ID A0A0E0EGH2_9ORYZ Unreviewed; 911 AA.
AC A0A0E0EGH2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI07G23800.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI07G23800.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI07G23800.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI07G23800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0E0EGH2; -.
DR STRING; 40149.A0A0E0EGH2; -.
DR EnsemblPlants; OMERI07G23800.1; OMERI07G23800.1; OMERI07G23800.
DR Gramene; OMERI07G23800.1; OMERI07G23800.1; OMERI07G23800.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008021; Chromosome 7.
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; 2.
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; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
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; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF226; UBIQUITIN-ACTIVATING ENZYME E1 3; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021}.
FT DOMAIN 784..906
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 17..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100816 MW; 8D16B1C7C028420A CRC64;
MRCLRFLRRG LLSMLPTTNK RAAGPDDDDA RATDPKRPKV AAQNGSTNGV VVPEIDEDLH
SRQLAVYGRE TMRRLFASHV LVSGLNGLGA EIAKNLALAG VKSVTLHDVK NVEMWDLSAN
FFLSENDIGK NRAAACVSKL QELNNAVIIS ALTEELTTDH LSKFQAVVFT DIGLDKAYEF
DDCCHNHCPP ISFIKAEVCG LFGTVFCDFG PEFTVLDVDG EDPHTGIIAS ISNDNPAMVS
CVDDERLEFQ DGDFVVFSEV HGMSELNDGK PRKVKEPKIL RFKSLRDAMR DPGDFLLSDF
SKFERSPVLH LAFQALDKFK KEYGRNPAPG CEQDAQSFLK CAADINEDLT DHKLDTIDEK
LFRHFASGSQ AVLNPMAAMF GGIVGQEVVK ACSGKFHPLY QKKLEEANTF VVGSGALGCE
FLKNLALMGV SCSPKGKLTI TDDDVIEKSN LSRQFLFRDW NIGQAKSTVA AAAASAINPN
LCIDALQNRA CPDTENVFHD TFWEGLDVVV NALDNVNARM YMDMRCLYFQ KALLESGTLG
AKCNTQMVIP HLTENYGASR DPPEKQAPIF EDYFSNRVKQ LTFTFPEDAA TSTGAPFWSA
PKRFPRPLQF SVADPSHIHF IVSASILRAE SFGIAIPDWA KNTSRLADAV SEVAVPQFEP
KKGVSIVTDE KATSLSSASV DDASVIDDLL AKLEECAKRL PPGFQMKPIQ FEKDDDTNFH
MDLISGFANM RARNYSIPEV DKLKAKFIAG RIIPAIATST AMATGLVCLE LYKVIAGEHP
IEDYRNTFAN LALPLFSMAE PVPPKVIKHQ DMSWTVWDRW SIKGNLTVAE LLQWFSDKGL
TAYSISCGTS LLYNNMFARH KERLNKKVVD VAREVAKVHV PEYRKHLDLV AACEDDDGND
IDIPLVSVYF R
//
