ID A0A0V1LT89_9BILA Unreviewed; 667 AA.
AC A0A0V1LT89;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinase suppressor of Ras 2 {ECO:0000313|EMBL:KRZ62667.1};
GN Name=Ksr2 {ECO:0000313|EMBL:KRZ62667.1};
GN ORFNames=T02_11075 {ECO:0000313|EMBL:KRZ62667.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ62667.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ62667.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ62667.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ62667.1}.
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DR EMBL; JYDW01000007; KRZ62667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LT89; -.
DR STRING; 6335.A0A0V1LT89; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR23257:SF780; AT08303P; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00109; C1; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KRZ62667.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transferase {ECO:0000313|EMBL:KRZ62667.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 54..110
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 357..621
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 159..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 74981 MW; 1F55CA74AD09BF48 CRC64;
MVILLCSNPK RGVVAVVNYE PPSSESCEKW NSSDESLAST PTSGYNSGYP FVINCRFIKK
FFSFPKTCNS CNKLVIGAGF SCRNCHFRCH KRCAIVIDEN KEPRLKSKMC SLSRLPPESA
DFFARLFDSS KQWKRNDDLF SPEDMQKCRS KKLQVADNER SLDSCSGNAL NQSRPDPTVP
ANNLSGDGFG FAQSQRPSLS SCTTQSLTSG PHFNKEADDK SQPTAFNQLL FTEQLKKVKR
LHDDNLIQAN NQHQSNGRHK AENDAKLSSA RSPSSHLHIN SKVLNNKVEH RRRLLSHMLA
CNCITCGTRV NTAQNKSTLA TAGRKATYCN SEDRGNRRSL ANHTSDLNEW TIPFEDLKFE
QCILHSQSIT VFKGEWHGPV MINVFPLQRD GSNLATFLDD VHALNKIRHE NIALFMAVSI
EPPHLAIVTC LNKGISLYQA LHVENVRPFS EQQKLNIAGQ IAQGMSYLHA RGVTLKTLSS
KNVMLESKVK ISMLDYGVAP SKYDRCNKGC TRRGNLTYLS PELLRGLHVQ PPTVVLHSVQ
TEQSDVYAFG TLVYEIFTST FPYEDLTSEE LIWSVCSGKM ANLDALRGQT ILQNLCHKCW
TFDRFERPSF PTVLQMLHHH TNNILSKTNS SSMPNAIHLV GEPHHRGEVF QFGIVNMRVL
ENLNDKN
//
