ID ATG1_ASPNC Reviewed; 1007 AA. AC A2QIL5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 25-NOV-2008, entry version 16. DE RecName: Full=Serine/threonine-protein kinase atg1; DE EC=2.7.11.1; DE AltName: Full=Autophagy-related protein 1; GN Name=atg1; ORFNames=An04g03950; OS Aspergillus niger (strain CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., RA Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., RA Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., RA Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M., RA Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., RA van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., RA Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., RA Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., RA van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., RA van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., RA Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., RA Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., RA Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., RA Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., RA Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory RT Aspergillus niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). CC -!- FUNCTION: Serine/threonine protein kinase probably involved in the CC cytoplasm to vacuole transport (Cvt) and in autophagy, where it CC may be required for the formation of autophagosomes (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. APG1/unc-51/ULK1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM270075; CAK38659.1; -; Genomic_DNA. DR RefSeq; XP_001401761.1; -. DR GeneID; 4990801; -. DR KEGG; ang:An04g03950; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Autophagy; Complete proteome; Cytoplasm; Kinase; KW Nucleotide-binding; Protein transport; KW Serine/threonine-protein kinase; Transferase; Transport. FT CHAIN 1 1007 Serine/threonine-protein kinase atg1. FT /FTId=PRO_0000317788. FT DOMAIN 30 336 Protein kinase. FT NP_BIND 36 44 ATP (By similarity). FT ACT_SITE 174 174 Proton acceptor (By similarity). FT BINDING 59 59 ATP (By similarity). SQ SEQUENCE 1007 AA; 108897 MW; D15EEE57D480DAFD CRC64; MGLFHHSTLF LPLLRRSNEG PHGEMPIGHY TRLSEIGRGS FAVVYKGVHT RSRTYVAIKS VTMTKLSRKL KENLASEISI LKQLHHPHIV ALLDCHDTTS NIHLVMEFCA LGDLSHFIKG RNTLQDSPYT RELIAKYPNP GEGAGLNEVI VRHFLKQLSS ALRFLRDRDL IHRDIKPQNL LLCPAPSSYR SGAADVVPFK SSEDSFSPKT GLESLPMLKL ADFGFARSLP ATSLAETLCG SPLYMAPEIL RYEKYDAKAD LWSVGTVLYE MVVGRAPFRA VNHIELIKKI EQNKDQISFP SKNRVSEDIR ELIRGLLKQH PMDRMNFDVY FAHKVLTEPI PGLVADDAPL GRSPADPTPR PGSGSRRSTP VQMKRENALS GGVRDEPATY PAAQRAMTQS PRPETPSTPM RRTGSAGTPH AAPNEPTPPA SHPTRPSPVS LATAPGRQEH VDRPPTTTVV EQQRRRTASS GVPQVDKPVE KAKDEKEHAA QEVAFERDYV LVEKRAVEMN AFADELAYNP RMQGGQAGAV SRRSGAAPGT PPAGGSSPHA SPSKAMQIIS GRSRADSAHV RQNSYDRRYG QSPTSATSAI SKALNMASGR LFGMSFSPPL TITKGGRSPP LAYNPFPAYP SAQTSLIVHA DGGKPGANLD EDSKTVHDLE ECATRSDVVY GFAEVKYKQL IPLAPSAATG YPGDPGSDAV DSADGGLTVD AIVTLSEEAL VLYVKALSLL AKSMDIARVW WTRKSRGDTL SRADTGSTVA GNRINNVVQW VRNRFNEVLE KAEFVRLKLV EAQKRLPSDH PSHPSNLSVG SSLGSGTSAD VVVSPDVTAE KLMYERALEM SRVAAINEIT GEDLAGCEIS YVTAIRMLEA ILDDVEVSRP GQSGGADRAD ARRDNEDGGQ NEPQAVILAK SANAWHSDIE NPESPGVAPE EAGAAVESVH APVQWTGQNA AVESGASLPC SGSHAAEIRT LTVRSMQDHA HFAPLLFSIF ISSYSSSISC PSSCGHC //