ID A0A135TND5_9PEZI Unreviewed; 698 AA.
AC A0A135TND5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=CNYM01_05886 {ECO:0000313|EMBL:KXH49572.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH49572.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH49572.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH49572.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-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:KXH49572.1}.
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DR EMBL; JEMN01001069; KXH49572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TND5; -.
DR Proteomes; UP000070054; 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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 4..333
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 352..585
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 675..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 557
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ SEQUENCE 698 AA; 78301 MW; 5D23CFF95F132CD0 CRC64;
MAAIQYAPFS SEIELPFYAA LFSSKLEHDK LDDSARRVLG QYTALPVEPG QSCKMSILGN
ALTSDQPNDE HVRAEGFIKN VNTIEDFKNT DKQAMLKMAA RHVWDAINDG TIYSVPSLLS
SFTILSYADL KKYKFTYWFA FPALHSDPQW KRTGPIGRLD PKESTALVDR VGTWQANRDK
RQNGFFLAKK ARGVDVSDLD KDANSDLHDL NDTFGYVWEV ANLGEFENGF FDDVAEDDRY
VSFVDPSTYP ENPSWPLRNL LWLVRQRFRQ TKVQILCYRD IRSSRHAARS IILPLEMDPV
EPLAVAEMPK VTGWERDGEG KLRARIANLG EYMDPTRLAD QSVDLNLKLM KWRISPNLDL
DTIKSTKCLL LGAGTLGSYV SRNLMGWGVR KITFVDYGRV SYSNPVRQPL FEFEDCLEGG
KFKATRAADA LKRIYPGVES EGHVLSVPML GHPFTDEARS KADYDKLKQL IDEHDAIFLL
MDSRESRWLP SVLGKATGKI VLNAALGFDS FVVMRHGAEP TDVQPEDKER KTLGCYFCND
VVTPADSQKD QTLDQQCTVT RPGVAAIASA LLVELFASLL QHPLKQHAPA PQTSADEKDP
VDHALGLVPH TVRGYLHNFN NKVIRGESYP CCSACGPPIL EAYRNDGWGF VKKALLEKDF
VAELSGLAEV QREAERRAAS MDWEEEEDGA DDGDGELI
//
