ID W9YKX5_9EURO Unreviewed; 916 AA.
AC W9YKX5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=AGC/AKT protein kinase {ECO:0000313|EMBL:EXJ82909.1};
GN ORFNames=A1O3_06725 {ECO:0000313|EMBL:EXJ82909.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ82909.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ82909.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ82909.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ82909.1}.
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DR EMBL; AMGY01000005; EXJ82909.1; -; Genomic_DNA.
DR RefSeq; XP_007735032.1; XM_007736842.1.
DR AlphaFoldDB; W9YKX5; -.
DR STRING; 1182542.W9YKX5; -.
DR GeneID; 19170832; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_0_1; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EXJ82909.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 526..787
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 788..872
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 916 AA; 101932 MW; 9564C338044B4647 CRC64;
MYRPLGLGSS HPSNQSLFAG SGHPFRFLAN SLNSSARHDN REEFPDQIGS NSPTPSGVET
PRPDLHDKRL PGINHSYFGQ VGRDPSQDTP SRSSPAATAS ETNDQSAYLA GQSEKEKEDR
RASFASVGSM VMVERDQGSI PTPPPDERHP ERMKPVEETD ASRFLPTPIS SAASVVHRDG
EAAENGASMI EGGLATITQA LRNFVLPKTA FVMKERRHQS LPVSSVTKSN VSAAHISNPT
SSTHSSRPQT PSSSSPNSAK PQSSQTLQES IKLTSDVAAV PRDKRTPPQT PRALSQEDRR
VEARSPLSST STSTSISTPA ADANAETEKQ DEDLVKNDIP NSTPRGKLSI KIAEGRNLKP
SFDPYVICQF EWNEYVSKGP KHDTMDIDDD DRKGPVAALQ SIPIRRTDSD MGKPMAIPMR
SRQSSSNGAA EDRPLTKVTD PQWDHEATFD VVSNQSELDV TVYDRQTEEF LGHVRLCLIL
TEQHPILEGF FRLEPRSAED QDVTGEIHIR MQFSKVEKKH FGPNDFQILK LIGKGTFGQV
YQVRKKDTQR IYAMKVLSKK VIIQKKEIQH TIGERNILVR TATTESPFIV GLKFSFQTPT
DLYLVTDFMS GGELFWHLQK EGRFKEDRAK FYIAELILAL KHLHDHNIVY RDLKPENILL
DANGHIALCD FGLSKANLTQ DDTTNTFCGT TEYLAPEVLL DEQGYTKMVD FWSLGVLVFE
MCCGWSPFYA EDTQQMYKNI AFGKVRFPRD ALSTEGRNFV KGLLNRNPKH RLGARGDAEE
LMRHAFFADV DWDALGKKNL VPPFKPKLSS VADTSNFDPE FTNALNTSSS LNARAAALAA
GAAPTSTPLS PTMQNAFRGF TFVDESAMEE RFGGSHEIED DKIDEKDEQS LSRSRTREHR
MSGVQRTGEE GFFFEE
//
