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Database: UniProt
Entry: K1X9Q1_MARBU
LinkDB: K1X9Q1_MARBU
Original site: K1X9Q1_MARBU 
ID   K1X9Q1_MARBU            Unreviewed;      1173 AA.
AC   K1X9Q1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE            EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN   ORFNames=MBM_00835 {ECO:0000313|EMBL:EKD21722.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD21722.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD21722.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21722.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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; JH921428; EKD21722.1; -; Genomic_DNA.
DR   RefSeq; XP_007288724.1; XM_007288662.1.
DR   AlphaFoldDB; K1X9Q1; -.
DR   STRING; 1072389.K1X9Q1; -.
DR   GeneID; 18756770; -.
DR   KEGG; mbe:MBM_00835; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   HOGENOM; CLU_000288_54_0_1; -.
DR   InParanoid; K1X9Q1; -.
DR   OMA; MGANWCC; -.
DR   OrthoDB; 21591at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; 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};
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKD21722.1};
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:UP000006753};
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          165..242
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          480..528
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          548..598
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          845..1104
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1105..1173
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          72..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          15..65
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          219..246
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        615..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         874
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1173 AA;  130177 MW;  4B3C184496BC5413 CRC64;
     MNNDDDALSS VFKKIEREKA LITAANQMRQ QTQNEQVRSR LDTQMREGRR NIQYLEERME
     ELQMRRMGQG VEGMNLGGPA GGQGRPLSAG FRSDREGPPA LPPKDARGGY VEQSSDRGDY
     GGKQEYSQAG GHGDMMPPRH PYAPPAPGTG IPKSRPNFTK LDLIKYDTPY LGPRIQLMLS
     QLEFKLNVEK QYLKGIEKMV QLYQMEGDRK SKADAAGRRV ESTQKIQLLK QALKRYEDLH
     IDMESTADAP DDDSINTPNM RKPLTGQLSI RIQAVKDVDH AVTGRFTRGP ETFVAIKVED
     NVVARTKISR IDRWDAEYHN VNVDKANEIE LTVYDKPGDH PLPIGLLWVR ISDIVEEMRK
     KRIEAEISSS GWVSADRMAS GAAPGAPPPQ SNMNPSTPQF GQTPGTAGAG LGLTPSGGLQ
     GAGVIPPQPI DAWFALEPSG AVHLTISFTK QTKDRRPFDV GLNRKGAIRQ RKEEVHEMYG
     HKFILQQFYN IMRCALCGEF LKYSAGMQCE DCKYTCHTKC YTSVVTKCIS KSNAETDPDE
     EKINHRIPHR FEKFANMSAN WCCHCGYILP FGKKNCRKCT ECSLTCHAGC VHLVPDFCGM
     SMSVANVILD GIRNQKRRQT AQTPMTGRTL RQGSNKPVAG VEPTTPSDPR NSYGQQDSSH
     HPRTQSYGGQ SSSSSIEATE AAKAMYAQGP TSPVAQRPPG PDRTSSSSAA AAAIAAMAGP
     KSPTQQRDPY QRSSADYAGR QSGSSSQGYA NRLDSHPEDG GYGSTPKPQA AHPSYNPAAY
     AGYAAPQASQ QQMQSLQSPT ATMYSHQAQA PAPEPVPPAT AVIPRKSAPP ASESGTGRRI
     GLDHFNFLAV LGKGNFGKVM LAETKASKQL YAIKVLKKEF IIENDEVEST RSEKRVFLIA
     NKERHPFLLT LHACFQTETR VYFVMEYISG GDLMLHIQRG QFGTKRAQFY AAEVCLALKY
     FHENGVIYRD LKLDNIMLTL DGHIKIADYG LCKEDMWYGS TTSTFCGTPE FMAPEILLDK
     KYGRAVDWWA FGVLIYQMLL QQSPFRGEDE DEIYDAILAD EPLYPIHMPR DSVSILQKLL
     TREPDQRLGS GPTDAQEIMS QPFFRNINWD DVYHKRIQPP FQPQITSATD TSNFDSEFTS
     VTPVLTPVQS VGVVLSQAMQ EEFRGFSYSA DFI
//
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