ID F0WVY7_9STRA Unreviewed; 976 AA.
AC F0WVY7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=AlNc14C306G10448 {ECO:0000313|EMBL:CCA25589.1};
GN ORFNames=ALNC14_117330 {ECO:0000313|EMBL:CCA25589.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA25589.1};
RN [1] {ECO:0000313|EMBL:CCA25589.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA25589.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FR824351; CCA25589.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WVY7; -.
DR EnsemblProtists; CCA25589; CCA25589; ALNC14_117330.
DR HOGENOM; CLU_304495_0_0_1; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd03135; GATase1_DJ-1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR019339; CIR_N_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF30; MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE; 1.
DR Pfam; PF10197; Cir_N; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01083; Cir_N; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCA25589.1};
KW Transferase {ECO:0000313|EMBL:CCA25589.1}.
FT DOMAIN 596..877
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 325..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 110944 MW; 97FF9079574DBCB9 CRC64;
MDCSMITPNE RKLDSINCSR TRGFVGIAST RVTSMFLYGM GMGFWGVLKK GENRGWHPSN
KANQKRIWIA EQKEKAKEEK EKEAASELRK NAELYRFQKI AAAKGDERSV TQLASQSVEF
MYAPPPGLQK IDKSVENDMR EDDAVREFRR RMEKKTKNHK NEEAKKTQRN LERYVGRRPD
ESLTIDEQVE RFPFLKDAPV QGDYTGNVKV NFKPMGVQLR NVRCLRCGEW GHLSGDRECK
LRNFNPHDAA RQALEDPFSY MNKMTQVSKQ ELVLRRAAIP FEMHGENIAK DYELLSSEDD
SDCDSESAFL EKLTTKEKKL LLKKLKKASK KKKREKSRDE DRPARKHSKR DTKGMATRVI
NLAQVREGSP DLHPKLAMIA VSDGTDELET MILYDVLKRA NIRVILASCS TKDGRIVHTS
HGMKLITTSP VEDSVDYNID LIALPGGNAL DGLRECEVLI KLLKKQLEKG KWIAAFSNAP
AGVLMPHLLL DGKATCHPSK ARDMTGYFVD QDFAISKNCV TSQGQGTSMR CALKLVELLC
GHETAKSVAD ELLFKLHPRV SCQNVCQKRR TKRTIHDRLR QLMGAEITEE EFWNRFTFGK
MLGTGSTCKV YEAFDTVTNE TVAVKVFDKV EMIETRSSMA ASEDKIVKER AVDRACRRLL
KIISELEIVK TLHHPNIIQF RGAYETSHRI CIVYERTQGS DLLEYLLAHG RMQEPQAAYV
ARQLLSAVQY CHDRRLYHRD LKLENVLISP ELKVKLIDFG LSEYVPEGKE LHSVCGTPLY
CSPEILFMHS SNEHSREGFE GGPADVWSVG IFLFAILTGC TPFDDSTLMR LREDVFQNSI
CFPPYLSYEV KGMLKAILNP DPTLRPTVQD LMEYGWIKAK GLHETQLVVS HTTHTKCKLS
RSKTVSSSPL NKAPAFHRSL FRPSSDGTEN TARSSLSYDE ISQELAKWNL GNLDPHIDLS
DTRRPLHTAF SFTKKT
//
