ID   ATG1_ASPTN              Reviewed;         964 AA.
AC   Q0CLX3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 86.
DE   RecName: Full=Serine/threonine-protein kinase atg1 {ECO:0000250|UniProtKB:P53104};
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE   AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
GN   Name=atg1 {ECO:0000250|UniProtKB:P53104};
GN   ORFNames=ATEG_05311 {ECO:0000303|Ref.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to
CC       vacuole transport (Cvt) and found to be essential in autophagy, where
CC       it is required for the formation of autophagosomes. Involved in the
CC       clearance of protein aggregates which cannot be efficiently cleared by
CC       the proteasome. Required for selective autophagic degradation of the
CC       nucleus (nucleophagy) as well as for mitophagy which contributes to
CC       regulate mitochondrial quantity and quality by eliminating the
CC       mitochondria to a basal level to fulfill cellular energy requirements
CC       and preventing excess ROS production. Also involved in endoplasmic
CC       reticulum-specific autophagic process, in selective removal of ER-
CC       associated degradation (ERAD) substrates. Plays a key role in ATG9 and
CC       ATG23 cycling through the pre-autophagosomal structure and is necessary
CC       to promote ATG18 binding to ATG9 through phosphorylation of ATG9.
CC       Catalyzes phosphorylation of ATG4, decreasing the interaction between
CC       ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of
CC       ATG8. {ECO:0000250|UniProtKB:P53104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P53104};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P53104};
CC   -!- SUBUNIT: Homodimer. Forms a ternary complex with ATG13 and ATG17.
CC       {ECO:0000250|UniProtKB:P53104}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}.
CC       Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; CH476600; EAU34380.1; -; Genomic_DNA.
DR   RefSeq; XP_001214489.1; XM_001214489.1.
DR   AlphaFoldDB; Q0CLX3; -.
DR   SMR; Q0CLX3; -.
DR   STRING; 341663.Q0CLX3; -.
DR   EnsemblFungi; EAU34380; EAU34380; ATEG_05311.
DR   GeneID; 4320695; -.
DR   VEuPathDB; FungiDB:ATEG_05311; -.
DR   eggNOG; KOG0595; Eukaryota.
DR   HOGENOM; CLU_006447_0_0_1; -.
DR   OMA; INNVVQW; -.
DR   OrthoDB; 346907at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR   GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
DR   GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblFungi.
DR   GO; GO:0051365; P:cellular response to potassium ion starvation; IEA:EnsemblFungi.
DR   GO; GO:0000423; P:mitophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:TreeGrafter.
DR   GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR   CDD; cd14009; STKc_ATG1_ULK_like; 1.
DR   FunFam; 1.10.510.10:FF:000817; Serine/threonine-protein kinase ATG1; 1.
DR   FunFam; 3.30.200.20:FF:000399; Serine/threonine-protein kinase atg1; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR048941; ATG1-like_MIT2.
DR   InterPro; IPR022708; Atg1-like_tMIT.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   Pfam; PF12063; ATG1-like_MIT1; 1.
DR   Pfam; PF21127; ATG1-like_MIT2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transport.
FT   CHAIN           1..964
FT                   /note="Serine/threonine-protein kinase atg1"
FT                   /id="PRO_0000317790"
FT   DOMAIN          26..331
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..952
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         32..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   964 AA;  105333 MW;  E5834643C699499C CRC64;
     MASAHHSRRP RETSQTSQSE MSVGRYTRLG QIGKGSFATV YQGVHTKSRT YVAIKSVNLS
     QLNKKLKENL FSEIHILKGL YHPHIVALID CHETTSHIHL VMEYCALGDL SQFIRHRNTL
     GEHRYTRDMI AKYPNPRGGA LNEVVVRHFL KQLASALKFL RDRNLIHRDI KPQNLLLCPS
     PTSYRAGVAQ IVPFKGSEDS FSPATGLDSL PMLKIADFGF ARSLPATSLA ETLCGSPLYM
     APEILRYEKY DAKADLWSVG TVLYEMVVGK PPFRASNHVE LLRRIERGED NIKFPPENPA
     SDDIKALIRM LLKRNPVERM NFADFFESNV ITSPIPGLIP DDTGTLRRPS ADLDPLGQNS
     PAEPQPSPGA AAGSRREKDV SREDQITYPQ RTTAQTPRSG TPPSSVPMRR GGSADKAPST
     PKDTATTYPQ RPSTVSHATA PGRQELLDRN ATTAAMERQR NRHTFGPSQH ERPVDKAKEE
     QERAAQDVAF ERDYVVVEKR AVEVNAFADE LAHSPRIQGG FTRNAQTGAI SRRATVQGPQ
     TTATSPLASN TKAMQVFPGR SRADSTHARQ SSYERRYGQS PTSATSAISK ALNMASGRLF
     GMGFSPPMAI TKGGRSPPLA YNPFPAYPAA QPTLLPIGDG SKTNATLDED AKTVQVIEEC
     ATRSDVVYGF AEVKYKQLIP LAPSVPTDPS GRSSLPGGYR EPSDSTDGGL TVDAVVTLSE
     EALVLYVKAL SLLAKSMDIA SAWWNRKNRV DVFGDSTINR TDASMTVVGS RINNVVQWVR
     SRFNEVLEKA EFVRLKLIEG QKRLPPDHPS HPNNHSIGSS LGSGASVDVV VSPGVTAEKL
     MYDRALEMSR AAAINELTGE DLSGCEIAYV TAIRMLEAVL EEDEMPSTAG DKADRKDGEQ
     TMLDSVQAED RQVVVKLVSS IRGRLTALQK KLTVLAKRPT GSLGKTPSSN LTPVAHAVGA
     TPPR
//