KCC1A_EMENI
ID KCC1A_EMENI Reviewed; 414 AA.
AC Q00771; C8VNX3; Q5BAL8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase cmkA {ECO:0000305};
DE Short=CMPK;
DE EC=2.7.11.17 {ECO:0000269|PubMed:2835766, ECO:0000269|PubMed:8898358};
DE AltName: Full=Multifunctional calcium/calmodulin-dependent protein kinase {ECO:0000303|PubMed:2835766, ECO:0000303|PubMed:8898358};
DE Short=ACMPK {ECO:0000303|PubMed:2835766};
DE Short=CaMK {ECO:0000303|PubMed:8898358};
GN Name=cmkA; ORFNames=AN2412;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1563634; DOI=10.1016/0378-1119(92)90671-b;
RA Kornstein L.B., Gaiso M.L., Hammell R.L., Bartelt D.C.;
RT "Cloning and sequence determination of a cDNA encoding Aspergillus nidulans
RT calmodulin-dependent multifunctional protein kinase.";
RL Gene 113:75-82(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R153;
RA Subbaramaiah K., Greene V., Bartelt D.C.;
RT "Structure of the cmkA gene encoding a CaMKII homolog in Emericella
RT (Aspergillus) nidulans.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND AUTOPHOSPHORYLATION.
RC STRAIN=R153 {ECO:0000303|PubMed:1563634};
RX PubMed=2835766; DOI=10.1073/pnas.85.10.3279;
RA Bartelt D.C., Fidel S., Farber L.H., Wolff D.J., Hammell R.L.;
RT "Calmodulin-dependent multifunctional protein kinase in Aspergillus
RT nidulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3279-3283(1988).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LYS-50.
RX PubMed=8898358; DOI=10.1091/mbc.7.10.1511;
RA Dayton J.S., Means A.R.;
RT "Ca(2+)/calmodulin-dependent kinase is essential for both growth and
RT nuclear division in Aspergillus nidulans.";
RL Mol. Biol. Cell 7:1511-1519(1996).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase (PubMed:2835766).
CC Required in nuclear division cycle for progression from G2 to mitosis.
CC Required for hyphal growth (PubMed:8898358).
CC {ECO:0000269|PubMed:2835766, ECO:0000269|PubMed:8898358}.
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=2.7.11.17;
CC Evidence={ECO:0000269|PubMed:2835766, ECO:0000269|PubMed:8898358};
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=2.7.11.17; Evidence={ECO:0000269|PubMed:2835766,
CC ECO:0000269|PubMed:8898358};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin (PubMed:8898358).
CC Binding of calmodulin may relieve intrasteric autoinhibition
CC (Probable). {ECO:0000269|PubMed:8898358, ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2835766}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000250|UniProtKB:Q63450}.
CC -!- PTM: Autophosphorylated in a calcium/calmodulin-dependent manner.
CC {ECO:0000269|PubMed:2835766}.
CC -!- DISRUPTION PHENOTYPE: Spores arrest with a single nucleus and fail to
CC extend a germ tube. {ECO:0000269|PubMed:8898358}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA64523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M74120; AAB97502.1; -; mRNA.
DR EMBL; AF054580; AAD22581.1; -; Genomic_DNA.
DR EMBL; AACD01000039; EAA64523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF86796.1; -; Genomic_DNA.
DR PIR; JN0323; JN0323.
DR RefSeq; XP_660016.1; XM_654924.1.
DR AlphaFoldDB; Q00771; -.
DR SMR; Q00771; -.
DR STRING; 162425.CADANIAP00009119; -.
DR EnsemblFungi; CBF86796; CBF86796; ANIA_02412.
DR EnsemblFungi; EAA64523; EAA64523; AN2412.2.
DR GeneID; 2874845; -.
DR KEGG; ani:AN2412.2; -.
DR VEuPathDB; FungiDB:AN2412; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q00771; -.
DR OMA; ADCPEGK; -.
DR OrthoDB; 330091at2759; -.
DR BRENDA; 2.7.11.17; 517.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IDA:AspGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:AspGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:AspGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:AspGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Cell cycle; Cell division; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..414
FT /note="Calcium/calmodulin-dependent protein kinase cmkA"
FT /id="PRO_0000086087"
FT DOMAIN 23..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 278..314
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT REGION 293..315
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT REGION 320..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 50
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:8898358"
FT CONFLICT 408
FT /note="A -> R (in Ref. 1; AAB97502 and 2; AAD22581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 46804 MW; 1E8D58A1C0B2E85C CRC64;
MSFANMFNKL SGQPESYEKK SLYRFGRTLG AGTYGIVREA DCSSGKVAVK IILKRNVRGN
ERMVYDELDL LQKLNHPHIV HFVDWFESKD KFYIVTQLAT GGELFDRICE YGKFTEKDAS
QTIRQVLDAV NYLHQRNIVH RDLKPENLLY LTRDLDSQLV LADFGIAKML DNPAEVLTSM
AGSFGYAAPE VMLKQGHGKA VDIWSLGVIT YTLLCGYSPF RSENLTDLIE ECRSGRVVFH
ERYWKDVSKD AKDFILSLLQ VDPAQRPTSE EALKHPWLKG ESASDRDLLP EIRAYIARSR
LKRGIEIIKL ANRIEALKMQ EEDEEDIPSA VDVQASEASD KSGLSPFPAL STENSNTHPA
STGNGESGGT KKRSLSKIAR GAIFREVVLA KVREMKENEE REKVEREARE RAHS
