ID   ATG13_EMENI             Reviewed;         974 AA.
AC   Q5BBK4; C8VLQ3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=atg13; ORFNames=AN2076;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Activates the atg1 kinase in a nutritional condition
CC       dependent manner through the TOR pathway, leading to autophagy. Also
CC       involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC       in Cvt vesicle formation. Seems to play a role in the switching
CC       machinery regulating the conversion between the Cvt pathway and
CC       autophagy. Finally, atg13 is also required for glycogen storage during
CC       stationary phase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with atg1 to form the atg1-atg13 kinase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC       Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC   -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AACD01000032; EAA64908.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF86130.1; -; Genomic_DNA.
DR   RefSeq; XP_659680.1; XM_654588.1.
DR   AlphaFoldDB; Q5BBK4; -.
DR   SMR; Q5BBK4; -.
DR   STRING; 162425.CADANIAP00008746; -.
DR   EnsemblFungi; CBF86130; CBF86130; ANIA_02076.
DR   EnsemblFungi; EAA64908; EAA64908; AN2076.2.
DR   GeneID; 2874917; -.
DR   KEGG; ani:AN2076.2; -.
DR   VEuPathDB; FungiDB:AN2076; -.
DR   eggNOG; KOG4573; Eukaryota.
DR   HOGENOM; CLU_007151_0_0_1; -.
DR   InParanoid; Q5BBK4; -.
DR   OMA; MHQHPRS; -.
DR   OrthoDB; 1519629at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.900.10; -; 1.
DR   InterPro; IPR040182; ATG13.
DR   InterPro; IPR018731; Atg13_N.
DR   InterPro; IPR036570; HORMA_dom_sf.
DR   PANTHER; PTHR13430; PTHR13430; 1.
DR   Pfam; PF10033; ATG13; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..974
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000157969"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..963
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  103872 MW;  D923B5B94B8D00F2 CRC64;
     MHQQPRSPAP AASTSSARRS QDYDRRSDSP AFDLRTHTNR GLGIETENDT AEPEQSSQPG
     PEAISKVNQI VTNYHTKAAL IILHSRVELP PSYAKNSNVP RVNRWFNVEL EETDALKDQL
     KTWRTCDATD NRPPPMIIET YLDTAGLTNN QTLVALDDNG KRWDVTESLA ASQSSRPAKA
     SSSRAVDVIL ERWRVELGDM PGKLPSDLGA ILPTVYKKSI ILFRSLFTYS KFLPAWKFIK
     RNGRSRAHPA LRVKYRIFSG HARDLSKQDH LTMPLFEGDT KVVDTYSFGV TDSPAGPFSV
     QVTYRTCCDF RVDDSEALLS SQFMGADDEI FQPSLPSGGL DARVTPEVGS APLTRRTVED
     PDLSRAYGSL STFHHVGPTT GASPISALRA AREARASSPS PPTSSHRNSF AAARASPVGR
     AATLANDTNP NVARRPSISF QPFKAPPLSA SPSLVDPPLS ASPRTTGAGR TSLSDSRHMP
     PPSVTTSSRK PPSFGPDNAN SSPNSASPRP TPMSRYSSAF SHRRGRPSSG GINKLEDDNS
     SGRASATSSG AQPGSGLLAE ITGTSSDSIH ADDENISEFL KMLDLRKDLL SPSSQTAMDN
     HSRRMTAASA ALSRFRGMKD SNAALSDSMS SSLLMNRSSA TSSKQLSGVP GIAGTSISTA
     SSPGGKAISP HTPHTPAIPS RLSSNSIVDN TTTRLHGDNG SPVEEDASDE TTTERLPSTV
     TAIPIPTSPA TIFPSTFRRS SSAANRRSSH AIDDDEIFTM RSVSLGAEEP SHTTLGALQR
     QQDYEPIGTN IAPLESGARS SGGDDGNVLR GPTRRGPGAH RDASLSGPTV ATSPYSHHPL
     HQRRISHSRG RGFSGGPHSL SSGSSSIARG GLIHPYPAER EAERDANAGA SHSGTEDRRG
     TGRGSGGGRH NLPQAAQVEE DEPLLFAMSD FGASRRSFEE GRQGNHGPDS SGNTGSSRRG
     SGKRGTLSGF HLWP