KAPR_USTMA
ID KAPR_USTMA Reviewed; 525 AA.
AC P49605; A0A0D1BUG7; Q4P0B3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=PKAR; Synonyms=UAC1, UBC1; ORFNames=UMAG_06450;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=518;
RX PubMed=7995519; DOI=10.1101/gad.8.23.2805;
RA Gold S., Duncan G., Barrett K., Kronstad J.W.;
RT "cAMP regulates morphogenesis in the fungal pathogen Ustilago maydis.";
RL Genes Dev. 8:2805-2816(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic (C)
CC subunits. In the presence of cAMP it dissociates into 2 active
CC monomeric C subunits and an R dimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57470.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L33917; AAA57470.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CM003162; KIS65747.1; -; Genomic_DNA.
DR PIR; B55481; B55481.
DR RefSeq; XP_011392721.1; XM_011394419.1.
DR AlphaFoldDB; P49605; -.
DR SMR; P49605; -.
DR STRING; 5270.UM06450P0; -.
DR EnsemblFungi; KIS65747; KIS65747; UMAG_06450.
DR GeneID; 23566035; -.
DR KEGG; uma:UMAG_06450; -.
DR VEuPathDB; FungiDB:UMAG_06450; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; P49605; -.
DR OMA; REAVSHN; -.
DR OrthoDB; 1047290at2759; -.
DR PHI-base; PHI:466; -.
DR PHI-base; PHI:6078; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:EnsemblFungi.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IEA:EnsemblFungi.
DR GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IEA:EnsemblFungi.
DR GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
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; cAMP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..525
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205416"
FT REGION 28..213
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT REGION 114..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214..345
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 295
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 348..472
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT BINDING 417
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 44
FT /note="A -> E (in Ref. 1; AAA57470)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..180
FT /note="SA -> Q (in Ref. 1; AAA57470)"
FT /evidence="ECO:0000305"
FT CONFLICT 424..426
FT /note="APR -> RC (in Ref. 1; AAA57470)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="S -> T (in Ref. 1; AAA57470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 55258 MW; BFCE31530D508631 CRC64;
MSLPSSYTAL LNDLNRDVAR ARPADALQFC ANWFNSKLEE QRRAHLASNT NFATTNASTP
FSHNSVGPSD IVDFGGAAPG LASPTQRASL FHSDPFAPGA GGGALPVASL AVPMDASQSP
DSTPAPATPA APAAPAAPAA PFSSLGGSGS TSISNAAFIP PTFNLGRRTS VSAESMAPSA
ANAESDGSPL PKTVIPKSEE QMQRIRGSIG NNLLFRNLEQ DQYRDVLLAM KEVKVDANVT
VIEQGAQGDY FYVVEFGTLD VYVRSPDAVS EGAPSASALL GDKKVSYGPG SSFGELALLY
AQPRAATVLS TSACTLWALD RITFRSILME TNSRRRALYE KFLMDVPLFE RLSAAERAKI
SDSLELREYS RGEAVISQGE RGSEFFIIVE GDAEVRKTKQ GGEEVVGKLS RGDYFGELAL
LNNAPRAATV AAAGATDDAR LRVVTMSERA FTRLLGPLAG ILERHAKETY GDEYSAVHAN
ANADAATSVN SAALARSGAD TSFPHPMDSS AKPGEGAWSA PNPFA
