ID A0A096LX68_POEFO Unreviewed; 1966 AA.
AC A0A096LX68;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:ENSPFOP00000023759.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000023759.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000023759.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. ROCO subfamily. {ECO:0000256|ARBA:ARBA00008171}.
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DR EMBL; AYCK01012404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01012405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000025097.1; ENSPFOP00000023759.1; ENSPFOG00000009664.2.
DR GeneTree; ENSGT00940000160363; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
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 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 InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF30; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51424; ROC; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
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:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 577..771
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1193..1477
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1966 AA; 220066 MW; 349E5748C52177AF CRC64;
ENIKAAYEGG DEETARELIQ QACYSNYTVV DKVRLLSVAT QHCDLVSVCY LLKEARITVP
QELSLSNPAV LAAHGGNTNL LKELLDSIPG VSLKRDLVNC LLATACQQGH LDVVRLLVHC
YDADVKDFAI HSDEFAVLCG LPLYAAAQAS NEEIAHFLLE NGAEFSSYTL MDYPDFSKRL
LRQKLDETSG ANGVEVSSAS VRVYWSGLQL PYLDLDWFMD VCSQITHLDL SSNSLGVLPS
VVPWGLIHLR TLDLSNNALK ELPFAQNSQD VICSRLQMVN ISQNQLKSLP TGLLHLVHLQ
KLCAADNQLS TLFDIPATVN WIGLRKLEGL DVSGNCLTSL LTSVMHCLKS LRCLDVSRNK
LNAFPDPWAC PLNQCKASSN QIENLPNTIS IFWRTQLQEV DFSDNCLKEL PSYIFELEAI
VSLKLCGNLI ETLPSANKWK CSKLKTLDLS RNQLGRTEEG PKSRRLAFLT TWNRRDPDPG
NVCPIEFPSV LRDSLEVLIL NDNQLECVPQ SLCALHNLTE LYLSNNPGIR ELPAELGQLS
NLWQLDIENL NINNIPQAVK DEGANSVLAF LRAQLRKAEP CRLLKMLVVG PPRQGKSALV
EALLTGKASP FTPSECSIST FSWELEKPNA GKNNKESVMF HVWDIGGPAS MTTVNQCFFT
DKSLYVVIWN LALGEEAVAN LQTWLLNIEA RAPNSSVVVV GTHLDLIDTK FRTERLATLR
AYVLALCRSP SGLRAAGYPD VTVKHLHEVS CKTLEGFDGL KMLLYHVALS MKDSSSSSGC
GSKLLARLIP RSYFILQEAV VEEKKRRHAE GEVQYLTEAQ LLSIIEQNPE SDIRDYEDLQ
TAISFLIETG TLLHFPDTSH GLCTLYFLCP VWLSDCLERI VHLNSCRPVP RNGVIKVEDL
RKLLAGTGFT QETEEQYFQF LAKFEIALPV ANDRYLLPHL LPPKPAMDIH SFHRHTNNTL
QRLFKMSFVP AGFWERFIAR MLISLTEMDV QSFDSAKNRS LNRRSSLIYS FAGSQQRNRC
STFRVRRSQT IYWKEGLLVT FDGGYLSVES SDVNWKKMKS GGIKILCQSD IRDFSAMAFI
TDHVNSLMEQ WFPALTGTQS DGSLLIEQYV PCSLCAPRDQ QQEQAEDGRR REAEVHYFNM
EDCVLAAVEQ EHIVCPQHPE QSIPLQELVP ELFMTDFPAR RLFLEKAQLE LCEEEQNILG
QGGSGTIIYR ARYRDQPVAV KLFHFKRCRQ LSATSDTDTM VKHLQFVNAC RSFSEFRQEA
SMLHSLQHPC IVALVGISIH PLCFALQLAP LGSLNTVLEK RHKGSEYMPL GHMLTFKVAY
QVAAGLAYLH RKNIIFCDLK SDNILVWSLE VQDPINVKLS DYGISRQSFH EGALGVEGTP
GYQAPEVRPG IVYDEKVDMF SYGMVLYELL SGRRPALGNH QLQIARKLSR GIRPVLGGLE
QVQFYSLHTL MTECWDTKPE KRPVALRCVR QMEEPSFPCL RYLLSCGSQS QLFLSQLQGC
SAVFWHGDNE DRNYSVVNVE KGQVDVKRMC CPGNRISCQM KMQNSLWIAT EEQEVFVYSL
KDMCPLSQPQ KRLSCPAVVT CLFHVPAAEQ SLAKVFAGMS DGLVAVYTLV DDLPLDGEMY
LCSHTLNKTV FGLKDSDPRQ RPYPVRSMAL LSSGSQLWFS NGPGLLVIDT SSLQAVRRLE
PYKAPSSIVS MTTSFSLCGE EAVWTLDDHS NTLKLYYAAS YELCATYCCG DRNPLRDVFA
VQRPAGMAAA AGDDINTTDQ NGKLEWSNGD VTLIFSEEAG TQIIQHQDSV TDYCSLSSTC
SLEPPQSNCL SATDCSSLKS RSCSPLAQNL QAQQESITTN LDSAEEINSV VPELQAFNLL
PVNGTVWIPR RGGDLIIIEI QSCGNQLRGR VSAVLSPPGL SSLGTLEEAA LVAKDMVVCG
FQQKENMEWC LVVWRAWGHQ ELDVFYQSWE ELYRSESSRR RRIHPN
//
