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Database: UniProt
Entry: A0A2I4F2F7_JUGRE
LinkDB: A0A2I4F2F7_JUGRE
Original site: A0A2I4F2F7_JUGRE 
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
//
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