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Database: UniProt
Entry: J9IQB6_9SPIT
LinkDB: J9IQB6_9SPIT
Original site: J9IQB6_9SPIT 
ID   J9IQB6_9SPIT            Unreviewed;       389 AA.
AC   J9IQB6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=cAMP-dependent protein kinase, regulatory subunit 1-2 {ECO:0000313|EMBL:EJY74330.1};
GN   ORFNames=OXYTRI_04414 {ECO:0000313|EMBL:EJY74330.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY74330.1};
RN   [1] {ECO:0000313|EMBL:EJY74330.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY74330.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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:EJY74330.1}.
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DR   EMBL; AMCR01013339; EJY74330.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9IQB6; -.
DR   EnsemblProtists; EJY74330; EJY74330; OXYTRI_04414.
DR   OrthoDB; 179139at2759; -.
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; cd22961; DD_TEX55-like; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
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   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
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}.
FT   DOMAIN          150..264
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          267..388
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          64..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214
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         223
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         338
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         347
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   389 AA;  44867 MW;  D231E86E7193CDB1 CRC64;
     MEQKQFEVKE ILEKLVAHLL TKKPEDPLPY MIQFLEDMKG VGTAPITAEE REELERLRRE
     QSKLKLKLKS KTHEDKDQTD DSEDSEDEDT VQDMNFNPQK AKHLSQNMRI SVSAEVFGKY
     HKKESFVPTI IHKSDQIKDK IRNRLKQSFM FSALDENELE VVIDAMDEQR ATAGESIIIE
     GEKGDQLFVV EEGVLDCFKQ FFLKNYEPGD AFGELALLYN APRAATIKAK TDCFLWVLDR
     NTFNYIVKDA AARKREIYED FLKSVKLLQN MDHYERSKLA DAIKEEKYEA NEFIIKEGEL
     GNVFYIISEG EAIATKTLEA GQPPKQVMSY KPGDYFGELA LLRNEPRAAN VIATTKVKVV
     LLERNSFKRL LGPLDNILKR NMDAYQNYV
//
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