GenomeNet

Database: UniProt
Entry: T1JGV4_STRMM
LinkDB: T1JGV4_STRMM
Original site: T1JGV4_STRMM 
ID   T1JGV4_STRMM            Unreviewed;       375 AA.
AC   T1JGV4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR013079-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR013079-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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DR   EMBL; JH432212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1JGV4; -.
DR   STRING; 126957.T1JGV4; -.
DR   EnsemblMetazoa; SMAR013079-RA; SMAR013079-PA; SMAR013079.
DR   eggNOG; KOG1113; Eukaryota.
DR   HOGENOM; CLU_018310_1_0_1; -.
DR   OMA; GEQGDTF; -.
DR   OrthoDB; 55978at2759; -.
DR   PhylomeDB; T1JGV4; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12097; DD_RI_PKA; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF152; CAMP-DEPENDENT PROTEIN KINASE TYPE I REGULATORY SUBUNIT-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   3: Inferred from homology;
KW   cAMP {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRSR:PIRSR000548-1};
KW   cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW   1}; Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          131..246
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          249..370
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          57..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         196
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         205
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         320
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         329
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
SQ   SEQUENCE   375 AA;  41993 MW;  29041438941199F4 CRC64;
     MASWSEEEQS LRECEAYVQR HNIQQILKDC IVQLCVSRPE NPITFLREYF QKMEREALSR
     AKQQNAQSSA TPPGEDELSP PIPVQVATRR RGAVSAETYS EDDAATYVKK VVPKDYKTMG
     ALTKAISKNV LFTHLDDKEK SDIFDAMFPV VHNAGEVIIQ QGDEGDNFYV IDEGEVEVFV
     NGDMVVTIGE SGSFGELALI YGTPRAATVK AKTNIKLWAI DRDTYRRILM GSTIKKRKIY
     DEFLSKVSIL ESLDKWERLT IADALEQVVF DDGAVIVKQG ERGDDFFIIS EGNAVVLQQK
     SETDEPVEVG VLGPSDYFGE IALLLDRPRA ATVTARGFLK CVKLDRARFE RVLGPCADIL
     KRNIAQYNSY VSLSV
//
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