UniProt: A0A3Q7GMH0

Database: UniProt
Entry: A0A3Q7GMH0_SOLLC

LinkDB:  A0A3Q7GMH0_SOLLC 
Original site:  A0A3Q7GMH0_SOLLC

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (23)   
   InterPro (15)   
   Pfam (5)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (36)   

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ID   A0A3Q7GMH0_SOLLC        Unreviewed;      1091 AA.
AC   A0A3Q7GMH0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc06g007320.3.1};
RN   [1] {ECO:0000313|EnsemblPlants:Solyc06g007320.3.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc06g007320.3.1};
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [2] {ECO:0000313|EnsemblPlants:Solyc06g007320.3.1}
RP   IDENTIFICATION.
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc06g007320.3.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2019) 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   RefSeq; XP_004240416.1; XM_004240368.3.
DR   RefSeq; XP_010321768.1; XM_010323466.2.
DR   AlphaFoldDB; A0A3Q7GMH0; -.
DR   STRING; 4081.A0A3Q7GMH0; -.
DR   PaxDb; 4081-Solyc06g007320-2-1; -.
DR   EnsemblPlants; Solyc06g007320.3.1; Solyc06g007320.3.1; Solyc06g007320.3.
DR   GeneID; 101245462; -.
DR   Gramene; Solyc06g007320.3.1; Solyc06g007320.3.1; Solyc06g007320.3.
DR   KEGG; sly:101245462; -.
DR   InParanoid; A0A3Q7GMH0; -.
DR   OMA; GANLHAF; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000004994; Chromosome 6.
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:UP000004994};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          964..1086
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        666
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1091 AA;  121563 MW;  A36B8FF207C4D759 CRC64;
     MLPRKRPAEG VVVEGNSSSC DPESSLKKHK ISCVISSGTE ENTSGCSSNK VVSNNTNGNT
     SSGSVGERSV TEMAFDDGNP HDIDEDLHSR QLAVYGRETM RRLFASNVLV SGIQGLGAEI
     AKNLILAGVK SVTLHDEGEV QLWDLSSNFI FSESDVGMNR ALASVQKLQE LNNAVVVSSF
     TTKLTKEKLS DFQAVVFTNT SLEDALEFND YCHNHQPPIA FIRTEVRGLF GYVFCDFGPE
     FTVFDVDGEE PHTGIIASIS NDNPALISCV DDERLEFQDG DLVVFSEVQG MTELNDGKPR
     KISSARPYSF TLDEDTTNFG PYVRGGIVTQ VKPPKILNFK TLRESIMDPG DFLLSDFSKF
     DRPPLLHLAF QALDKFRSDL ARFPLAGSED DAQTLISIAT NLNESNGNVK LDDINPKLLQ
     KFSYGARAEL NPMAAMFGGI VGQEVVKACS GKFHPLYQFF YFDSLESLPT EPLDPSDLKP
     LNTRYDAQIS VFGKKFQKKL EDAKVFMVGS GALGCEFLKN LALMGVACTE QGKLTVTDDD
     VIEKSNLSRQ FLFRDWNIGQ AKSTVAAAAA TSINPQLRVE ALQNRVGPET ENVFDDTFWE
     NLSVVINALD NVNARLYVDQ RCLYFQKPLL ESGTLGAKCN TQMVIPHLTE NYGASRDPPE
     KQAPMCTLHS FPHNIDHCLT WARSEFEGLL EKTPAEVNAY LSNPNEYTSA QTNAGDAQAR
     DNLERILECL DRESCETFED CIAWARLKFE EYFANRVKQL IFTFPEDAVT SSGAPFWSAP
     KRFPRPLQFS STDPSHLHFI MAASILRAET FGIPIPDWVK HPQKLSEAVH KVMVPCFQPR
     KDAKIVTDEK ATSLSSSASI DDAAVIDELI SKLECGRKNL PPGFRMKPIQ FEKDDDTNFH
     MDLIAALANM RARNYCIPEV DKLKAKFIAG RIIPAIATTT AMATGLVCLE LYKVLDGSHK
     LEDYRNTFAN LALPLFSIAE PVPPKIIKHN DLSWTVWDRW VIKDNPTLRE LIQWLADKGL
     NAYSISCGSC LLFNSMFPRH KERMDQKVVD LARDVAKMEI PPYRRHLDVV VACDDDNDED
     VDIPLVSVYF R
//

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