ID A0A6G1FGQ9_9ORYZ Unreviewed; 1062 AA.
AC A0A6G1FGQ9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=E2562_037453 {ECO:0000313|EMBL:KAF0935972.1};
OS Oryza meyeriana var. granulata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza meyeriana.
OX NCBI_TaxID=110450 {ECO:0000313|EMBL:KAF0935972.1, ECO:0000313|Proteomes:UP000479710};
RN [1] {ECO:0000313|EMBL:KAF0935972.1, ECO:0000313|Proteomes:UP000479710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Menghai {ECO:0000313|Proteomes:UP000479710};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF0935972.1};
RA Li W.;
RT "Whole genome sequence of Oryza granulata.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP. {ECO:0000256|ARBA:ARBA00002457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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:KAF0935972.1}.
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DR EMBL; SPHZ02000001; KAF0935972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1FGQ9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000479710; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR CDD; cd01491; Ube1_repeat1; 1.
DR CDD; cd01490; Ube1_repeat2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000479710};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 935..1057
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 638
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1062 AA; 117212 MW; C5058F5B52CC35AC CRC64;
MLPTKRADGA EGGSDAAAKK ARVGGSASKA EAMVAGEAGG GGGGVSGNGN EAAEIDEDLH
SRQLAVYGRE TMRRLFASNV LVSGLNGLGA EIAKNLALAG VKSVTLHDVE NVEMWDLSGN
FFLSEDDIGK NRAVACIAKL QELNNAVLIS VLTEDLTNEH LSKFQAVVFT DISLDKAFEF
DDYCCNHQPS ISFIKAEVCG LFGSVFCDFG PKFTVLDVDG EEPHTGIISS ISNDNPAMVS
CVDDERLEFQ DGDLVVFSEV QGMTELNDGK PRKIINARPY SFCIQEDTSN FGIYAKGGIV
TQVKEPIILE FKSLRDSIRE PGNFLLSDFS KFDRPPLLHF AFLALDKFRK EFGRFPGAGC
DQDAQRFIEF VASVNEATID YKMDELDGKL LRIFASGSRA VLNPMAAMFG GIVGQEVVKA
CSGKFHPQYQ FFYFDSVESL PTYPLDSKDL KPLNSRYDAQ ISVFGSKLQK KLRDANVFVV
GSGALGCEFL KNFALMGVSC GLKGKLTITD DDIIEKSNLS RQFLFRDWNI GQAKSTIAAA
AASAINSSLH INALQNRACP ETEHVFHDAF WEGLDVVINA LDNVNARMYM DMRCLYFQKP
LLESGTLGPK CNTQMVIPHL TENYGASRDP PEKQAPMCTV HSFPHNIDHC LTWARSEFEG
LLEKTPNEVN SFISNPAQYA AAMRKAGDAQ ARELLERVCE CLDKERCDGF EDCITWARLK
FEDYFSNRVK QLTFTFPEDA VTSTGAFFWS APKRFPRPLQ FSTVDSSHIH FILAASILRA
MSFGISIPDW AKNTSNLVDA ISKVVVPEFE LKSGIKIETD EKASNISSAS VDDAAVIEDL
LTKLEACAKK LPPGFLMKPI QFEKDDDANF HMDLIAGLAN MRARNYGIQE VDKLKAKFIA
GRIIPAIATS TAMATGLVCL ELYKVLAGGH PVEDYRNSFA NLAIPMFSMA EPLPPKVIKH
QDMRWTVWDR WSIEGNITVA ELLKWLSDKG LSAYSVSCGT SLLYNTMFPR HKDRVNKKIV
DVAKEVAKVD VPAYRRHLDV VVACEDDDGN DIDIPLISIY FR
//
