ID   ATG7_NEUCR              Reviewed;         699 AA.
AC   Q871U2; Q1K6Y7; V5IMK4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=apg-5; Synonyms=atg7; ORFNames=100H1.190, NCU06672;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 apg-4/atg5 and apg-
CC       6/atg8 for its conjugation with phosphatidylethanolamine. Both systems
CC       are needed for the apg-6/atg8 association to Cvt vesicles and
CC       autophagosomes membranes. Autophagy is essential for maintenance of
CC       amino acid levels and protein synthesis under nitrogen starvation.
CC       Required for selective autophagic degradation of the nucleus
CC       (nucleophagy) as well as for mitophagy which contributes to regulate
CC       mitochondrial quantity and quality by eliminating the mitochondria to a
CC       basal level to fulfill cellular energy requirements and preventing
CC       excess ROS production. Plays a role in the regulation of filamentous
CC       growth and chronological longevity (By 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; BX294019; CAD70899.1; -; Genomic_DNA.
DR   EMBL; CM002240; ESA42585.1; -; Genomic_DNA.
DR   RefSeq; XP_011394689.1; XM_011396387.1.
DR   AlphaFoldDB; Q871U2; -.
DR   SMR; Q871U2; -.
DR   STRING; 5141.EFNCRP00000006657; -.
DR   EnsemblFungi; ESA42585; ESA42585; NCU06672.
DR   GeneID; 3877057; -.
DR   KEGG; ncr:NCU06672; -.
DR   VEuPathDB; FungiDB:NCU06672; -.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; Q871U2; -.
DR   OMA; VQTWRYS; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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..699
FT                   /note="Ubiquitin-like modifier-activating enzyme atg7"
FT                   /id="PRO_0000212818"
FT   REGION          680..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           370..375
FT                   /note="GXGXXG motif"
FT   COMPBIAS        683..699
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        550
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  78185 MW;  5F32AFB70C7702C9 CRC64;
     MDLKFATFSS EIELPFYSAL FSSKLDHDKL DSSARPVLGL YEPRSHASPE ASTRMQILGS
     ALTSDQDESG PLGMTRAEGY IKNVNTIEEF KNTDKNAMIK KAGEQIWDAI QDGTIYSCPS
     LLASFRILSY ADLKKYKFTY WFAFPALHSE PQWKRTGPIG RLTSDESTAL VERIGTWRYM
     VDRREHGFFL AKKVRREAAG PRSSLDDPGV DIGYRWDIGS LRDFETGFFN DAAEEDRYVA
     FVDPSNYPEY PSWPLRNLLI LIRQRYRLNK VQILCYRDTQ PRRHEARSTI LPLAMDQVGD
     VELKCMPKVT GWERNGNGDL RPRVANLAEY MDPTRLADQA VDLNLKLMKW RLAPNLDLDA
     IKNTKCLLLG AGTLGSYVSR NLLGWGVRKI TFIDYGSVSY SNPVRQPLFK FEDCHNGGKP
     KAIQAAEALK EIYPGVDVEG YALSVPMLDH AIHNEAKTKA DFDKLKELID SHDAIFLLMD
     TRESRWLPTL MGKAANKIVM NAALGFDTYV VMRHGAAPND GSEETLGCYF CNDVVVAADS
     MKDQTLDQQC TVTRPGVAAI ASALLVELLT SILQHPLKQH APAPVSTGTG SAVSYERDPP
     DHPLGLVPHQ VRGFLSNFQN MVIRGKSYPQ CSACSKPILD AYKEGGWEFV KTALASRDYV
     AELSGLAEVQ RLAEKAAAEM QWSEDEEGMD EEEGEGELI