ID A0A445LSL7_GLYSO Unreviewed; 1092 AA.
AC A0A445LSL7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=D0Y65_004808 {ECO:0000313|EMBL:RZC26319.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZC26319.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZC26319.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC26319.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) 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:RZC26319.1}.
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DR EMBL; QZWG01000002; RZC26318.1; -; Genomic_DNA.
DR EMBL; QZWG01000002; RZC26319.1; -; Genomic_DNA.
DR EMBL; QZWG01000002; RZC26321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445LSL7; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000289340; Chromosome 2.
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 Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 965..1087
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 668
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1092 AA; 120641 MW; FCE35D8988ED67BD CRC64;
MLPRKRASEG GVVVEGDTDP TNSSNSGAAS FSKKARIGSL AACSGAGAAE SAVNVSGQGF
GSGSGDDSVG NSVGGMALGN SQPAEIDEDL HSRQLAVYGR ETMRRLFASS ILVSGMQGLG
VEIAKNLILA GVKSVTLHDE GNVELWDLSS NFVFSENDVG KNRAEASVGK LQELNNAVVV
LTLTTKMTKE QLSNFQAVVF TEVSLEKAVE FNDYCHSHQP PIAFIKSEVR GLFGSLFCDF
GPEFTVVDVD GEDPHTGIIA SISNDNPALV SCVDDERLEF QDGDLVVFSE VHGMEELNDG
KPRKIKNARA YSFTLEEDTT NYGRYEKGGI VTQVKQPKVL NFKPLREALS DPGDFLLSDF
SKFDRPPLLH LAFQALDKFV SEIDRFPVAG SEDDAQKLIS IASNINGSLG DGRLEDVNPK
LLQQFAFGAR AVLNPMAAMF GGIVGQEVVK ACSGKFHPLF QFLYFDSVES LPTEPLDPND
LKPLNSRYDA QISVFGQKLQ KKLEDAEVFV VGSGALGCEF LKNLALMGVS CGQGKLTITD
DDVIEKSNLS RQFLFRDWNI GQAKSTVAAS AAASINPRLN IEALQNRVGP ETENVFHDTF
WENLSVVINA LDNVNARLYV DQRCLYFQKP LLESGTLGAK CNTQMVIPHL TENYGASRDP
PEKQAPMCTV HSFPHNIDHC LTWARSEFEG LLEKTPAEVN AYLSNPNEYT NAMRNAGDAQ
ARDNLERVLE CLDKEKCETF EDCITWARLK FEDYFANRVK QLIYTFPEDA ATSTGAPFWS
APKRFPHPLQ FSSSDLGHLQ FLMAASILRA ETFGIPIPDW VKNPKKLAEA VDRVIVPDFQ
PKKDAKIVTD EKATSLSSAS IDDAAVINDL ILKLEGCRTK LLPEFRMKPV QFEKDDDTNY
HMDLIAGLAN MRARNYSIPE VDKLKAKFIA GRIIPAIATS TAMATGLVCL ELYKALDGGH
KVEDYRNTFA NLALPLFSMA EPVPPKVIKH QDMSWTVWDR WILKDNPTLR ELLEWLKSKG
LNAYSISCGS CLLYNSMFPR HRERMDKKMV DLAREVAKVE IPSYRRHLDV VVACEDDDDN
DIDIPQISIY FR
//
