ID A0A0J6YM45_COCIT Unreviewed; 453 AA.
AC A0A0J6YM45;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=cAMP-dependent protein kinase regulatory subunit {ECO:0000313|EMBL:KMP08214.1};
GN ORFNames=CIRG_07895 {ECO:0000313|EMBL:KMP08214.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP08214.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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DR EMBL; DS028097; KMP08214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YM45; -.
DR STRING; 404692.A0A0J6YM45; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
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 II REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KMP08214.1};
KW Transferase {ECO:0000313|EMBL:KMP08214.1}.
FT DOMAIN 197..325
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 328..437
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 127..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 49702 MW; C870EB22D79F2A98 CRC64;
MPSLRLESRS RTLCIPSRLL PKLLRLKNST RLHCRQIPYT VMSESNAFPG SHAGHGERHA
GGGAAPFNRI VEEDENVTSP TTSTFHRTDV SRQRAHIHHV LSPFQSGDGV GTFGEFGAFG
PNPFGGRGEQ EHGTFRPAAG PSDSGFPNHY ALGRRTSVSA ESLNPTSSDS DSWTPPYHPK
PPEQLDRLKT AVAGNFLFSH LEEDQFKTVL NALVEKPVPA KDIKVITQGD AGDYFYIVEQ
GHFDVFIHPS GSAQPGHNGM GSKVNEIGPG GSFGELALMY NAPRAATVVS TEPSTVWALD
RVTFRRILMD SAFKRRRMYE AFLEEVPLLS SLKPYERSKI ADALDTIKHP AGHTIIEEGD
PGDAFYLLES GEAAAYKRGI DGAVKHYRRG DYFGELALLD DKPRQASVIA KTDVKVAQLG
RDGFKRLLGP VEDIMRRTEY GVPEGQPKLE ASE
//
