ID A0A094HGG3_9PEZI Unreviewed; 710 AA.
AC A0A094HGG3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7 {ECO:0000256|ARBA:ARBA00017647, ECO:0000256|RuleBase:RU366022};
DE AltName: Full=Autophagy-related protein 7 {ECO:0000256|RuleBase:RU366022};
GN ORFNames=V501_06537 {ECO:0000313|EMBL:KFZ07351.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ07351.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ07351.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU366022}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU366022}.
CC Preautophagosomal structure {ECO:0000256|RuleBase:RU366022}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000256|ARBA:ARBA00010931,
CC ECO:0000256|RuleBase:RU366022}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ07351.1}.
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DR EMBL; JPKD01001996; KFZ07351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HGG3; -.
DR STRING; 1420914.A0A094HGG3; -.
DR HOGENOM; CLU_012998_2_1_1; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR CDD; cd01486; Apg7; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1.
DR Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 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 NCBIfam; TIGR01381; E1_like_apg7; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU366022};
KW Cytoplasm {ECO:0000256|RuleBase:RU366022};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU366022};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 3..342
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 361..587
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 193..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..710
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 561
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ SEQUENCE 710 AA; 78048 MW; 04D258A89AEDEBB5 CRC64;
MALQYAPFQS EIELPFYSAL ANLKIDHDRL DVSARQVLGL YGAPINLTSR TNCQMQILGN
ALSSSSVPAG LVRAEGIIRN VNTIEEFKNA DKNAIINTAG KQIWDAIQDG TIYSLPSLLS
SFTILSFADL KKYRFTTWSG FPALHSDPVW TQSAPIDRLD GRETTALVDE VGTWRYSVDP
REHGFFLAKK VYNSDKPKPD EEGETKPDER TSIDDDIGYN WKIGSLHAFE TGFFRDVDAK
DQFIAFADPS TYPQNPGWML RNLLVLVRQR YKLDNVRILC FRDVQSKRHE ARSIILNLSS
TSSAVKDETA PPAVAKMPKV TGWERNSHGK LSSRLTDLSQ YMDPRLLADQ SVDLNLKLMK
WRIAPNLNLT KISQTKCLLI GAGTLGSYVS RNLLGWGVRK ITFVDNGTVS FSNPVRQPLF
TYQDCLGGGG KKAELAAKAL QDIYPGVDST GHVISVPMLG HPVTDEAKAK RDFETLKKLI
DEHDAIFLLM DTRESRWLPT LMGKATGKIV MNAALGFDTY VVMRHGMTPP DGAQAALGCY
FCNDVVAPAD SVKDQTLDQQ CTVTRPGIAA IASAQLVELL ASILQHPLGG LAPAPKPVQP
SGSGPVTYER DPPEHPLGIV PHQIRGFLAS WQNMLISGQS YDCCSACSSK VVDAYEKDGW
DFVKKALAER DYITELSGLA EVQRAAEAAG GDIDWDSEGG GEEEGEGELL
//
