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KAPR_NEUCR
ID   KAPR_NEUCR              Reviewed;         385 AA.
AC   Q01386; Q7RVE4; V5ILJ8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE            Short=PKA regulatory subunit;
DE   AltName: Full=Microcycle blastoconidiation protein;
GN   Name=mcb; ORFNames=123A4.120, NCU01166;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8918454; DOI=10.1002/j.1460-2075.1996.tb00963.x;
RA   Bruno K.S., Aramayo R., Minke P.F., Metzenberg R.L., Plamann M.;
RT   "Loss of growth polarity and mislocalization of septa in a Neurospora
RT   mutant altered in the regulatory subunit of cAMP-dependent protein
RT   kinase.";
RL   EMBO J. 15:5772-5782(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
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DR   EMBL; L78009; AAB00121.1; -; Genomic_DNA.
DR   EMBL; AL670009; CAD21365.1; -; Genomic_DNA.
DR   EMBL; CM002240; ESA42511.1; -; Genomic_DNA.
DR   EMBL; CM002240; ESA42512.1; -; Genomic_DNA.
DR   RefSeq; XP_011394477.1; XM_011396175.1.
DR   RefSeq; XP_011394478.1; XM_011396176.1.
DR   AlphaFoldDB; Q01386; -.
DR   SMR; Q01386; -.
DR   STRING; 5141.EFNCRP00000004245; -.
DR   EnsemblFungi; ESA42511; ESA42511; NCU01166.
DR   EnsemblFungi; ESA42512; ESA42512; NCU01166.
DR   GeneID; 3877728; -.
DR   KEGG; ncr:NCU01166; -.
DR   VEuPathDB; FungiDB:NCU01166; -.
DR   HOGENOM; CLU_018310_0_0_1; -.
DR   InParanoid; Q01386; -.
DR   OMA; YDNWSPP; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
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   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   SMART; SM00100; cNMP; 2.
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..385
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205412"
FT   REGION          1..128
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129..260
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         207
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         261..378
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         328
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  42156 MW;  4B3F52B7486735D4 CRC64;
     MSSTGFTSPF GNANPFGSSG RSESGPMHRL VEEDENDTIT SPTTPHFGVK NNAAPAFWNG
     FGGDAPSDMP VRRQPDDFPA HYNLGRRTSV SAESLKPVTD NSDNWSPPVH PKTAEQLERL
     KKAISGNFLF NHLEDDQSAQ VLGALVEKPV PAKGIKVITQ GDAGDYFYVV EKGRFEVYVN
     STGALQPGPD GMGQKVGEIA EGGSFGELAL MYNAPRAATV VSAEPQCTLW ALDRVTFRRI
     LMESTFSRRR MYESFLEEVP ILKTLTPYER SKIADALESQ KYPAGHEIIL EGDPGHSFFL
     LEAGEAAAFK RGNDSPVKNY KKGDFFGELA LLNDAPRAAS VISQTEVKVA RLGKNAFQRL
     LGPIESILRR TRYVEAEEVD PLQVS
 
 
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