ID A0A5N5G161_9ROSA Unreviewed; 1132 AA.
AC A0A5N5G161;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=D8674_006849 {ECO:0000313|EMBL:KAB2607132.1};
OS Pyrus ussuriensis x Pyrus communis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=2448454 {ECO:0000313|EMBL:KAB2607132.1, ECO:0000313|Proteomes:UP000327157};
RN [1] {ECO:0000313|EMBL:KAB2607132.1, ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 {ECO:0000313|EMBL:KAB2607132.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB2607132.1};
RA Ou C.;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT "A de novo genome assembly of a pear dwarfing rootstock.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAB2607132.1, ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 {ECO:0000313|EMBL:KAB2607132.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB2607132.1};
RA Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT "A de novo genome assembly of a pear dwarfing rootstock.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB2607132.1}.
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DR EMBL; SMOL01000559; KAB2607132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5G161; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000327157; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000327157};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1132
FT /note="E1 ubiquitin-activating enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024448208"
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1005..1127
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 721
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1132 AA; 125751 MW; 4416905FF7B1B0CE CRC64;
MPKLRFLIVA SAAPILLGLA LRTYSGADDA ANSIFTTRFL VWSLLVSVMV TFSGVFSRLL
HCMLPKKRPG DGVVVEVEVG GDAGSSVALS SINKHRVGNF VAESTVSNNS SLASSNHGSV
VEKDVPIMAL GHSNQSDIDE DLHSRQLAVY GRETMRRLFA SNVLISGIQG LGAEIAKNLI
LAGVKSVTLH DEGNVELWDL SSNFVFSEDD VGKNRSLASV QKLQELNNAV VVNTLTTELT
KEQLSNFQVV VFTDISLEKA IEFDDYTHDH QPPIAFIKTE ARGLFGSVFC DFGPEFTVFD
VDGEEPHTGI IASISNDNPA IVSCVDDERL EFQDGDLVVF SEVHGMTELN DGKPRRIKNA
RAYSFTLEED TTRFGAYEKG GIVTQMKQPK VLKFKPLRGA LNDPGEFLPS DFSKFDRPPL
LHLAFQALDK VVSELGRFPV AGSEEDAQKL ISIASNINEN LGDGKMEDIN PKLLRHFAFG
AKAVLNPMAA MFGGIVGQEV VKACSGKFHP LFQFFYFDSV ESLPTEPLES SDLKPLNSRY
DAQISVFGSK LQKKLEDAKI FLVGSGALGC EFLKNLALMG VSCGKQGKLT VTDDDVIEKS
NLSRQFLFRD WNIGQPKSTA AASAAASINP YLNVEALQNR VSSETEDVFD DAFWENLSVV
INALDNVNAR LYVDQRCLYF QKPLLESGTL GTKCNTQMVI PLLTENYGAS RDPPEKQAPM
CTLHSFPHNI DHCLTWARSE FEGLLGKTPA EVNAYLAKPS EYAASKRNAG DAQARDTLER
ILECLDRERC ETFQDCIAWA RLKFEDYFYN RIKQLIYTFP EDATTSSGTP FWSAPKRFPH
PLQFSTADPG HLNFVMAASI LRAETFGIPI PHWVRNSKKF AEAVEKVMVP EFQPRRDANI
VTDDNATNLT SQSTDDAQVI DDLIIKMKPI QFEKDDDTNY HMDLIAGLAN MRARNYGIPE
VDKLKAKFIA GKIIPAIATT TAMVTGLVCL ELYKVLDGGH KLEDYRNTFA NLALPLFAMA
EPVPVKVIKH RNMSWTIWDR WIVRGNPTLR EFIQWLKDRG LDAYSISYAS SLLYNTMFAR
HQDRMDKKMV DLAREVGGLE LSPNRSHFDV VVACEDDEGN EVDIPLVSIY FR
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