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Database: UniProt
Entry: G1QJY7_NOMLE
LinkDB: G1QJY7_NOMLE
Original site: G1QJY7_NOMLE 
ID   G1QJY7_NOMLE            Unreviewed;      1816 AA.
AC   G1QJY7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 3.
DT   27-MAR-2024, entry version 65.
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=LRRK1 {ECO:0000313|Ensembl:ENSNLEP00000001232.3};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000001232.3, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000001232.3, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000001232.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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};
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DR   EMBL; ADFV01101781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 61853.ENSNLEP00000001232; -.
DR   Ensembl; ENSNLET00000001307.3; ENSNLEP00000001232.3; ENSNLEG00000001049.3.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000160363; -.
DR   HOGENOM; CLU_255049_0_0_1; -.
DR   InParanoid; G1QJY7; -.
DR   OMA; GEEVIWC; -.
DR   TreeFam; TF313679; -.
DR   Proteomes; UP000001073; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   CDD; cd14067; STKc_LRRK1; 1.
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   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR020859; ROC_dom.
DR   PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR   PANTHER; PTHR48055:SF13; LEUCINE-RICH REPEAT SERINE_THREONINE-PROTEIN KINASE 1; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08477; Roc; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00364; LRR_BAC; 8.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          632..826
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1082..1365
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1589..1611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1642..1693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1642..1676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1677..1693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1816 AA;  202490 MW;  801F1405E8318F44 CRC64;
     MAGMSQRPPS MYWCVGPEES AVCPEHAMET LNGAGDMGSK PSTPGGDPTA QSHRTEGIRA
     AYRQGDRGGA RDLLKEACDQ CTSQLEKGQL LSIPAAYGDL EMVRYLLSER LVELPTEPTD
     DNPAVIAAYF GHTAVVQELL ESLPGPCSPQ RLLNWMLALA CQRGHLGVVK LLVLTHGADP
     ESYAVRKNEF PVIVRLPLYA AIKSGNEDIA IFLLRHGAYF CSYILLDSPD PSKHLLRKYF
     IETSALPSSY PGKTALRVKW SHLRLPWVDL DWLIDISCQI TELDLSANCL ATLPSVIPWG
     LINLRKLNLS DNHLGELPGV QSSDEIICSR LLEIDISSNK LSHLPPGFLH LSKLQKLTAS
     KNCLEKLFEE ENASNWIGLR KLQELDISDN KLTELPALFL HSFKSLNSLN VSRNNLKVFP
     DPWACPLKCC KASRNALECL PDKMAVFWKN HLKDVDFSEN ALKEVPLGLL RLDALMFLRL
     QGNQLAALPP QEKWTCRQLK TLDLSRNQLG KNEDGLKTKR IAFFTTRGRQ RSGAEAACVL
     EFPAFLSESL EVLCLNDNHL DTVPPSVCLL KSLSELYLGN NPGLRELPPE LGQLGNLWQL
     DTEDLSISNV PAEIRKEGPK AMLSYLRAQL RKAEKCKLMK MIIVGPPRQG KSTLLEILQT
     GRAPQVVHGE ATIRTTKWEL QRPAGSRAKV ESVEFNVWDI GGPASMATVN QCFFTDKALY
     VVVWNLALGE EAVANLQFWL LNIEAKAPNA VVLVVGTHLD LIEAKFRVER IATLRAYVLA
     LCRSPSGSRA TGFPDITFKH LHEISCKSLE GQEGLRQLIF HVTCSMKDVG STIGCQRLAG
     RLIPRSYLSL QEAVLAEQQR RSVDDDVQYL TDRQLEQLVE QTPDNDIKDY EDLQSAISFL
     IETGTLLHFP DTSHGLRNLY FLDPIWLSEC LQRIFNIKGS RSVAKNGVIR AEDLRMLLVG
     TGFTQQTEEQ YFQFLAKFEI ALPVANDLTA TESDGTPLME QYVPCPVCET AWAQHTDPSE
     KSEEVQYFDM EDCVLTAVER DFISCPRHPD LPVPLQELVP ELFMTDFPAR LFLENSKLEH
     NEDEGSVLGQ GGSGTVIYRA RYQGQPVAVK RFHIKKFKNF ANVPADTMLR HLRATDAMKN
     FSEFRQEASM LHALQHPCIV ALIGISIHPL CFALELAPLS SLNTVLSENA RDSSFIPLGH
     MLTQKIAYQI ASGLAYLHKK NIIFCDLKSD NILVWSLDVK EHVNIKLSDY GISRQSFHEG
     ALGVEGTPGY QAPEIRPRIV YDEKVDMFSY GMVLYELLSG QRPALGHHQL QIAKKLSKGF
     RPVLGQPEEV QFHRLQALMM ECWDTKPEKR PLALSVVSQM KDPTFATFMY ELSCGKQTAF
     FSSQGQEYTV VFWDGKEESR NYTVVNTEKG LMEVQRMCCP GMKVSCQLQV QRSLWTATEN
     SYLVLAGLAD GLVAVFPVVR GAPKDSCSYL CSHTANRSKF SIADEDARQN PYPVKAMEVV
     NSGSEVWYSN GPGLLVIDCA SLEICRRLEP YVAPSVVTSV VCSSEGRGEE VVWCLDDKAN
     SLVMYHSATY QLCARYFCGD PNPLRDVFPV RPLDTEPPAA SHTANPKVPE GDSIADVSIM
     YSEERGTQIL IHQESLTDYC SMSSYSSSPP RQAARSPSSL PSSPASSSSV PFSTDCEDSD
     MQHEPSAASD RSEHDLTLMD GETFSQHLQA VKILAVRDLI WVPRRGGDVI VIGLEKDSGA
     QRGRVIAVLK ARELTPHGVL VDAAVVAKDT VVCTFENENT EWCLAVWRGW GAREFDIFYQ
     SYEELGRLEA CTRKRR
//
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