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Database: UniProt/TrEMBL
Entry: B7Q903_IXOSC
LinkDB: B7Q903_IXOSC
Original site: B7Q903_IXOSC 
ID   B7Q903_IXOSC            Unreviewed;       667 AA.
AC   B7Q903;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=IscW_ISCW011622 {ECO:0000313|EMBL:EEC15325.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC15325.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC15325.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW011622-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW011622-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}.
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DR   EMBL; ABJB010118019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010286420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010310013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010354852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010501597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010502164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010540761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010663878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB011040306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB011096310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS886656; EEC15325.1; -; Genomic_DNA.
DR   RefSeq; XP_002412436.1; XM_002412391.1.
DR   AlphaFoldDB; B7Q903; -.
DR   STRING; 6945.B7Q903; -.
DR   PaxDb; 6945-B7Q903; -.
DR   EnsemblMetazoa; ISCW011622-RA; ISCW011622-PA; ISCW011622.
DR   KEGG; isc:IscW_ISCW011622; -.
DR   VEuPathDB; VectorBase:ISCI011622; -.
DR   VEuPathDB; VectorBase:ISCP_032958; -.
DR   VEuPathDB; VectorBase:ISCW011622; -.
DR   HOGENOM; CLU_023684_1_0_1; -.
DR   InParanoid; B7Q903; -.
DR   OMA; MYLMEYQ; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR   CDD; cd20811; C1_Raf; 1.
DR   CDD; cd01816; RBD_RAF; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR003116; RBD_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR44329:SF262; RAF HOMOLOG SERINE/THREONINE-PROTEIN KINASE RAF; 1.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF02196; RBD; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          96..166
FT                   /note="RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50898"
FT   DOMAIN          176..222
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          383..617
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          63..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         409
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   667 AA;  74685 MW;  CAEFB7556C10DC69 CRC64;
     MIRLTKGNLE ALIAKFSQYQ HPPSMYIVEY EDLTGRLNEF QLREQTLLER LCQLDGSCSP
     DPCDTDSEEP CTAPLQGPRV PSTGEAKEVP RSPMKSVVRA FLPNQQRTTV QVRPGQTVME
     ALSKAMKRRK LTTEMCVVYK CSTRLAVDWG EDVTSLEDDE IQVEIKEKFP VTTSISHNFV
     RKTFFSLAFC ECCRKLLFHG FRCQTCGYRF HQRCASSVPT LCQPLRVEND YYKHLLAMQD
     VVGPQYEGGG YAPFLAPAAP CEASAPLSVP RPHPPPLGQR ERSTSAPNVC YNLVSSQDFS
     AEDLANRYRS HNSSAGGVGL APPQSCSSPG GSPTRTQSAQ GSPTSAHKAC RPRARSADES
     SKKLVTKPTR ESIEDWEILP DEILTGPRIG SGSFGTVYRG HWHGHVALKK LNVTNPTPAQ
     LQAFKNEVSV LRKTRHVSII LFMGCVSRPQ LTIVTQWCEG SSLYKHLHVL ESKFEMLQVI
     DIARQTAQGM DQILSHAGEG RRREGARGFG TWLAQHNPRA PEVIRMKDPN PYSFQSDVYA
     FGIVLYELIT GQLPYAHINN KDQILFMVGH GLLRPDLSIA RKDTPKALIR FTEDCIKFNR
     DERPLFRQML ASLESLMRSL PKIHRSTSEP TLNRTHLQSE DFLYVCASPK TPSQFGAFPF
     FSTTGNF
//
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