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ATG7_CRYNB
ID   ATG7_CRYNB              Reviewed;         673 AA.
AC   P0CM39; Q55NS2; Q5KC57;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
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=CNBH0170;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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; AAEY01000040; EAL19445.1; -; Genomic_DNA.
DR   RefSeq; XP_774092.1; XM_768999.1.
DR   AlphaFoldDB; P0CM39; -.
DR   SMR; P0CM39; -.
DR   EnsemblFungi; EAL19445; EAL19445; CNBH0170.
DR   GeneID; 4937519; -.
DR   KEGG; cnb:CNBH0170; -.
DR   VEuPathDB; FungiDB:CNBH0170; -.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   Proteomes; UP000001435; Chromosome 8.
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:0019778; F:Atg12 activating enzyme activity; IEA:EnsemblFungi.
DR   GO; GO:0019779; F:Atg8 activating enzyme activity; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IEA:EnsemblFungi.
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; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..673
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000410021"
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        536
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   673 AA;  73352 MW;  81DA4A55A6D33334 CRC64;
     MAPLQFQPLA SQPTPAFWAA LAAHKLNHLK LDDSHLPITA QIEPAKRVLI NKERVDDTAD
     VGIDGSLVVG GDAFEAERGR LPPNAVSVTG TLKIFNTIEE FKDTSAKKRL FDDLVSQMLE
     SFDTDRPVLN PFLLVTFADL KKYVYHYWFA FPALVSSPAW VMDGEFMPVD EIEDIRNLAQ
     SHFQHNTAAF LLKGAAPHLS AAPLSSCSTF YDKTQSEMVT VVFHDTSSLP SNPGWGLRNV
     LYYLSAKHGI TSLVVICLRG GSSSTQASLS LSSPPSTAPA KPPQAVGWER HPSGKLSPRV
     ADLGPMMDPT RLAAQAVDLN LKLIKWRLLP ALDLDKISGT RCLLLGAGTL GCYVARILMG
     WGVRNITLVD SSTVSYSNPV RQPLFTFSDC LNGGLPKAPT AAKKLQEIFP GVNAQGVVLG
     IPMPGHPISS SDDAVEKDVA KLEALVKSHD AVFLLMDSRE SRWLPTVLGR KWGKVVVNAA
     LGFDSFLVMR HGAGAGARRI QWDEGGVGEK GLGCYYCNDI VAPADSLSDR TLDQMCTVTR
     PGVAPIAAAM AVELLISVLQ HPLGVHAPAE RPDTAETSTS TKTSPLGCVP HQLRGQMYQW
     KTQIVEGEAF DRCTGCSDYV LNEYETNGFA FLRRVFNEKD YLEKVTGLDE LYRESEKVIE
     GMEGLDWDSE GEE
 
 
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