ID A0A061D4Q4_BABBI Unreviewed; 1030 AA.
AC A0A061D4Q4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=BBBOND_0102570 {ECO:0000313|EMBL:CDR93929.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR93929.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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; LK391707; CDR93929.1; -; Genomic_DNA.
DR RefSeq; XP_012766115.1; XM_012910661.1.
DR AlphaFoldDB; A0A061D4Q4; -.
DR STRING; 5866.A0A061D4Q4; -.
DR EnsemblProtists; CDR93929; CDR93929; BBBOND_0102570.
DR GeneID; 24562470; -.
DR KEGG; bbig:BBBOND_0102570; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0102570; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000033188; Chromosome 1.
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:UP000033188};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 885..1023
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 1030 AA; 115530 MW; FD2C60232E276A6D CRC64;
MDLDGQNTGI DTDLYSRQIG TFGIEMMGKL QKLKVLIIGA KGVGTEIAKN LALMGVDTIC
LHDDDTVKRQ DLGVNFFLRS ADVGVKVVSE VCLRHLQDLN GNVNVIAHRG EITEEVIVQY
DVVVCCDQKL DMLMKVSGSC RNNRLNKRIG FISADTFGMV GAIFVDFGNN FVCVDPSGKD
TITAIVSGIS SEEKGVVYIH TEGSMPFQSG DVVTFSEVEG MEELNSMGPV EITVKDKDSF
TIGDTRGFKP YISGGIVKEI RRPKQINFIS FEEAMTNPSK NNCMLTMDYS LFGRAEQLHW
ISMAYRMCGN DVNSVKASAQ NLNAKAQSSA VEQIDEKVLS NFVRFAHLRI SPLCSFVGGV
VAHEVIKFTG KYHPIDQWLY CDFTLPEEVT TGNTSDVGFD SRYSDQIAIW GREVQSKIQS
AKIFTVGSGA LGCEFMKHFA LLGCGTQNGG VVTLTDNDRI EVSNISRQFL FRKKPPEIHK
RFQKHVGLPK SKVAAMAAKD INEHMRIEAL EIAVGQETED YFNDRFWEHL TVVVNALDNV
KARQYVDGRC VWYEKPLLES GTLGTMGNVQ VIIPHITQCY SESQDPQETS IPLCTLKHFP
YQVDHTIQWA RDLFEGLFTQ LAHDMRKIQN NSSGKRAKNS VTSRFTEIDD IPDDKVKMIA
QLVKITDNNA KEELLRIAAH LLNQYFVNNI KQLLYSFPAD HLTSDGLKFW SPPKRIPEPL
VFNSEEKYVN MFLVATSNIL GTVIGKDVRV DANDAKAMPK VEFEEFKPVV LKLSNDKLNV
EVEAPANNDK MREVLIDEIR RSNAKFNSVD FEKDDDTNFH IEFIWATANM RCRNYDIEQC
DRMKAKLIAG KIIPAIATTT AMVAGLVMLE FVKTICYKKL KLEHFRNSFC CLATPVWLQS
EPMPPTTTSD KEYDPIVGGA VRALPANFTT WDKVHLNLPN GTVKEIIEAI RDKFNVEIII
LSAGNICIYN SFMPSHQRER LNQPVAELME KLSKKPLPPS CSHLVMEASC TDDDDVDVVI
PTIKFSFRNA
//
