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Database: UniProt
Entry: A0A1D2NL39_ORCCI
LinkDB: A0A1D2NL39_ORCCI
Original site: A0A1D2NL39_ORCCI 
ID   A0A1D2NL39_ORCCI        Unreviewed;       789 AA.
AC   A0A1D2NL39;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428, ECO:0000256|PIRNR:PIRNR000559};
DE            EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428, ECO:0000256|PIRNR:PIRNR000559};
GN   ORFNames=Ocin01_00658 {ECO:0000313|EMBL:ODN05961.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN05961.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODN05961.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODN05961.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
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=2.7.11.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000962};
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=2.7.11.12; Evidence={ECO:0000256|ARBA:ARBA00000555,
CC         ECO:0000256|PIRNR:PIRNR000559};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cGMP subfamily. {ECO:0000256|ARBA:ARBA00006352,
CC       ECO:0000256|PIRNR:PIRNR000559}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN05961.1}.
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DR   EMBL; LJIJ01000012; ODN05961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2NL39; -.
DR   STRING; 48709.A0A1D2NL39; -.
DR   OMA; ESCLADC; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000094527; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd05572; STKc_cGK; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR002374; cGMP_dep_kinase.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR035014; STKc_cGK.
DR   PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR   PANTHER; PTHR24353:SF147; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000559; cGMP-dep_kinase; 3.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000559};
KW   cGMP {ECO:0000256|ARBA:ARBA00022535, ECO:0000256|PIRNR:PIRNR000559};
KW   cGMP-binding {ECO:0000256|ARBA:ARBA00022992,
KW   ECO:0000256|PIRNR:PIRNR000559}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000559};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000559};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000559}.
FT   DOMAIN          121..236
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          239..381
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          457..738
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          739..789
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..58
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        581
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT   BINDING         463..471
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT   BINDING         487
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
SQ   SEQUENCE   789 AA;  88919 MW;  1B457F1DC2919BE8 CRC64;
     MSDISDSSPE ERPPGNGENI FSELNRLREA LIEKEKEINR LQREVHKLKS VIEKSELTRI
     PSYKEGSHQK KCGVSGECGI VPDSQTKDGA SDSAKPTPPD RHNKDFRTRQ LIRAALGDND
     FLQNLDTDQV RDIVDFMYPQ KFNPGEYVIR EGDQGCHLYV TAEGQLQVSQ DSRNLGILKP
     GVAFGELALL YNCKRTASVR AITECKTWVL ERRAFQMVMV KAGMQRIKDR MTFLKSVPLL
     KGLDTASLAR IADCLEVELY PPGAFIIREG MCGDTFFIIS QGRVRVTVSE LAVRGADIVE
     GDEPTEEPKE PSSSSSDQIA PNGAKMLALR ELSHGDYFGE HALLREERRS ANVIAITNVE
     VLTLDRESFM QLIGDLSEFN RLKKPLHFSS CSQLPLQASS SSHMTGMNQI LDDDDGEGAA
     SSTEKLSKSL PNPSFEMFHY ERKEDEFDHS HLKLDDLEFV ATLGVGGFGR VDLVKVSFDP
     TKVFALKCLP KLHIISTQQQ DHVYAEKNIM LSCNSPFIAR LYRTFKDAKY VYMLMEACLG
     GEVWSVLRDK GSFDDAISRF IAGCVLQALE YLHEREIVYR DLKPENLMFA NNGYIKLVDF
     GFSKVVKAGQ RTWTFCGTPE YCSPEIILNR GHDKLTDLWS CGILLFELLT GYLRYDYITT
     LLPYSPPYGP HSENALGNDS SSDPLATYNC ILKGIDSVKF PKTCSKAAVS LIRRLCRQTP
     GERLGARNLR DIISHRWFQG FDWDGLRSRK LKPPIIPNLR GPLDTSNFDK FEIEIEDTPD
     DLSGWDEEF
//
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