ID A0A067BTA8_SAPPC Unreviewed; 1038 AA.
AC A0A067BTA8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KDO17882.1};
DE Flags: Fragment;
GN ORFNames=SPRG_22374 {ECO:0000313|EMBL:KDO17882.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO17882.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO17882.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO17882.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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DR EMBL; KK583544; KDO17882.1; -; Genomic_DNA.
DR RefSeq; XP_012211409.1; XM_012356019.1.
DR AlphaFoldDB; A0A067BTA8; -.
DR STRING; 695850.A0A067BTA8; -.
DR EnsemblProtists; KDO17882; KDO17882; SPRG_22374.
DR GeneID; 24142757; -.
DR KEGG; spar:SPRG_22374; -.
DR VEuPathDB; FungiDB:SPRG_22374; -.
DR OrthoDB; 4263002at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 6.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00248; ANK; 13.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 9.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Kinase {ECO:0000313|EMBL:KDO17882.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KDO17882.1};
KW Transferase {ECO:0000313|EMBL:KDO17882.1}.
FT REPEAT 1..33
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 34..66
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 67..99
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 195..227
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 273..295
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 310..342
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 343..375
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 376..408
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 533..566
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 601..854
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 861..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KDO17882.1"
SQ SEQUENCE 1038 AA; 111317 MW; A22E880BA43521CF CRC64;
NGQMPLHYAA SGGRLDVARL LLEKGANVDA CDKSGWMPLH SAAYGGHVDV ARLLLEKGAT
LDACTTDGST PLYMAAQANK PEMVQLLLEK GAKIDAKNKD GKTPLEVAEA RGSNAPVATL
LRDYLRMQGE QLFDALRNKC IDDAMRILRN NSYHVNLRDS SKTPLLHSVV ATQDMSLIQI
LLQKRNLQID AKDSTDRTAL AVAITDDNAE VVQALYQAGA SIHLVDIPPC DKRLCASTPV
LVAALRQAAS INDGSTVAQL LRLGVSCSLA NEKGETAWHM AAAKGHMSIL TMLLQQKTKD
ENGIDVTNHN GESPLFLAST SGHTDVVKCL LRGNASPHIV SHDGSTLLHA AAIGGNMIVV
HQIVQSGVNV DACDAMGQTP LHIASEKAND SVVKYLLDVD ANVFAKDKTG KTPLMLATHP
LVINTLLQAE KSTKQKAPQL SQTMLDHIVT RICDTGVLRD LIRTSVCGSE ELLGQLVQRV
CDRLDVGRES LGASVDRPVD TRGANERVRA DNDIDASQTL LADDSDSNAA NEAGDSPLHL
AVQANDHKTL MSLLRTPSIN VDVRNAVGMT PVILAVQRGH RRLATMLQTA AHPSIADVPT
TDIKMDQSSP LNGTMYKGTY KGRVVAIKTP SDESSAQAIL HEMETMQQCN SPYVQQLLAV
SDVTTSSPKL VLEYMDAGDL RSYLDAKRLG EPTKINVSPL QVAWVLANAL ADLHHNGLLH
HDLESYNVLL SSTNYIKVAN LGCGLESDAT TGKSTPYWTA PEVLASTSNY SCAADIYSFG
VILTELDTLQ LPFHDAKGLG YWGIIDGVRL GNLRPTVSTN CPPWLRDLAD ACLSFDPTQR
PSALMLVQSL QKLLDRSEEE LAAPAGREPE MTFAAPSDGS SPLEVLSNES PPPPTSEESS
DDFDDYVAPA IESPTPPKAP AISTNTPTPS SSPSSMPVST HAVCQLCRAS NSLLESHCKA
CAAPLASITS KLKALLKRLA VAKKNGFEID DGLFCDCCDA HQPMDATVCG VCEEELPDDH
EKLSILILRI EQATKSTA
//
