ID   ATG1_ASPCL              Reviewed;         928 AA.
AC   A1CHL6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=ACLA_048410;
OS   Aspergillus clavatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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.
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DR   EMBL; DS027054; EAW10371.1; -; Genomic_DNA.
DR   RefSeq; XP_001271797.1; -.
DR   GeneID; 4704065; -.
DR   BRENDA; 2.7.11.1; 18580.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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_BS.
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    928       Serine/threonine-protein kinase atg1.
FT                                /FTId=PRO_0000317787.
FT   DOMAIN        6    315       Protein kinase.
FT   NP_BIND      12     20       ATP (By similarity).
FT   ACT_SITE    149    149       Proton acceptor (By similarity).
FT   BINDING      35     35       ATP (By similarity).
SQ   SEQUENCE   928 AA;  101306 MW;  F833AB1702209C5C CRC64;
     MSLGRYTRLD EIGRGSFATV YQGVHTKTGT YVAIKSVNLS KLNKKLKENL SSEIHILKGL
     YHPHIVALID CQETSSHIHL VMEYCALGDL SLFIKRRDTL GDHRYTRDMI AKYPNPPGGA
     LNEVVVRHFL KQLSSALKFL RDRNLIHRDI KPQNLLLCPS PSSYRSGAGS GAATVVPFKG
     CEDSFNPATG VDSLPLLKIA DFGFARSLPA TSLAETLCGS PLYMAPEILR YEKYDAKADL
     WSVGTVLYEM VVGKPPFRAT NHVELLRKIE KGEDRIKFPE DNPASDAIKA LIRALLKRNP
     VERLNFPEFF ENEVITGPIP GLLADDQPSI SRHRSVDPGT TEVPPRPDSR SGTSVPSGTR
     REREVNREDV YSPRSSPRNQ KPSTPPTSTP MRRVGSTDRP PSAPKESEPP MAYPQRPNAV
     SHATAPGRQE LLDRKATTTA IERQRSRNTY SEGSPRLDQP ADKLKEEQER AAQDVAFERD
     YVVVEKRAVE VNAFADELAH SPRIQGGLSR AAQAGAISRR ATVQGATPTL SSPQTTTGKA
     MQVFSGRSRA DSTHHRQASY ERRYGQSPTS ATSAISKALN MASGRLFGMG FSPPLTITKG
     GRSPPLAYNP FPAYPTAHGS LMIIGDGAKS QVALDEDTKT VQVIEECATR SDVVYGFAEV
     KYKQLIPLAP SIQTDPSAKS NMSGVRDTAG STDGDLTVDA TVTLSEEALV LYVKALSLLA
     KSMDIAGVWW TRKNRGETFG DPVMSRADTT GALVGTRINN VVQWVRNRFN EVLEKAEFVR
     LKLIEGQKRL PPDHPSHPSN HSVTSSLGAG STDIVVSSGV TAEKLMYDRA LEMSRAAAIN
     ELTGEDLAGC EIAYVTAIRM LEAVLEDDEV PGLGPGKVDT SKDMYDGVPA EDRQVVVKLV
     SSIRGRLQAL RKKLAILAKR APTASVNV
//