ID H6C6L6_EXODN Unreviewed; 1164 AA.
AC H6C6L6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN ORFNames=HMPREF1120_07353 {ECO:0000313|EMBL:EHY59362.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY59362.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY59362.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY59362.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000946};
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; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; JH226135; EHY59362.1; -; Genomic_DNA.
DR RefSeq; XP_009159823.1; XM_009161575.1.
DR AlphaFoldDB; H6C6L6; -.
DR STRING; 858893.H6C6L6; -.
DR GeneID; 20311992; -.
DR VEuPathDB; FungiDB:HMPREF1120_07353; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_54_0_1; -.
DR InParanoid; H6C6L6; -.
DR OMA; NRIYFAM; -.
DR OrthoDB; 21591at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 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; 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 PANTHER; PTHR24351:SF228; PROTEIN KINASE C; 1.
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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHY59362.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..68
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 167..244
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 248..368
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 472..520
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 540..590
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 839..1098
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1099..1164
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 66..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 868
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1164 AA; 130502 MW; 83F8F835F4E3CC3A CRC64;
MADTDQAIAE VYRKIEREKA LINAATHMRQ STNNAAVQAR VDSNIRDGRR NITYLEDKLQ
ELQLRKQGGP NEDGAPAPPV HGGAGYQTSA ARGQRPYPGG NAPTPPPKDQ RGYFSGDRGD
YGDPGAGGYS QGGTGTMPPR APYGDPRPYE TPIPKARPNF SKLDLIKYDT PYLGPKIQLM
LSQLEFKLSV EKQYKAGIEK MVRLYQDEGD RKSRLDAEGR RIESNQKVQL LKQALKRYMD
LHVDIESSDG ADDDSLNAPN MRKPLTGHLE MRIHAIKDVD HAASSRFSRG PETFVIMKVE
DNIRAKTRAT RTDKWTEEIH HVDIDKANEI ELTVYDKAGD RPTPIGFLWI RISDIAEEMR
RKKIESEFQQ NGWVSADKMA NGGSTGKPPG SDFQPAPFMP PGDSAGAGSA AGFPQHAQPI
MIDSWFSLEP AGRIHLTMSF QKQTGARRPF DIGLNRQGAV RQKKEEVHEK QGHKFVKQQF
YNVMRCALCG EFLKYSAGMQ CADCKYTCHT KCYPKVVTKC ISKANYETDP DEEKINHRIP
HRFDNFSNIG ANWCCHCGYL LPLGRRNAKR CSECGLTCHA HCQHLVPDFC GMSMIVANEI
LETIQRTKHH NKSSSVSSGM SGRTLRPNSG RPGPASPTQS YTSDAASLTP QISNQSYDYH
PEQTKPSPAA KSAAQNLMYN HPQQAQSQQP QRPIPHRPVS ATAIQAAAAA TSRPPSQPYG
HGASDYGPQK VAVDRYANAR PPAPEAQPPH ASYDPRAYQQ YDRQPMQQQQ QQPPQMQHQP
PQQAVVPQQR PQQVQPSYAP APAKPAPSQQ QQQQQQQQQQ VATPVSGRGS GPRIGLDHFN
FLAVLGKGNF GKVMLAEAKS SKKLYAIKVL KKEFIIENDE VESTKSEKRV FLIANKERHP
FLLNLHACFQ TETRVYFVME YISGGDLMLH IQRGQFGLKR AQFYAAEVCL ALKYFHENGV
IYRDLKLDNI LLTLDGHIKI ADYGLCKEDM WYGSTTSTFC GTPEFMAPEI LLDKKYGRAV
DWWAFGVLIY QMLLQQSPFR GEDEDEIYDA ILADEPLYPI HMPRDSVSIL QKLLTREPEM
RLGSGPGDAQ EVMSHAFFKG INWDDIYHKR VPTPFKPTIK NEKDTSNFDQ EFTSVTPVLT
PVQSVLSPAH QEEFRGFSYS ADFI
//
