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Database: UniProt
Entry: E2A801_CAMFO
LinkDB: E2A801_CAMFO
Original site: E2A801_CAMFO 
ID   E2A801_CAMFO            Unreviewed;      1179 AA.
AC   E2A801;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=EAG_08733 {ECO:0000313|EMBL:EFN70438.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN70438.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; GL437468; EFN70438.1; -; Genomic_DNA.
DR   RefSeq; XP_011253194.1; XM_011254892.2.
DR   AlphaFoldDB; E2A801; -.
DR   STRING; 104421.E2A801; -.
DR   EnsemblMetazoa; XM_011254892.3; XP_011253194.1; LOC105249432.
DR   GeneID; 105249432; -.
DR   KEGG; cfo:105249432; -.
DR   InParanoid; E2A801; -.
DR   OMA; HYKNTNL; -.
DR   OrthoDB; 103262at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   PANTHER; PTHR22967:SF57; AUXILIN, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR22967; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EFN70438.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Transferase {ECO:0000313|EMBL:EFN70438.1}.
FT   DOMAIN          34..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          413..588
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          592..728
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          1113..1179
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          313..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1041
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..345
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..374
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1029
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1179 AA;  129412 MW;  FBD79A8E543FDE66 CRC64;
     MSDYLRSAFG YLNGGSGGGN EYVGQTLDIN NVRLRVTRLI AEGGWALVFA VEDITTGKEY
     ALKKLIAVDE DTNKTIIQEI ETLKKLSGHP NIIQFFYAQR LEREDRKGYE YLVVTELCPG
     GTIADILRNV SANTLTLAQV CKVAYQATQA VHYMHSQQPE PFVHRDIKLE NFLIGKDGLV
     KLCDFGSAST QQILPNPSWN AQKRATLEDQ MAKYTTPMYR APEMMDTWNN EPIGPPVDCW
     ALGCILYSLI TLRHPFPEGN KLAIVNGKYP PLPPNPRYAC LNDLVKGCLQ VSPIQRSTTA
     QLLERLAAIA ESNNFDPREP PQIEVTAVRP SPPPRPTPPP PPSSSSSSSS SSNMPPPRPS
     QPATMPPPRP APMQVSKIPA TQATTGLFNS LRGGAGSILR NLKDTSSKVM HTVQQSMART
     ELDASYMTSR MLVMPYPADG IESAYRANHV EDVRAFLQAR HPPPAKIQLY NLSRGRPNVT
     RLPGRHIDCS FAYATPESNA PMLFALYQIC QDIYQYLNAD FNHVVVLYCT DGYRASATVA
     CTLLIHCRAL TTAEEAIALF TTRRCQPPQL QPSELRSINY MSLLSSGRLP HTKPLVFRSV
     VIQPVPLFTR ARDGCRPYIE IYSNGALVFT TKKVIYEEMK LFGMMEGKVC LILGDAAVRG
     DVTIIIHHAR QQLGRVIGIK IASLHFHTGY VPITESALTF EKHDLDDAPE IGGKFRIVLN
     VMIGEENSKL SRVPAPWEAE TCINLVPDPL FGSTLEMEET LENFRTAPHP EEIQAPSNET
     DNNMKQHEAI PQQPEDLKEE EEANTNEEIN FQEADLLNLG MPDNTNSTSN TPASTAPNPG
     LDIFSSSSQN ENDLLGGFGM SAPHTETANS PLINNSASAD LLFGHDSSAT RNNSTANNNL
     NMNDLLFGQN QTMSSNVKQV NEMLFDPLGG SSANNLLGGF AAAKSPNAED NLPRNASVPN
     FAAQANKDPF ANLASSLGAG LTGSWNGTPR NSSTPQSASP APASTPIHSS PNTIHRSNDA
     NSANSGNTDA LGAKAKEKAS GDAFEDLLGS QGYKFSRKAE KDSPKTINQM RKVEAAKTMD
     PDRLKIAEWT EGKKGNLRAL LCTLHTVLWP EADRWQRCEM HQLVTSADVK KAYRKACLVV
     HPDKQTGTAN ENIAKLIFME LNNAWSTFDN DPSQQNLFS
//
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