ID L8WM38_THACA Unreviewed; 818 AA.
AC L8WM38;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=cAMP-dependent protein kinase inhibitor {ECO:0000313|EMBL:ELU39020.1};
GN ORFNames=AG1IA_06941 {ECO:0000313|EMBL:ELU39020.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU39020.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU39020.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(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:ELU39020.1}.
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DR EMBL; AFRT01001963; ELU39020.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WM38; -.
DR SMR; L8WM38; -.
DR STRING; 983506.L8WM38; -.
DR HOGENOM; CLU_018310_0_1_1; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12098; DD_R_ScPKA-like; 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; 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 II REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 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};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022566};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 279..411
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 414..531
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 104..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 90249 MW; 4B961184F617EBA9 CRC64;
MMDYASFSIQ YNSPPHILHS LPPTAARMAA PYSSTYAELV ADLTRDVQRA QPRDVLQYCA
NWFNSRLQEQ RTRIRDAFQA QAFGRPSAAA GLTDELFVDR AVPARGSVPN GSMSISSSVR
SSPMPSHSQP HPQAHPQPPQ PHTQTTPQPS IHQHAPQPNP FALSSGSAFS LVPGARLADP
FAPSASPRPR PGQRAVTPSR HNTIHEEEEP PTPSSPAAPA PTGSPAFLAP PPSALGRRVS
VSAESITPSA SGSLPPMPSY PKSTEQLQRI KASIANAFLF RNLDTEQEKA VLGAMQERHV
SAGERVIEQG ADGDYFYVVE SGSLDCFVKR AGDNEGSVGD EVHPTYGRKV LTYTTGGTFG
ELALMYNAPR AATIVAIEPS TLWALDRMSF RSIILSVANR KRKMYERFLA TVPLLETLDA
SERSRIADVL EPRTYNEGDS VVEEGDTGNE FFIIESGEAT AFKRVKGEDG ELRDDVVMKY
GPGDFFGELA LLHRAPRAAT VRASVTGDNN GEPNKLKVAV LDAQAFTRLL GNLKSLLDRH
ATQNYGASYR LQPIKAQYPP YSIPRFSHLP MTSTSFPQRA AFQLYPSVDP QGPQHQTETR
LGASTRWEDK STSRRWRSVN RSVRLVFLRF EQKSLDASNR IKSTSALETT SEASPTARTC
EGISYPIDKN VDDRQRWCNT YKPKREFLRT EKFIDSVQGK IDVNLYSAVG MSRVVQKLRY
TLADLIGRFM SASYNRMMSA RFPSLTCLGN WASCSGVYES FSSLRLMTIR SNDSPLADNT
YALVASCPDR IENVNDGLHH VAFPERFHGL DTMANRFP
//
