KAPC2_CAEBR
ID KAPC2_CAEBR Reviewed; 385 AA.
AC A8XJQ6;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=cAMP-dependent protein kinase, catalytic subunit-like {ECO:0000303|PubMed:16806821};
DE EC=2.7.11.11 {ECO:0000250|UniProtKB:P21137};
GN ORFNames=CBG14305 {ECO:0000312|WormBase:CBG14305};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549};
RN [1] {ECO:0000312|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [2] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=16806821; DOI=10.1016/j.cellsig.2006.05.002;
RA Bowen L.C., Bicknell A.V., Tabish M., Clegg R.A., Rees H.H., Fisher M.J.;
RT "Expression of multiple isoforms of the cAMP-dependent protein kinase (PK-
RT A) catalytic subunit in the nematode, Caenorhabditis elegans.";
RL Cell. Signal. 18:2230-2237(2006).
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=2.7.11.11;
CC Evidence={ECO:0000250|UniProtKB:P21137};
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=2.7.11.11; Evidence={ECO:0000250|UniProtKB:P21137};
CC -!- DEVELOPMENTAL STAGE: No obvious expression before embryo hatching but
CC is probably expressed at later stages (at protein level).
CC {ECO:0000269|PubMed:16806821}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; HE600983; CAP32882.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XJQ6; -.
DR SMR; A8XJQ6; -.
DR STRING; 6238.CBG14305; -.
DR WormBase; CBG14305; CBP09612; WBGene00034852; -.
DR eggNOG; KOG0616; Eukaryota.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; A8XJQ6; -.
DR OMA; QEDPPRY; -.
DR OrthoDB; 963519at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..385
FT /note="cAMP-dependent protein kinase, catalytic subunit-
FT like"
FT /id="PRO_0000432403"
FT DOMAIN 63..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 318..385
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 385 AA; 44076 MW; CADD2AE5CAABDC83 CRC64;
MSSSTSSVES VEDESCSNEC SASFTFDTNN NSRGDQQVDE LAEETHMKLS ITPTRESFSL
SQLERIVTIG KGTFGRVELA RDKISGAHYA LKVLNIRRVV DMRQTQHVHN EKRVLLQLKH
PFIVKMYASE KDSNNLYMIM EFVPGGEMFS YLRASRSFSN SMARFYASEI VCALEYIHSL
GIVYRDLKPE NLMLSKEGHI KMADFGFAKE LRDRTYTICG TPDYLAPESL ARTGHNKGVD
WWALGILIYE MMVGKPPFRG KTTAEIYDSI IEHKLKFPRS FNLAAKDLVK KLLEVDRTQR
IGCMKNGTQD VKDHKWFEKV NWDDTLHLRV EVKKLIGIFL IPIFQPPIVP TLYHPGDTGN
FDDYEEDTTG GPLCSQRERD LFAEW
