 849..1108
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1109..1174
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 458..506
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 526..576
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 69..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 974
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 855..863
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 878
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1174 AA; 130506 MW; 26A4ADD42849F37C CRC64;
MANVEETVAN VQRKIDREKA LINAANAMRQ STNNPAVLSR LDGQIKDGRR NIDYFESKLR
DLDLQRTTSG VDNMSLQPGR SPTNPLTPPP KDNWDGYAQQ DQGGYGGPQS QYSQLSGGEA
LQPPRAPFAA PPPATANKRP NYSKLDLIKY DTPHLGPRIQ LMLTQLEFKL SVEKQYKDGI
EKMVRLYQME GDRKSKQDAE AKRIESNQKI QLLKHSLKRY EDLHVDIDGD GDDNDSLDIP
SQRKPLSGQL SLRIHAVADV DHAATGRFSR GPETFVNIKV EDTIKGRTKP TRNDRWTDEV
HDFSIDKANE IEITVYDKTG DHLLPIGMLW VRISDIAEEM RRKKLETELA NSGWVAADKM
GGHTGIQPDM QFQPPPGQSP AGGPGGGPTP AGVRPPGAPQ PQTGPIMIDD WFSLEPVGRI
HLTMSFIKNT GNKQPFDLGL GRKGAVRQRK EDVVEQYGHK FVQQQFYNVM RCALCAEFLK
YAAGMQCSDC NYTCHKKCYP KVVTKCITQS NAETDPDEAK LNHRIPHRFE NFSNMGANWC
CHCGYVLPLG RKQTKKCNEC GLTCHAHCVH FVPDFCGMSM EVANQILMEI KRTRRGQSSS
GPGMSQRTLR PQSAAKPLPP TQPQSPGQPG QESPTQSDRY SYGKEQMSPP PGPPRQPSYP
SSATSVDAAR ASYSTTGTAS TGAPTSPTSG SRPPSGPRTQ SSVAAAAAAM NKATQPGYGR
SNTDYSPQSG RSSGSGYPTE QRMSQQQAPQ PAAYDPSVYA NIPSYPPSHQ QPAPVPSYPT
KSSYPLPQPP PPQSPPQHPQ QPTPSQQKMP EQQALTQQPP SAVGEVPGKK VTPAANTQGT
GKRIGLDHFN FLAVLGKGNF GKVMLAETKT TKQLYAIKVL KKEFIIENDE VESTRSEKRV
FLIANKERHP FLLNLHACFQ TETRVYFVME YISGGDLMLH IQRGQFGTKR AQFYAAEVCL
ALKYFHENGV IYRDLKLDNI MLTLDGHIKV ADYGLCKEEM WYGSTTSTFC GTPEFMAPEI
LLDKKYGRAV DWWAFGVLIY QMLLQQSPFR GEDEDEIYDA ILADEPLYPI HMPRDSVSIL
QKLLTREPEM RLGSGPTDAQ EIMSHAFFRN INWDDIYHKR VQPPFIPQIT SPTDTSNFDT
EFTSVTPVLT PVQSVLSQAM QEEFRGFSYS ADFA
