UniProt: V4NXB5

Database: UniProt
Entry: V4NXB5_EUTSA

LinkDB:  V4NXB5_EUTSA 
Original site:  V4NXB5_EUTSA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (15)   
   Pfam (5)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (34)   

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ID   V4NXB5_EUTSA            Unreviewed;      1086 AA.
AC   V4NXB5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   ORFNames=EUTSA_v10016166mg {ECO:0000313|EMBL:ESQ51531.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ51531.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ51531.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(2013).
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; KI517385; ESQ51530.1; -; Genomic_DNA.
DR   EMBL; KI517385; ESQ51531.1; -; Genomic_DNA.
DR   RefSeq; XP_006410077.1; XM_006410014.1.
DR   RefSeq; XP_006410078.1; XM_006410015.1.
DR   AlphaFoldDB; V4NXB5; -.
DR   STRING; 72664.V4NXB5; -.
DR   EnsemblPlants; ESQ51530; ESQ51530; EUTSA_v10016166mg.
DR   EnsemblPlants; ESQ51531; ESQ51531; EUTSA_v10016166mg.
DR   GeneID; 18026909; -.
DR   Gramene; ESQ51530; ESQ51530; EUTSA_v10016166mg.
DR   Gramene; ESQ51531; ESQ51531; EUTSA_v10016166mg.
DR   KEGG; eus:EUTSA_v10016166mg; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   OMA; GANLHAF; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000030689; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:EnsemblPlants.
DR   GO; GO:0051707; P:response to other organism; IEA:EnsemblPlants.
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:UP000030689};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          959..1081
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   REGION          38..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        662
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1086 AA;  120631 MW;  A3AB7D23890FE9BA CRC64;
     MLHKRASEAF VANENIDKSI SSDLASSPIK KRRIDITDST ASDKSSVVAS GSSSSSGFNG
     DSVDQHRDMA FGNSNRQEID EDLHSRQLAV YGRETMRRLF ASNVLISGMH GLGAEIAKNL
     ILAGVKSVTL HDESVVELWD LSSNFVFSED DIGKNRADAS VQKLQDLNNA VVVSSLTTSL
     TKELLSGFQV VVFSDISLDR AIEFNDYCHS HQPPIAFVRA DVRGLFGSVF CDFGPEFAVL
     DVDGEEPHTG IIASISNENQ AFISCVDDER LEFEDGDLVV FSEVEGMTEL NDGKPRKIKS
     ARPYSFTLEE DTSGYGTYVK GGIVTQVKQP KLLKFKPLRE ALKDPGDFLF SDFSKFDRPP
     LLHLAFQALD RFTSEAGRFP VAGSEADAQQ LISIATAINT GQGDLKVENV DHKLLRHFSF
     GAKAVLNPMA AMFGGIVGQE VVKACSGKFH PLFQFFYFDS VESLPSEPLD SSDVAPRNSR
     YDAQISVFGA KFQQKLEDAK VFTVGSGALG CEFLKNMALM GVSCGSQGKL TVTDDDIIEK
     SNLSRQFLFR DWNIGQAKST VAASAAAAIN PKFNIEALQN RVGAETENVF DDAFWENLTV
     VVNALDNVNA RLYVDSRCLY FQKPLLESGT LGAKCNTQMV IPHLTENYGA SRDPPEKQAP
     MCTVHSFPHN IDHCLTWARS EFEGLLEKTP AEVNAYLSSP VEYTNSMMTA GDAQARDTLE
     RIVECLEKEK CETFQDCLTW ARLRFEDYFV NRVKQLIYTF PEDAATSTGA PFWSAPKRFP
     RPLQYSSSDP SLLNFITSTA ILRAETFGIP VPEWTKNPKE AAEAVDRVIV PDFEPRKDAK
     IVTDEKATTL TTASVDDAAV INDLIAKLEQ CRHNLSPDFR MKPIQFEKDD DTNYHMDVIA
     GLANMRARNY SIPEVDKLKA KFIAGRIIPA IATSTAMATG LVCLELYKVL DGGHKVEDYR
     NTFANLALPL FSMAEPVPPK VVKHRDMAWT VWDRWVLRGN PTLREVLQWL EDKGLSAYSI
     SCGSCLLFNS MFPRHKERMD KKVVDLARDI AKVELPPYRR HLDVVVACED EDDNDVDIPL
     VSIYFR
//

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