ID   ATG7_CRYNJ              Reviewed;         675 AA.
AC   P0CM38; Q55NS2; Q5KC57;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE   AltName: Full=ATG12-activating enzyme E1 ATG7;
DE   AltName: Full=Autophagy-related protein 7;
GN   Name=ATG7; OrderedLocusNames=CNI00160;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC       systems required for cytoplasm to vacuole transport (Cvt) and
CC       autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for
CC       its conjugation with phosphatidylethanolamine. Both systems are needed
CC       for the ATG8 association to Cvt vesicles and autophagosomes membranes.
CC       Autophagy is essential for maintenance of amino acid levels and protein
CC       synthesis under nitrogen starvation. Required for selective autophagic
CC       degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC       contributes to regulate mitochondrial quantity and quality by
CC       eliminating the mitochondria to a basal level to fulfill cellular
CC       energy requirements and preventing excess ROS production. Plays a role
CC       in the regulation of filamentous growth and chronological longevity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC       structure {ECO:0000250}.
CC   -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC       through binding with ATP. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR   EMBL; AE017349; AAW45433.1; -; Genomic_DNA.
DR   RefSeq; XP_572740.1; XM_572740.1.
DR   AlphaFoldDB; P0CM38; -.
DR   SMR; P0CM38; -.
DR   STRING; 5207.AAW45433; -.
DR   PaxDb; P0CM38; -.
DR   EnsemblFungi; AAW45433; AAW45433; CNI00160.
DR   GeneID; 3259392; -.
DR   KEGG; cne:CNI00160; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; P0CM38; -.
DR   OMA; GKMGPNI; -.
DR   OrthoDB; 549762at2759; -.
DR   Proteomes; UP000002149; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IEA:EnsemblFungi.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0019778; F:Atg12 activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0019779; F:Atg8 activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.140.100; -; 1.
DR   Gene3D; 3.40.140.70; -; 1.
DR   InterPro; IPR006285; Atg7.
DR   InterPro; IPR032197; Atg7_N.
DR   InterPro; IPR042522; Atg7_N_1.
DR   InterPro; IPR042523; Atg7_N_2.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF16420; ATG7_N; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..675
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000212813"
FT   REGION          268..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           346..351
FT                   /note="GXGXXG motif"
FT   ACT_SITE        538
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   675 AA;  73527 MW;  03592634460F9246 CRC64;
     MAPLQFQPLA SQPTPAFWAA LAAHKLNHLK LDDSHLPITA QIEPAKRVLI NKERVDDTAD
     VGIDGSLVVG GDAFEAERGR LPPNAVSVTG TLKIFNTIEE FKDTSAKKRL FDDLVSQMLE
     SFDTDRPVLN PFLLVTFADL KKYVYHYWFA FPALVSSPAW VMDGEFMPVD EIEDIRKLAQ
     SHFQHNTTAF LLKGAAPHLS AAPLSSCSTF YDKTQSEMVT VVFHDTSSLP SNPGWGLRNV
     LYYLSAKHGI TSLVVICLRE GSSSTQASLS LSSPPSTAPA KPPQAVGWER HPSGKLSPRV
     ADLGPMMDPT RLAAQAVDLN LKLIKWRLLP ALDLDKISGT RCLLLGAGTL GCYVARILMG
     WGVRNITLVD SSTVSYSNPV RQPLFTFSDC LNGGLPKAPT AAKKLQEIFP GVNAQGVVLG
     IPMPGHPISS SDDAVEKDVA KLEALVKSHD AVFLLMDSRE SRWLPTVLGR KWGKVVVNAA
     LGFDSFLVMR HGAGAGAGAR RIQSDEGGVG EKGLGCYYCN DIVAPTDSLS DRTLDQMCTV
     TRPGVAPIAA AMAVELLISV LQHPLGVHAP AERPDTAETS TSTKTSPLGC VPHQLRGQMY
     QWKTQIVEGE AFDRCTGCSD YVLNEYETNG FAFLRRVFNE KDYLEKVTGL DELYRESEKV
     IEGMEGLDWD SEGEE