ID T0Q219_SAPDV Unreviewed; 942 AA.
AC T0Q219;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=TKL protein kinase {ECO:0000313|EMBL:EQC31879.1};
GN ORFNames=SDRG_10397 {ECO:0000313|EMBL:EQC31879.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC31879.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC31879.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC31879.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH767166; EQC31879.1; -; Genomic_DNA.
DR RefSeq; XP_008614607.1; XM_008616385.1.
DR AlphaFoldDB; T0Q219; -.
DR STRING; 1156394.T0Q219; -.
DR EnsemblProtists; EQC31879; EQC31879; SDRG_10397.
DR GeneID; 19951124; -.
DR VEuPathDB; FungiDB:SDRG_10397; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR InParanoid; T0Q219; -.
DR OMA; IENKACE; -.
DR OrthoDB; 4263002at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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 Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 7.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24180; CYCLIN-DEPENDENT KINASE INHIBITOR 2C-RELATED; 1.
DR PANTHER; PTHR24180:SF43; NAD-DEPENDENT DEACETYLASE SIR2B; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 6.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00248; ANK; 18.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 13.
DR PROSITE; PS50088; ANK_REPEAT; 14.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Kinase {ECO:0000313|EMBL:EQC31879.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:EQC31879.1}.
FT REPEAT 67..99
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 100..132
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 133..165
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 166..198
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 199..231
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 232..264
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 265..297
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 298..330
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 331..363
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 421..453
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 487..519
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 520..552
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 553..585
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 586..618
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 657..918
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 942 AA; 102386 MW; 7816C7FB207F3E33 CRC64;
MSLSRGRDTR RAIIRMTRRA RSTVISTMSW FWSRKDVRLA QAAKDGNLYD VTKLLDAGLD
PNSFDEEGHA PLYLAAAKGH YAVASVLLQA RADINRSDRV GQTPLLIAAW NGHDKVVAIL
LQARADVNKG RRDGWTPLHS ASFNGHAAVV ALLLQARADI NRISKVDRTP LHLAAVKGHL
RVVSLLLDAH ADVNEIDTVG QTPLHIAAWN GHDSVVQLLL HARADVNKND KAGWTPLYVA
SEKGHVAVVA LLIAAHARVD QRRGDAWTPL HVAACNGYAA VVSLLLQANA DVNSTSKAGW
TPLHLAAVKG HAAVVSLLLG ANANVDQTDH EGQTPLHIAA EKGHASLVTL LLEADADINI
KSRAGRTPLM LAKEKNHDNV GAILEDIMAF KLVDAVRQGD LDQVFHTIVH ERLSPNTINT
NGESLLFTAV LSRNAKMTRT LSDAGADVNK GDENGRSPLI AAIELDHFPT IITLLQAKAD
VNQGPPGGMT PLCMAAFNGQ EAITSMLLSC NADVNLPGTD GQSPLLLAVT AGHKGVVGML
LVAGADVNGA NAHGYTPLAR ATMNGDSVLV EMLLAGGANV NQTDKEGRTA IFVAASKGDD
PMVDLLLEAH ADVTIENKAC ESPLQVAIKH GYRKIAQKLH SILVLEAPKI ELDEIELLSE
QPIGRGGQGI VYKGRYKTTE VAIKTVFDKE GIAALEIEIE NIIRCNSPYI IKLLAAYGLH
TNEPKMVLEY MNSGNLRHYL NRKRDGLPVA LEFSTLQIAW VIANAICDLH EKNLLHRDLK
SDNVLLCSTN YIKLADLGIS RQYDIHTMTS AVGTWHWIAP EVFDGGHYDF SADVYSFGVI
LTELETYQRP YWNVHLGQMT LIDQVRNGVL RPTLSAKCDE WYRQLTEACL RHDPASRPKA
KEIVKCLEGQ IAQSRKFIDR SWETASFAAM TMVPLANLAR AA
//
