ID K3ZH11_SETIT Unreviewed; 1053 AA.
AC K3ZH11;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=101778880 {ECO:0000313|EnsemblPlants:KQK93439};
GN ORFNames=SETIT_8G019500v2 {ECO:0000313|EMBL:RCV36910.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK93439, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EMBL:RCV36910.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK93439,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV36910.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV36910.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV36910.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK93439}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK93439};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; AGNK02004608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003535; RCV36910.1; -; Genomic_DNA.
DR RefSeq; XP_004978585.1; XM_004978528.3.
DR AlphaFoldDB; K3ZH11; -.
DR STRING; 4555.K3ZH11; -.
DR EnsemblPlants; KQK93439; KQK93439; SETIT_025863mg.
DR GeneID; 101778880; -.
DR Gramene; KQK93439; KQK93439; SETIT_025863mg.
DR KEGG; sita:101778880; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; K3ZH11; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000004995; Chromosome VIII.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IBA:GO_Central.
DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF215; UBIQUITIN-ACTIVATING ENZYME E1 1; 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:UP000004995};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 926..1048
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 629
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1053 AA; 117150 MW; 0182C4A5A0B0D5B6 CRC64;
MLPRKRGVDA GEVQDLHNKA PRPASPSPDQ DKEELLGEMA ARAPEIDEDL HSRQLAVYGR
ETMKRLFGSN VLVSGLQGLG AEIAKNLVLA GVKSVTLHDD GKVDLWDLSS NFFLSEKDVG
QNRAQACVPK LQELNNAVII STITGDLTKE QLSNFQAVVF TDISIEKAVE FDDYCHSHQP
PIAFIKSEVR GLFGSVFCDF GPEFTVLDVD GEEPHTGIVA SISNDNPALV SCVDDERLEF
QDGDLVVFSE VHGMTELNDG KPRKIKSARP YSFTLEEDTT SYGTYIRGGI VTQVKPPKVL
KFKTLKEAIK EPGEFLMSDF SKFDRPPLLH LAFQALDKFR AELLRFPIAG SADDAKKLID
FAMSINESLG DSKLEEIDKK LLQHFASGSR AVLNPMAAMF GGIVGQEVVK ACSGKFHPLY
QFFYFDSVES LPVEPLEPSD LKPENSRYDA QISVFGAKLQ KKLEQSKIFM VGSGALGCEF
LKNLALMGIS CSENGKLTVT DDDVIEKSNL SRQFLFRDWN IGQPKSTVAA TAAMAINPKL
HVEALQNRAS PETENVFNDA FWESLDAVVN ALDNVTARMY IDSRCVYFQK PLLESGTLGA
KCNTQMVIPH LTENYGASRD PPEKQAPMCT VHSFPHNIDH CLTWARSEFE GLLEKTPTEV
NAFLSNPSGY ATAARTAGDA QARDQLERVI ECLDRDKCET FQDCITWARL KFEDYFANRV
KQLTFTFPED AMTSSGAPFW SAPKRFPRPL EFSSADPSHL NFLLAASILR AETFGIPIPD
WAKNPKKLAE AVDKVIVPDF QPRQGVKIET DEKATSLSSA SVDDAAVIEE LIAKLESINK
TLPSGFHMNP IQFEKDDDTN FHMDLIAGFA NMRARNYSIP EVDKLKAKFI AGRIIPAIAT
STAMATGLVC LELYKVLAGG HKVEDYRNTF ANLAIPLFSM AEPVPPKTIK HQDMSWTVWD
RWTITGNITL RELLEWLKEK GLNAYSISCG TSLLYNSMFP RHKERLDKKV VDVAREVAKV
EVPSYRRHLD VVVACEDDDD NDVDIPLVSI YFR
//
