ID A0A0B2V5Y0_TOXCA Unreviewed; 1017 AA.
AC A0A0B2V5Y0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=lrk-1 {ECO:0000313|EMBL:KHN76857.1};
GN ORFNames=Tcan_05220 {ECO:0000313|EMBL:KHN76857.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN76857.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN76857.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN76857.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the SHOC2 family.
CC {ECO:0000256|ARBA:ARBA00023786}.
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:KHN76857.1}.
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DR EMBL; JPKZ01002413; KHN76857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V5Y0; -.
DR STRING; 6265.A0A0B2V5Y0; -.
DR OMA; NCIKSVP; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020859; ROC_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF12799; LRR_4; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00369; LRR_TYP; 9.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51450; LRR; 6.
DR PROSITE; PS51424; ROC; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KHN76857.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KHN76857.1}.
FT REPEAT 78..110
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 763..985
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT REGION 527..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 112046 MW; AD72FA3301D13490 CRC64;
MEFPYEEDVL TRIEDASGRF SYRFVADVNA LDSQCRTALY LAVANSHYDV VKYLLEVKFP
SMSTEHKCPF QLDVYCSGGR TPLMVAAANA NLPLVKLLLD HGADVNLPCA LTDADISSVE
GARCVGSGAL NEACRVGCAP LVQLLFQHGA IDHENVALAT AVKYEQEALV RLLLSRLVFV
DPDYRVNKKG IDFGQMTINR NLLPSTVFPT TSCMLNWHNA SLSVIANDWL LSACLQLNQR
LRTSRMALAA LTRIDISSNK LTALNASLLQ LPSLRSLTAA YNQIEQLEMP SDGWNAPMLE
SLCLEHNQLT QLPQQIFSSR LPNLGVIDVS FNKLTHLPDT VWMAPRLREL NVANNCLSAI
PAVAGCSLKP VNRLSASDFR DGSLAESKTF HSTVSTDDSL SISGRIDDPN ITIHELKRHN
LWQASVRLAR SDESDTEGGA IISSSTLSLL NVSHNQLKVV PACLACCCPR LARLNISHNE
LASLGPVECL PSRLRHLDVS HNQLIMAFEQ ATNAHLVCHA TATTGSNGVT QLRQNSPTRN
PRSRSKSAVR SQRSLSVARI GDALRDSHVD ACVHKQHTRL ESLRTFQAGG NRLQEIPLMI
PGAPALSPRK KLRDARLKDT NNKRRNLIFP ALTSLDVSNN CIKSVPAALS CLSSLSVLNL
SNNTAIESLP PELGLLALTS LDVSNNCIKS VPAALSCLSS LSVLNLSNNT AIESLPPELG
LLGKLWNLNL KGCSLRDPIR SMIQVDNYKT VDLIAYLKSI LEDSRPYTRL KLMIVGVQGI
GKTSLLQQIR LEGTVGKRTQ PNDSWSRRMG HTAANADRTA KGANISTVGV DIAEWTFEPK
KIKGEPTFGP ITFRTWDFGG QREYYATHQY FLSRRSLYIV VWRATDGDAA IPDMHQWLVN
IQARAPNSPV IIVGTHVDQI LSNAERFPNG YLDELEAVIR ERFVLVPDAD KKGLPRVVDS
MFVSSKTKHN IRALCNLLYR TAFDIRTAGS KERLLDQKIP ASYLALEKAS CFIFFFD
//
