KPC1_CANAX
ID KPC1_CANAX Reviewed; 1097 AA.
AC P43057;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein kinase C-like 1;
DE Short=PKC 1;
DE EC=2.7.11.13;
GN Name=PKC1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX PubMed=8813761;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<741::aid-yea967>3.0.co;2-g;
RA Paravicini G., Mendoza A., Antonsson B., Cooper M., Losberger C.,
RA Payton M.A.;
RT "The Candida albicans PKC1 gene encodes a protein kinase C homolog
RT necessary for cellular integrity but not dimorphism.";
RL Yeast 12:741-756(1996).
CC -!- FUNCTION: Necessary for osmotic stability.
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; X81142; CAA57048.1; -; Genomic_DNA.
DR PIR; S47220; S47220.
DR AlphaFoldDB; P43057; -.
DR SMR; P43057; -.
DR BindingDB; P43057; -.
DR ChEMBL; CHEMBL5515; -.
DR VEuPathDB; FungiDB:C3_04470W_A; -.
DR VEuPathDB; FungiDB:CAWG_02760; -.
DR BRENDA; 2.7.11.13; 1096.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0005856; C:cytoskeleton; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0030427; C:site of polarized growth; IEA:EnsemblFungi.
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:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IEA:EnsemblFungi.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
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; 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; 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; Calcium; Coiled coil; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1097
FT /note="Protein kinase C-like 1"
FT /id="PRO_0000055739"
FT DOMAIN 2..76
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 106..183
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 189..311
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 770..1029
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1030..1097
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 415..462
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 304..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 895
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 776..784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1097 AA; 125312 MW; EC48A14575F26CD5 CRC64;
MSTSQPSQQQ NPEQVVNDIR QKIEKERKII QGFNDVKRNT NNPEVIQKWK SKIIESQSMI
DYYQETMNKL TRQMQRLNTN SSSRTASRSS VISEYKPSYS NFDLIKYECP SLGNKIQFML
QYLEFKLQVE NKYSEANKKL SHLYLMDGDK SSSNAAEGGR AESDQRIQLL EKALKKYQKF
SINDHEFDRD YEIMDSTKHS RKLLTGRLTV SITCIRDVDH IATALAKKRE TVVVIKVDDL
EKARTKPSKN DNWNEEMVID VDKSHEIELA VMDKQNGIYV PVAVNWFSLF DLAEEIRKKK
VAKDQGSSGW LPAANLPQTG GSGAGTGSSM TGGASYGATS PLPAHNDLRP SVSPSSDAKE
NKVSVSTWLS LEPGGQMLIN LNFEKSITNG KQFRGPLGRH GAIRQKKEEV FEKHGHQFVQ
KQFYNIMSCA LCGEFLRYTG YQCQDCKFLC HKKCYQKVVT KCISKSGSDY DAAQLNHRIP
HRFEPITNHG TKWCCHCGYI LPWGKKNVRK CTECGVMCHA QCTHLVPDFC GMSLQMANEI
LATIESTKVS PKKAQHQQSH AKPLPPKPPI ESKPSMDSEE TLHNEPSYKS LRPASVVHQD
TNFVSKLPTT VQNKYQEPVE LPPQQQNQVV PSTRRRGHGS TDLSFETGYG QQQHQHHRDV
PQIVVEDHQH YNSNDNRDVE MEESKDEFDN FDYNNKYTEN EILTDVQQDQ VRSPFADQIQ
GVPETSHAKQ QNQQVQQVQQ QEELGHQRTH SSGKSGKSKR RKRKVGLDDF QFLAVLGKGN
FGKVMLAESR HTSKLCAIKV LKKDFIVEND EAESVKSEKR VFLTANKEMH PFLLNLHCCF
QTENRIYFVM EYISGGDLMW HIQKNRFTAK RAKFYACEVL LGLKYFHDNG IVYRDLKLDN
ILLTTKGHIK IGDYGLCKED MWHKSTTSTF CGTPEFMAPE IVAGKAYDRS VDWWAFGVLL
FQMLLCQSPF KGDDEDDIFN AIENDEVKYP INLSRQTVLV LQALLTKDPS QRLGSGPKDA
EEIMEHPYFH DVNFDDVLNC RIPAPYIPEV QSEHDYSNFD KEFTSETPRL TPVETVLTSE
MQEQFRGFSH ISDNATI
