ID A0A1J1IT77_9DIPT Unreviewed; 1841 AA. AC A0A1J1IT77; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 24-JUL-2024, entry version 34. DE SubName: Full=CLUMA_CG015381, isoform A {ECO:0000313|EMBL:CRL02310.1}; GN ORFNames=CLUMA_CG015381 {ECO:0000313|EMBL:CRL02310.1}; OS Clunio marinus. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae; OC Clunio. OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL02310.1, ECO:0000313|Proteomes:UP000183832}; RN [1] {ECO:0000313|EMBL:CRL02310.1, ECO:0000313|Proteomes:UP000183832} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Syromyatnikov M.Y., Popov V.N.; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 CC subfamily. {ECO:0000256|ARBA:ARBA00008959}. 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 EMBL; CVRI01000057; CRL02310.1; -; Genomic_DNA. DR STRING; 568069.A0A1J1IT77; -. DR OrthoDB; 5475340at2759; -. DR Proteomes; UP000183832; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0004679; F:AMP-activated protein kinase activity; 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:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008047; F:enzyme activator activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:TreeGrafter. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IEA:TreeGrafter. DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:TreeGrafter. DR CDD; cd00009; AAA; 1. DR CDD; cd12122; AMPKA_C; 1. DR CDD; cd18139; HLD_clamp_RarA; 1. DR CDD; cd14079; STKc_AMPK_alpha; 1. DR CDD; cd14336; UBA_AID_AMPKalpha; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.272.10; -; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.1020.10; TAZ domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032423; AAA_assoc_2. DR InterPro; IPR051314; AAA_ATPase_RarA/MGS1/WRNIP1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR032270; AMPK_C. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR021886; MgsA_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR049020; PRKAA1/2_AID. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR035898; TAZ_dom_sf. DR InterPro; IPR000197; Znf_TAZ. DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1. DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF16193; AAA_assoc_2; 1. DR Pfam; PF16579; AdenylateSensor; 1. DR Pfam; PF21147; AMPK_alpha_AID; 1. DR Pfam; PF12002; MgsA_C; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF02135; zf-TAZ; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00551; ZnF_TAZ; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF103243; KA1-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF57933; TAZ domain; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50134; ZF_TAZ; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00203}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000183832}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00203}. FT DOMAIN 681..765 FT /note="TAZ-type" FT /evidence="ECO:0000259|PROSITE:PS50134" FT DOMAIN 1323..1575 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT ZN_FING 681..765 FT /note="TAZ-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203" FT REGION 775..829 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 809..823 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1352 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1841 AA; 210407 MW; FE63B6DF77D6FC99 CRC64; MPKHIKRWCG GILGASTLIG LAFYDSYRCV QRLRRPLNTN FLTKRCEYIY IKHNYLREPV KDILNELFQE ETMIYSVLYN IKKKLTFTKI EYALKTLRVA KHSTSPFERR KAIRNLSSIR LDLDDWEFRF LAQYCNSETA VSLARSLGDP NLIRKPREFG KFRTKSEIVA DFKSMLEKMK DNPCVKFIFE TTSAFENIKD VDHETSFHDF HHENDHIHQS LDHLLHLTND PRLCLKIAEH DGLDIILDIY KTFKDNIDIK MILTKIITNM SSSHDTMIDY FHKSGWLYLL SNWQCDEDLR IQVLASTSLH NLDKYDNSSF IYRPKLYPLY PRTKINKDPA VDVIFVHGIL GGIWITWRVQ RESDISSVEK NQKSILPFDE NIQNSFIQEE AVFRDEKIVQ MEPGPANKIL TITQETAKRV IAALHEMAED KLTNDDMKLS RQILKHIVKK IDEQKYSYCW PIDWLPQQFP SARILGLQFE SALSYWVKKV CPCERDKLKL KYRSLDYIPR LADAGIGNDR PIVWICHSMG GLIVKGIINE ALKSNDPNVR KIGENTRGII FLGTPHRGSA IAKYSQQAGV LWPTIEVQDM EENSKDLLKL NDEFLENVSD TKNHVEIVSI AEGSSMKVFQ NIKLIVVPLE SAYLGYGEFY GGSKTSPGDL QNMISKMMKN ANQHEQRVRH VSSREEAINR CLSSLIHALN CREGVSCVAA GCQKMKRVVE HTRTCQRKTS NSRGCPICMQ LMSLCLYHSK LCRQTVCHVP FCRIMKRKLQ AANEHKAQQQ SIQSLKPVPQ FVIPPINNPP PSSVRREENS SEPSPKRMRL ENDSSVNNEA QQHKLSSMIK NKFISAESIE NHANDCFEQQ SQKLLSPSIN KRKSNENTYK IFSFNKKQKI AIDDNDETKT SSSMQQPKES LKSPLAEFIR AENFEQYVGQ KQVVGDNSLI RKLLKSNDIP SMIFWGPPGC GKTTLANLIY KQQCNQDKDH FRFIKLSACT SNISDVKEVV KQAKSYKDTV KKRTILFMDE IHRFNKLQQD AFLPHVENGT IVLLGATTEN PSFSLNNALL SRCRVIILEK LKSEEIMEIL RRAIIQFKAI EVKNETTERN VLENHVSKLN FSPEICITEE CLQWIADTSD GDARIALNSL EMSLKQASAA RKESDEVLKP IVLNDIKDGI KKSHLLYDRV GDQHYDIISA LHKSIRASDD NASLYWVTRM MMSGEDPRFI CRRLIRAASE DIGLADPQAL ILATSTLTAV QQIGMPEADC IIAQLVVYLA RAPKSVESYG ALLKCKNQIM IHKGALPSVP IHLRNAPTKL MKNLAPLIKI GHYTLGRTLG NGTFGKVKIG EHIVTKHKVA IKILNRQKIK SLDVVGKIRR EIQNLKLFRH PHIIKLYQVI STPTDIFMIM EYVSGGELFD YIVKQGKLHE SEARKFFQQI ISGVDYCHRH MIVHRDLKPE NLLLDHNMHV KIADFGLSNM MMDGEFLRTS CGSPNYAAPE VISGKLYAGP EVDIWSCGVI LYALLCGTLP FDDEHVPTLF RKIKSGIFPI PEYLNKQVVS LLCQMLQVDP LKRATVEEIK KHEWFQKDLP AYLFPSPVEQ DSSVIDTGAV TEVCEKFGVK EIEVHTALLS GDPHDQLAIA YHLIIDNRRM DEAAKAEIKD FYVASSPPPV VTPSHPISDP NPGKPHPERI APLRERALNL QTSSYTEGPT AVATLVGQEK YRGTPVKRAK WHLGIRSQSK PNDIMLEVYR AMKALDYEWK VLNPYHVRVR KKNKEDHYVK MSLQLYQVDP KSYLVDFKSL TNDEVEQSDD IISLTPPVSG QQQQSQNQQI TGHHTMEFFE MCASLIIQLA R //