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
//