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Database: UniProt
Entry: A0A024TS53_9STRA
LinkDB: A0A024TS53_9STRA
Original site: A0A024TS53_9STRA 
ID   A0A024TS53_9STRA        Unreviewed;      1241 AA.
AC   A0A024TS53;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ETV96965.1};
GN   ORFNames=H310_09818 {ECO:0000313|EMBL:ETV96965.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV96965.1};
RN   [1] {ECO:0000313|EMBL:ETV96965.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV96965.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI913974; ETV96965.1; -; Genomic_DNA.
DR   RefSeq; XP_008874211.1; XM_008875989.1.
DR   AlphaFoldDB; A0A024TS53; -.
DR   STRING; 157072.A0A024TS53; -.
DR   EnsemblFungi; H310_09818-t26_2; H310_09818-t26_2-p1; H310_09818.
DR   EnsemblProtists; ETV96965; ETV96965; H310_09818.
DR   GeneID; 20086868; -.
DR   VEuPathDB; FungiDB:H310_09818; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   OrthoDB; 4035061at2759; -.
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; 1.10.260.100; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 7.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Kinase {ECO:0000313|EMBL:ETV96965.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ETV96965.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ETV96965.1}.
FT   REPEAT          37..69
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          71..103
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          105..140
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          200..232
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          233..265
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          362..395
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          526..796
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   1241 AA;  135732 MW;  2F7CC521D73BDAB9 CRC64;
     MSKEVSLYIA ARLGQIQDVK MYLAQGANVN WTNLENNGWT PLHAASERGY VEIVKILVDN
     GANVNATDTF FGNTSLHEAS QHGRVDVVKI LLDNGANANA PNLYDGSTPL HSAASSCFEH
     AADAVEWLLD AGASLSTRNK SGMSARDVAA EKNRRAALAA LDRWTKGAAL FHAAKSGLVR
     EVLTCLAQGA NVNWRNKAEQ GWTALQIAWT CGHVDVVQAL LDAKADVNTT DEDGHTPVHI
     ASSNGKHAVV KPLVLCGAKN DPPSTLRDLP CHEVPGHVEP ALHAKANASA RMEDGIYAQV
     VAEAVMALDQ DAQVQHDHAD RFNAGMDCQA LVARSIDCFC AGQHDLAVQI ANEALATLGI
     AKSAWVWIGE NLRGRGQYEQ ALAAYVMGQQ VDPSDVDCIV GMEDVRDTIQ VAKVFNHNML
     QLLAKDRRMR EYLKDKAFVS RLNSIQADPT QYDPQDKRLA HVFEYLHDRG GIPPPHVPPS
     VAPLTDSFES NGTPIGAIPI KESLTELTEY LLCPGTPTVW RLSNTYLLIT DLVNESSHCV
     FKAEDPTRRH KQFVVKLTDQ EAEVTFVKRM NDRDDSKHVA NVVECVQVCT IPLAGPAKTC
     FALVMEQGEP LDTCHLRNLQ RRPLLALECV QDVAKALQFL HRDHAIIHGD VKLENVLYFD
     RAVGYKLIDF DQTVTIGSAM RLHCTHEYCP PEMARLILQR HNHVLMAASP TFDVWCLGVL
     MLKLFVDGGH LEEFDGVAAG DGILEIVAAP GFCFRKSLAK ASHLNSRQMT FLMTCLEPDV
     SKRANNVNDI VDIATFESPT STMPPTRSAS KESVCEMPSV WTITIVNGRR RLPRGDVLRG
     LECRIGVVNV AGATSCKFDQ DKSMTASCGS DVVALVLPFF RVLMVLLDVL DALEDHGADV
     ASWKALAWPP IDSIHAAVDA LESIHTTTTV LPIELELRAL DDRLTQMTCL AMEEVEALLA
     SVTRALKQFA TSSDTLERVV AVLTCPGVAP TCVGGLVGHV HPATGVVAWK CCVHGGGFVR
     GGDMASGAVA NPGDLPLLWS LEPMAQLGSR IKDPPSLRRD RFRLVFQCEW RRESACHTQQ
     HDARNDAMLQ LLGDSDAIRC LLPMLKVSSL VLRALSVAAV FGLTLHGLRF DYTKLPLGLQ
     TIAAMEALHG STRTLHEWEA TFESILDRLD AEDTDDAEMA SQMNKLQMAL TAYRVAVDPI
     MKDALAGLGF DWKHERLGGL TRVTLPTGHS RWVCDLHRTM T
//
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