ID A0A2I4F2F7_JUGRE Unreviewed; 1018 AA.
AC A0A2I4F2F7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=LOC108994888 {ECO:0000313|RefSeq:XP_018825830.2};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018825830.2};
RN [1] {ECO:0000313|RefSeq:XP_018825830.2}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018825830.2};
RG RefSeq;
RL Submitted (SEP-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_018825830.2; XM_018970285.2.
DR AlphaFoldDB; A0A2I4F2F7; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000235220; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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:SF245; E1 UBIQUITIN-ACTIVATING ENZYME; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 891..1013
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 594
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1018 AA; 113856 MW; 3B560F273DEFEA8D CRC64;
MALGNGNSID IDEDLHSRQL AVYGRETMRR LFASNVLISG MQGLGAEIAK NLVLAGVKSV
TLHDKGAVEL WDLSGNFIFS EDDVGKNRAL ASVQKLQELN NSVVVSTLTT ELTKEQLSHF
QVVVFTDISL EKAIEFDDYC HNHQPPISFI KSEVRGLFGS TFCDFGPEFT VFDVDGKDPH
TGIIASISND NPALVTCVDD ERLEFQDGDL VVFSEVNGMT ELNDGKPRKI KNVRAYSFAI
EEDTAKYSAY VKGGIVTQVK QPKVLNFKPL REALKDPGDF LLSDFSKFDR PPLLHLAFQA
LDKFQSEFGH FPVAGSEDDA QKFISSVTSM NDALSDGRLE TIDQSLLCHF ASGARAVLNP
MAAMFGGIVG QEVVKACSGK FHPLFQFFYF ESVESLPAEP LLPSDLKPLN TRYDAQISVF
GSKIQKKLED AKIFVVGSGA LGCEFLKNLA LMGVSCGKQG KLTITDDDVI EKSNLSRQFL
FRDWNIGQAK STVAASAAAL INPSLNIDAL QNRASPETEN VFNDEFWENL SVVVNALDNV
NARLYIDQRC LYFQKPLLES GTLGAKCNTQ MVIPHLTENY GASRDPPEKQ APMCTVHSFP
HNIDHCLTWA RSEFEGLLEK TPAEVNTYLT NPNEYASAMK KAGDAQARDN LERVLECLDK
ERCETFQDCI NWARLKFEDY FANRVKQLTY TFPEDATTSN GAPFWSAPKR FPRPLQFSVD
DTTHLYFIMS GSVLRAETFG IPIPDWVKSP RKLADAANQV IVPDFQPKRG VKIVTDEKAS
SFSTSSIDDA AVIDELIMKL EERRKQLSPG FRMNSIQFEK DDDTNYHMDL IAGLANMRAR
NYGIPEVDKL KAKFIAGRII PAIATSTAMA TGLVCLELYK VLDGGHKLED YRNTFANLAL
PLFSIAEPVP PKVIKHKDMS WTVWDRWILK DNPTLRELLQ WLKNRGLNAY SISHGSCLIY
NSIFPKHKER MDKKLVDLVR NVAKAELPPY RQHFDVVVAC EDEDDKDVDI PQVSIYFR
//