UBE13_WHEAT
ID UBE13_WHEAT Reviewed; 1053 AA.
AC P31252;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ubiquitin-activating enzyme E1 3;
DE EC=6.2.1.45 {ECO:0000269|PubMed:1634524};
GN Name=UBA3 {ECO:0000303|PubMed:1634524};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=1634524; DOI=10.1016/s0021-9258(18)42110-2;
RA Hatfield P.M., Vierstra R.D.;
RT "Multiple forms of ubiquitin-activating enzyme E1 from wheat.
RT Identification of an essential cysteine by in vitro mutagenesis.";
RL J. Biol. Chem. 267:14799-14803(1992).
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:0000269|PubMed:1634524}.
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:0000269|PubMed:1634524};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:1634524}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000305}.
CC -!- MISCELLANEOUS: There are multiple genes encoding E1 in wheat.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; M90664; AAA34266.1; -; mRNA.
DR PIR; T06483; T06483.
DR AlphaFoldDB; P31252; -.
DR SMR; P31252; -.
DR STRING; 4565.Traes_2AS_835DA0F8D.1; -.
DR PRIDE; P31252; -.
DR eggNOG; KOG2012; Eukaryota.
DR BioCyc; MetaCyc:MON-16754; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P31252; baseline.
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:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; 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 Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 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 PANTHER; PTHR10953; PTHR10953; 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_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..1053
FT /note="Ubiquitin-activating enzyme E1 3"
FT /id="PRO_0000194965"
FT REPEAT 59..197
FT /note="1-1"
FT REPEAT 456..608
FT /note="1-2"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..608
FT /note="2 approximate repeats"
FT ACT_SITE 629
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 573..574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
SQ SEQUENCE 1053 AA; 116481 MW; 99ABA3F0E85AF7EC CRC64;
MLPSKRPSDA AAGDENGRGG DARGPGSGRR RARAAAGAVT AAPQEIDEDL HSRQLAVYGR
ETMRRLFASD VLVSGLNGLG AEIAKNLALA GVKSVTIHDV KTVKMWDLSG NFFLSEDDIG
KNRAAACVAK LQELNNAVLI SALTEELTTE HLSKFQAVVF TDIDLDKAYE FDDYCHNHQP
PISFIKSEVC GLFGSVFCDF GPKFTVLDVD GEDPHTGIIA SISNDNPALI SCVDDERLEF
QDGDLVVFSE VHGMTELNDG KPRKVKNARP FSFSIEEDTS NFGIYVKGGI VTQVKEPKVL
CFKALRDAMT DPGEVLLSDF SKFERPPVLH LAFQALDKFK KDHGRCPAAG CEEDAHSFLK
IAAAINEASA DRKLDTIDEK LFRQFASGSR AVLNPMAAMF GGIVGQEVVK ACSGKFHPLN
QFFYFDSVES LPTYPLEPQD LKPSNNRYDA QVSVFGSKLQ KKMEEANTFV VGSGALGCEF
LKNLALMGVS CSSKGKLTIT DDDIIEKSNL SRQFLFRDWN IGQAKSTVAA TAASAINPSL
HIDALQNRAC PDTENVFHDT FWEGLDVVIN ALDNVNARMY MDMRCLYFQK PLLESGTLGA
KCNIQMVIPH LTENYGASRD PPEKQAPMCT VHSFPHNIDH CLTWARSEFE GLLEKTPNEV
NSFLSNPAQY AAAMRKAGDA QARELLERVS ECLNKDRCST FDDCISWARL KFEDYFSNRV
KQLTFTFPED AATSMGAPFW SAPKRFPRAL QFSAADQSHL NFIMSASILR AESFGVAIPE
WAKDTSKLAD VVNKIAVPTF EPKQGVNIVT DEKASNLSST SVDDVAVIED LLAKLQEYAK
MLLPGFQMKP IQFEKDDDTN FHMDLISGLA NMRARNYSIP EVDKLKAKFI AGRIIPAIAT
STAMATGLVC LELYKVIAGE HPVEDYRNTF ANLALPLFSM AEPVPPKVMK HKETSWTVWD
RWSVQGNLTL AELLQWFADK GLTAYSISCG TSLLYNNMFA RHKDRLTKKV VDIAREVAKV
DVPEYRRHLD IGVACEDEDE NDVDIPLVSV YFR