ID A7AUW0_BABBO Unreviewed; 1007 AA.
AC A7AUW0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=BBOV_II007710 {ECO:0000313|EMBL:EDO06721.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO06721.1, ECO:0000313|Proteomes:UP000002173};
RN [1] {ECO:0000313|EMBL:EDO06721.1, ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO06721.1};
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
RN [2] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33294524; DOI=10.1016/j.dib.2020.106533;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Transcriptome dataset of Babesia bovis life stages within vertebrate and
RT invertebrate hosts.";
RL Data Brief 33:106533-106533(2020).
RN [3] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33069745;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Comparative analysis of gene expression between Babesia bovis blood stages
RT and kinetes allowed by improved genome annotation.";
RL Int. J. Parasitol. 51:123-136(2021).
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:EDO06721.1}.
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DR EMBL; AAXT01000003; EDO06721.1; -; Genomic_DNA.
DR RefSeq; XP_001610289.1; XM_001610239.1.
DR AlphaFoldDB; A7AUW0; -.
DR STRING; 5865.A7AUW0; -.
DR EnsemblProtists; EDO06721; EDO06721; BBOV_II007710.
DR GeneID; 5478523; -.
DR KEGG; bbo:BBOV_II007710; -.
DR VEuPathDB; PiroplasmaDB:BBOV_II007710; -.
DR eggNOG; KOG2012; Eukaryota.
DR InParanoid; A7AUW0; -.
DR OMA; GANLHAF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002173; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 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; 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; 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; 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:UP000002173};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 862..1000
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 584
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1007 AA; 112616 MW; 9B46DA19F439CF8B CRC64;
MDIDDTASEV DTDLYSRQIG TFGIETMGKI QKLKVLILGM KGVGVEIAKN LALMGVEAIC
ITDDNIVERR DLGVNFFIRS SDVEVKTVSD ACLHHLQDLN RNVQITVHHG PIVEELITRH
DVVVCCDQQY EMLINVNRAC RNNKLNKRVG FIVADTFGMV GAVFVDFGNE FVCVDPSGKE
INTAIVSGIS NEEAGLVYIH TEGSMPFQSG DFVTFSEVEG MDELNNMGPI EITIKDKESF
TIGDTRGFGQ YVTGGIVKEI RRSKQIDFIS LEDAIQNPSK NGCMITMDLS LIGRAEQLHW
ISMAYRISGQ SADAVLATAK TLNTKAQSCA VEKIDEDVLN SFVKNARYRI SPICSFVGGV
VAHEVVKFTG KYHPIDQWLY CDFTLPTEIT SGNNSDIGYD SRYSDHIAIW GREIQSKIQS
AKIFTVGSGA LGCEFMKHFA LLGCGTQNGG IVKITDNDRI EVSNISRQFL FRKKHVGMSK
SKVAAISAKE INEHMKIDAL ELAVGADSEN MFNDSFWEEL TVVVNALDNI KARTYVDGRC
VWYEKPLLES GTLGTMGNVQ VIIPHMTQCY SESQDPQENS IPLCTLKHFP YQVDHTIQWA
RDLFEGIFTQ TAHDLKRIQQ NSPDVDDISD EKISLIAKLL KINDTNVKTE LLQIAAELVN
KYFINDINQL LYSFPKDHRT SDGHKFWSPP KRMPTPLTFN PSEKYVSMFL IATANILATV
IGKKVLVNQD DVAMMPPMQF EPFKPKILKL SQDKLNVVVE TPAECTISRS KSMQEIMNSR
NVFESVEFEK DDDTNYHIEF IWATANLRCQ NYDIDQCDRM KAKMISGKII PAIATTTSMI
AGLVMLEFVK TICYQKLKIE HFRNSFCCLA TPLWLQSEPM PPTTTSDKEY DPVVGGAIRA
LPPNFTVWDK VKINIPNGTV GDVIEAIRVK FNVEAIILSA GNTCIYNSFM PAHQRERRSQ
PIAQLLEKLT KAPLLPSCSY LVIEASCTDD DDVDVVIPTI QFGFRAT
//
