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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
 
 
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