ID A0A1S3ZGD7_TOBAC Unreviewed; 1080 AA.
AC A0A1S3ZGD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=LOC107786522 {ECO:0000313|RefSeq:XP_016463525.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016463525.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016463525.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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_016463525.1; XM_016608039.1.
DR AlphaFoldDB; A0A1S3ZGD7; -.
DR SMR; A0A1S3ZGD7; -.
DR STRING; 4097.A0A1S3ZGD7; -.
DR PaxDb; 4097-A0A1S3ZGD7; -.
DR GeneID; 107786522; -.
DR OMA; ERMDRKM; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000084051; Unplaced.
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:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 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:UP000084051};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 953..1075
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 656
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1080 AA; 120185 MW; 575F0A53B8D33B89 CRC64;
MLPVKRTVEV GGENDDVSVD PLTKKHKATA AASGDSSTVT MGGTGSATTG DVNTNGNATN
GKSPIDARNS PDIDEDLHSR QLAVYGRETM RRLFASNVLV SGLQGLGAEI AKNLILAGVK
SVTLHDEGNV ELWDLSSNFI FTEEDVGKNR ALASIQKLQE LNNAVIISTL TDALTKEQLS
NFQAVVFTDI SLEKAVEFDD YCHKHQPPIA FIKAEVRGLF GSVFCDFGPE FTVADVDGED
PHTGIIASIS NDNPALVGCI DDERLEFQDG DLVIFSEVRG MTELNDGKPR KIKNARPYSF
TIEEDTSNYA AYERGGIVTQ VKEPKVLKFK PLREAIKDPG DFLLSDFSKF DRPPILHLAF
QALDRFVSES GRFPLAGSEE DAQRLISFVT DLNNSLSDGK LEEIDQKLLR NFAFGARAVL
NPMAAMFGGI VGQEVVKACS GKFHPLYQFF YFDSVESLPT APLDPNDLKP LNSRYDAQIS
VFGNKLQKKL EEAKAFVVGS GALGCEFLKN LALMGVCCGD KGKLTITDDD VIEKSNLSRQ
FLFRDWNIGQ AKSTVAAAAA SLINPRIHIE ALQNRASPET ESVFDDTFWE NLSVVINALD
NVNARLYIDQ RCLYFQKPLL ESGTLGAKCN TQMVISHLTE NYGASRDPPE KQAPMCTVHS
FPHNIDHCLT WARSEFEGLL EKTPTEVNAY LINPSDYISA MQKAGDAQAR DTLDRVLECL
DKERCDTFQD CITWARLRFE DYFADRVKQL TFTFPEEATT SSGAPFWSAP KRFPRPLQFS
VDDASHLQFL LAASILRAET FGILIPDWVK SPQKLAEAVD KVIVPDFQPK KDVKIVTDEK
ATSMAASSID DAAVINELVM KLETCRQELP SGYKMNPIQF EKDDDTNYHM DLIAGLANMR
ARNYSIPEVD KLKAKFIAGR IIPAIATSTA MATGLVCLEL YKVLDGGHKV EDYRNTFANL
ALPLFSMAEP VPPKVVKHQD MNWTVWDRWI LKDNPTLREL LQWLQNKGLN AYSISYGSCL
LYNSMFPKHK ERMDRKLVDL AREVAKADLP PYRKHFDVVV ACEDEEDNDV DIPQMSIYFR
//
