ID A0A6P4JVZ3_DROBP Unreviewed; 1216 AA. AC A0A6P4JVZ3; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 03-AUG-2022, entry version 8. DE SubName: Full=LIM domain kinase 1 isoform X2 {ECO:0000313|RefSeq:XP_017086986.1}; GN Name=LOC108118705 {ECO:0000313|RefSeq:XP_017086986.1}; OS Drosophila bipectinata (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=42026 {ECO:0000313|Proteomes:UP000515201, ECO:0000313|RefSeq:XP_017086986.1}; RN [1] {ECO:0000313|RefSeq:XP_017086986.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2022) to UniProtKB. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. {ECO:0000256|ARBA:ARBA00005843}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_017086986.1; XM_017231497.1. DR GeneID; 108118705; -. DR Proteomes; UP000515201; Unplaced. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001781; Znf_LIM. DR Pfam; PF00412; LIM; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00132; LIM; 2. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 2. DR PROSITE; PS50023; LIM_DOMAIN_2; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Kinase {ECO:0000313|RefSeq:XP_017086986.1}; KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE- KW ProRule:PRU00125}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00125}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Transferase {ECO:0000313|RefSeq:XP_017086986.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}. FT DOMAIN 34..96 FT /note="LIM zinc-binding" FT /evidence="ECO:0000259|PROSITE:PS50023" FT DOMAIN 97..157 FT /note="LIM zinc-binding" FT /evidence="ECO:0000259|PROSITE:PS50023" FT DOMAIN 174..255 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT DOMAIN 379..669 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 531..571 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 743..796 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 844..886 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 992..1113 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1158..1216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 756..779 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..886 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1019..1037 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1074..1113 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 408 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1216 AA; 134105 MW; C873FA9C9582C946 CRC64; MHQQQQRLRT NGASQRPGGG GGGGGGPGSY FSGPSCAHCR GQLLPHPEEP IVMALGQQWH CDCFRCSVCE GHLHNWYFER EGLLYCREDY YGRFGDACQQ CTAVITGPVM VAGEHKFHPE CFCCAACGSF IGEGESYALV ERSKLYCGQC YGKRSCQPAD AKARITTAGK PMHSIRLVEI PKDATPGLRV DGVALDDGCP TVRIAEIDVN LTNLHIGDRI LEVNGTPVSD SSVEQIDKLI RSNEKMLQLT VEHDPVQVCR SCSQADIQRA CSASTLVLPL STSASSVEVG GRERLYRAQG EQSAKARKLR QASNASSITI PNATTQLKEK ERCSSLSKLL DEQHQAQQHS AHPQLYDLSR TQSCRVVQKP QRIFRASDLV IGEKLGEGFF GKVFKVTHRQ SGEVMVLKEL HRADEEAQRT FIKEVAVLRL LDHRHVLKFI GVLYKDRKLH MVTEYVAGGC LKELIHDSRQ ILSWPQRVCL ARDIACGMSY LHSMNIIHRD LNSMNCLVRE DRSVIVADFG LARSVDAPRI PGASGAAGPG TPGGYGSATN SDAAVSPGGT LRRSKSRQRR QRYTVVGNPY WMAPEMMKGL KYDEKVDVFS FGIILCEIIG RVEADPDFMP RNSDFSLNQQ EFREKFCAQC PEAFVKVAFV CCDLNPDMRP CFETLHTWLH GLAEHLTVER QRPPETLLHE IENFQESYAS SEDALSPTSQ RSLDNLDEIV KDAAPVEVEV SPVEKEKENL VIRPQDIPKS PHLGKDFSPS GERLRDSMRA RRRQRFLGAQ EAQRRNLTPE TESKERALKQ ALRKCRPFGE RGYLVDLRPG GDLQLQDVRD LNTYSDVDSS CDTSLNYHEV NNPPAATDLP GAEPQPEVEE EQPPPAGKEE PPQHRQQIED MRTRLNQCRS KFEHLEEASR RNFSQSQHSM RNFFKTPPVA LKMFQRLEHE AAAAMNGCQA TAPPPLPPRT QRINQTPIFG RKNPPIPVAA DQQKLQHSES LENLVGGRKS MPAIPAPKRS KGPPVTQPPT IILANSSSSN GTTAATTVDF PPKKHKLTLP LPPQSQLARS GHSKPPSSAK VKPLNVQPPP SSSRIVSTTS ISPTRNSRPS SPTKHLAQRH TAATAQRLNN VAATAAHHQQ QPSSRTTRLN ILSPEKVHRL GARLTDQKQK LREEAAAGSG CAPGVGGSAA NGHRTGATGG ASAAAGDRRR RAAPTPPART HFNTRC //