ID A0A2G5D1Y2_AQUCA Unreviewed; 1065 AA.
AC A0A2G5D1Y2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=AQUCO_03000241v1 {ECO:0000313|EMBL:PIA37529.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA37529.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA37529.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; KZ305047; PIA37529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5D1Y2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
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: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:UP000230069};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 938..1060
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 641
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1065 AA; 119158 MW; 35E4FB7EC2863168 CRC64;
MLPRKRAAEG RAEVVVVDSD NSNKKARIDY LSSCKSSKSS SEEVEIVRSS VDMAFGDIDE
DLHSRQLAVY GRETMRRLFA SNILISGMQG LGAEIAKNLI LAGVKSVTLH DEGNVELWDL
SSNFIFSEVD VGKNRALASL QKLQELNNAV IVSTITGPLT TEQLSEFQAV VFTDISLGKA
IEFDDYCHNH QPPISFIKAE VRGLFGGVFC DFGPKFTVVD VDGEEPHTGI IASISNDNPA
LVSFVDDERV EFQDGDLVVF SEVQGMKELN DGKPRRVKNA RPYSFILDED TTNYGAYERG
GIVTQAKQPK TLHFKQLKDA LQDPGDFLLS DFSKFDRPPL LHLAFQALDM FICELGRFPV
AGSEEDAQKL LLMANNINEN MGDGRLQEVD KTILQHFAFG SRAVLNPMAA MFGGIVGQEV
VKACSGKFHP LFQFFYFDSV ESLPTTPLDP TDLKPVNSRY DAQISVFGSQ FQKKLEQANV
FIVGSGALGC EFLKNLALMG VCCSNKGKLT ITDDDVIEKS NLSRQFLFRD WNIGQAKSTV
AASAASSINS HLHAEALQNR VSPETENVFN DTFWENLDVV INALDNVTAR LYVDQRCLYF
QKPLLESGTL GAKCNTQMVI PHLTENYGAS RDPPEKQAPM CTLHSFPHNI DHCLTWARSE
FEGLLEKTPA EVNAYLSNPI EYTSAMEKAG DAQARENMEH VLNCLDGDKC ETFQDCITWS
RLKFEDYFSN RVKQLTFTFP ENSTTSSGAP FWSAPKRFPH ALEFSIDDPG HLNFIMAASI
LRAETFGIPI PDWAKNPKKL ADAVNKVIVP DFQPKEGVKI VTDEKATNPT PASIDDAAVI
DDLIRRLDEC HKKLPPDFRM NPIQFEKDDD TNYHMDLIAG LANMRARNYS IPEVDKLKAK
FIAGRIIPAI ATTTAMATGL VCLELYKVLD GGHKVEDYRN TFANLALPLF SMAEPVPPKV
IKHQNLTWTV WDRWILQGNP TLRELLDWLK DKGLNAYSIS YGACMLYNSM FPRHKERMDQ
RVVDLVRDIA KVTLPPYRRH LDVFVACEDD EDNDIDIPQV SIYFR
//
