ID A0A2R2MNR6_LINUN Unreviewed; 1963 AA.
AC A0A2R2MNR6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Leucine-rich repeat serine/threonine-protein kinase 2-like isoform X1 {ECO:0000313|RefSeq:XP_023931687.1};
GN Name=LOC106175217 {ECO:0000313|RefSeq:XP_023931687.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_023931687.1};
RN [1] {ECO:0000313|RefSeq:XP_023931687.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_023931687.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_023931687.1; XM_024075919.1.
DR STRING; 7574.A0A2R2MNR6; -.
DR EnsemblMetazoa; XM_024075919.1; XP_023931687.1; LOC106175217.
DR KEGG; lak:106175217; -.
DR InParanoid; A0A2R2MNR6; -.
DR OrthoDB; 148126at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; 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; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_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; 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; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF13; SERINE_THREONINE-PROTEIN KINASE DDB_G0278509-RELATED; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SMART; SM00364; LRR_BAC; 9.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 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 SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51450; LRR; 3.
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|RefSeq:XP_023931687.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|RefSeq:XP_023931687.1}.
FT DOMAIN 737..921
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1296..1559
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1963 AA; 222435 MW; EB708DAC2F3AE6DF CRC64;
MALKVQSCKE KRRQRQLVKE SIPQDAASPQ LQLRYTFSRG HLMQQMKNPN PGLVLPTPKK
AHSHPGLSEK ERCGSYDALD GATPRRKSGM QIMKELLFKS SSQDDNSYDA LQVNKSQQSN
KWRRKTLATS SFREPSPTPE SQDRRRSSLV TIAVDEPDNS KVKPPKSPSF SFQKEEFEEW
KKGSVSGANT PFSRFDPRLT PEAESKDCLL EEIPWTSKFG RQGTDITKKI ASPLKRPSLP
VTPSRKITRP LKRVKSNIEK GTPGSPYLLS VEDYLLPVPK IVITRKPADM VDTPPSISLE
DLLLPRRKFT NEPGPIIDIS SLISTTKNVS FSHVEQFESI LESSLECSES SIPSGSNSNI
PEMPRKRSLT EGNLPGMVCH QQDLVSLDVS SNRIGSLSDL MDKSLLVHFQ AIQKLDLSQN
HLQNVPDELF EYLPKLEELY LRYNFITTFP AQALACKGLK IMDLSFNHIE DISKPPATTS
FSIHHFNISQ NRLGSIPDWI SDNMPGLTEL DIKGNKITKL PDRPLLLKKL HTLDIAQNYL
TEIPEQFLEE FNALEKLDAS CNELEKLPSP QVAKTLPKLQ TLKLSRNRLG QEEAPYIPKF
ILHLERLESL DLSHNDLTDI PTPKNWKTPN LREFFLGNNK IEKLNLGGEE ARLWSGLERL
EINHNELSEV PKEIGLLSSL TSLDIGHNSI LTLPDEMGRL NKLWELRYDR LELDLPQAIL
KGRTRDLIVY LSERLRNASE HYRMKMMVVG YAGRGKSTLI RTLMKLPQPD KSIATVGVQV
KDWELRTGRR KPPHYTLSTW DFAGQEEFYN THQCFLSNRS LYLVVYNLQI GPSEVETLRP
WLLNIKARAP HSPVIIVGTH KDGLAKDERE QKIKEMRSLI SELCCKPGFP DVKAVIELNC
CYESSDIERL RDKIKEAVEG FKIKGQPVMG QKIPESFIKL EELVSYEAKA RATLPVIKAQ
TLRKIIKDAN LDLDNEELKQ AVRFLHESGV MLHYEDASQQ LENFYFLDPQ WLGRMMAQVI
TVREINPFID EKGILRKTDI NLLFNGKRFE KFNFPTSLIP QYLRLLEKFE IILPRGNDEF
LIPCRLPAKK PPISFPGLSD VVDSNGNRKP IQIQRQYEMP YIPLGFWSRL IARLVVFIPK
MSANNPDSGV VPETVYWIEG ICVYWSELLY FMIEPFCRDG HEVVVITVPL SKMGTSVLGH
IVDHIDTLIE EWYPGLTEKS PTGLELVQRI VPCSQCIGPS IHHFVLDDLV SQSELDASMN
CPNCGPVPLS RLAPDVIFAD LEDHFQIDPQ SFFFNKSPEY LLGDGGFGSV YRAKYKNKEV
AVKVFNAVGD IHPHKMMRQE VTIIRELNHP SLISMVAVGV NPRAILLEVA PLGSLGSLLK
TRTLGRAEQQ RIAMQVAEGM AYLHHNMIIY RDMKPENILI FNLALGPNVV INAKISDYGI
SRFAAPCGLR ASEGTPGYRA PEVIRGEVYG AQADMYSFGM TLYELVTNGR HPYDDLSFRN
QLDEAVLMKR PINPITTKLD PMTGRPCCQP WPDMQDVIYL CLKYVPEERP TAAEIHEKLE
RCDLLSLRNF LPISKNMTVE CMTLRHDGDG MELWVGSGGS EDCAQLSWVS LTENDPKILD
LTLSLQGKFH PDSRILCLTT IGSSCVLIGC LSGHIWVYDA YTREHKHKLP RLPDSVLCMH
FHQNQSGDAQ VYVGLASGQL AIFDANNVLT DAFAEPSYTL RFGESSEPIR CIVPHTQSKT
LYIGCGSKIV MLLPDTWRDI PQEIDTATEQ SRGIICAMVV SRKYLYLAKM QEATVEAWDL
NKQVLKHTID IYKTVSEFDP SMKLSRGDCR VTSLLLQNTH TLWVGTGEGL LVILDTNSLR
PCAVLKRHRT AVRCMINVIL KSQRGTSCVV TGGFGFHTFR EEFETAQDEK TYGYIAMWDG
GLDQHARQLQ EYQKRRHGGF MDADSMSVHS DSFSVLKEQQ DWR
//
