ID A0A3N0XQG1_ANAGA Unreviewed; 1966 AA.
AC A0A3N0XQG1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Leucine-rich repeat serine/threonine-protein kinase 2 {ECO:0000313|EMBL:ROJ24393.1};
GN ORFNames=DPX16_20946 {ECO:0000313|EMBL:ROJ24393.1};
OS Anabarilius grahami (Kanglang fish) (Barilius grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Xenocypridinae incertae sedis; Anabarilius.
OX NCBI_TaxID=495550 {ECO:0000313|EMBL:ROJ24393.1, ECO:0000313|Proteomes:UP000281406};
RN [1] {ECO:0000313|EMBL:ROJ24393.1, ECO:0000313|Proteomes:UP000281406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-KIZ {ECO:0000313|EMBL:ROJ24393.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:ROJ24393.1};
RA Jiang W.;
RT "Genome assembly for a Yunnan-Guizhou Plateau 3E fish, Anabarilius grahami
RT (Regan), and its evolutionary and genetic applications.";
RL Submitted (OCT-2018) 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:ROJ24393.1}.
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DR EMBL; RJVU01063551; ROJ24393.1; -; Genomic_DNA.
DR Proteomes; UP000281406; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR010603; Znf_CppX_C4.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000313|EMBL:ROJ24393.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000281406};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:ROJ24393.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 161..342
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 710..973
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1426..1479
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 1401..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 737
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1966 AA; 219060 MW; 3CBBB13FEF3A6424 CRC64;
MAPCLSWNSA VAPSGGVNAD LALGQVEWGC LRSVDMRNNS ISVLLGPAFW VSVNLRELMF
SHNHISALDL SGPVYKWARL EKLHLSSNKL TEIPPQIGML EDLTSLDVSQ NEGLRSFPDE
MGKLVNLWDL PLDGLQLQLD LKHIGSKTKD IIRFLQQRLK KAVPYYRMKL IVVGSPCSGK
SSLIQQLIRL KRSQWHSDQH TVGVSVRNWP IRNKEKRNML LNVWELSGAE ECSGFHPHFM
SSRALYLVLY DLKKGTSEID AIKPWLFNIK AVAGQSPVIL VGTHADVCEE HHLQECVLKL
REELLSQPGF PVIKDSHMLC ACEESESISR LRKAIYRELI EFKIQGQPVM GQLIPDCYVE
LERRVLQERS CVPADFPVLW HSRLLEIIQE TQLQLEEGEL PHAIHFLSEA GVLLHFDDPV
LQLKDLYFID PQWLCNVISQ TLTLRSFGHW DSTRGVVQRS AIEKFLDKSH CFPKNHLTQY
FKLLEKFQIA LPFGDDQLLI PSSLSDQRPV IELPHCENSE VIIRLYEMPY FPMGYWSRQI
SRLLEVSAFL LYGTEKALRP NRIYWRKGIY LSWSAEAYCL VEALPLEESS ASFIKITVPC
SRKGRVLFGQ VVDHIDSLLE EWFPGLLATD VHGTGETLLK KWALYSFSDG QNCQKMLLED
LLSNINADGL LVNPVDPSCT LPISQISPDL VLSDQPSSTI LDPEQLEMEL SKEYLLGDGG
FGSVYKAVYK NEEVAVKIFN KHASALYVHR LVRQELAVLG RLCHPSLVGL LAAGCNPQIL
VMELAPCGSL DSLFERENGS LSWKLQHRIA LHVADGLRYL HSSMIIYRDL KPHNVLLFNL
KTDAEFIAKI TDYGIAQYCC SMGVRSSEGT PGFRAPEVAR GNVIYNVQAD VFSFGLLLYD
LLTCGERISD GMKFPSEFDE VAVQGKLPDP VKDYGCSPWP GFESLMRDCF RENPQDRPTS
AQVFDRLNSA EMLCLMRELN LMSLPGECFA VCSAGGVANR GTNARVWIGG GSSSKKVGCV
TSLDLETGGR LSQEIDSSPV LCMVIIRAPG SCNDWLVAGT QSGSLIIMDT INAEVLHCLK
SVNDSVTSLY FHTDQQRCLK NYLLVGTANG TIVVYEDSVL KVKNGGPVKT LQIGDVNTPL
MCIGPSNHPQ ERKALWAACG TRVILLSVEY NIYRSIDTKP KLLLPKQGRV SSDACISRLV
VDKHVYVSKT RSHAVEVWDK KTERMVNLID CTQLLGLSSN KKSKAQDEDQ HRQMVPSLAI
VKALLVQHSG TLWIGTKTGH ILLVDVSSCQ LLQTFSPHCD SIRCMGSAVL ETLNRKNVIL
VLGRRQRMPQ DQIKMQLAED SVLTVWSSSL PLEVRDLIRH CFSRSHVQLF SLTRPVCDEV
HLPRFLHNRS FSQTAVCFAS KESSPRDGDG GKKGVTEAGG KRASGGGGSG KGGSQLRCPK
CGDPCTHVET FVSSTRFVKC EKCHHFFVVL SETDSKKGLN KEAESSEHVK FALAQKPPPP
PKKIYTYLDK FVVGQSYAKK VLSVAVYNHY KRIYNNLPAV GRQQQAEAEK QSSLSPRELE
IRRREDEYRF TKLLQIAGIS PHGNALGASV QQQTNQQAPQ EKRGGDVLDS AHTDIKLDKS
NIVLLGPTGS GKTLLAQTLA KCLDVPFAIC DCTTLTQAGY VGDDIESVIA KLLQDANYSV
EKAQQGIVFL DEVDKIGSVP GIHQLRDVGG EGVQQGLLKL LEGTIVNVPE KNSRKLRGET
VQVDTTNILF VASGAFNGLD RIISRRKNEK YLGFGTPSNM GKGRRAAAAA DLANSSGNEL
DAMAEIEEKD RLLRHVEARD LIEFGMIPEF VGRLPVVVSL HSLDEEMLVQ ILTEPRNAVV
PQYQSLFSMD KCELNVTPDA LRAIARFALE RKTGARGLRS IMEKLLLEPM FEVPQSDIIA
VELTKDVVQG KCEPRYIRAP PKETEEEFDS AIEEDNWLRH ADAANN
//