ID   L0AVC3_THEEQ            Unreviewed;      1117 AA.
AC   L0AVC3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Ubiquitin-activating enzyme E1, putative {ECO:0000313|EMBL:AFZ79198.1};
GN   ORFNames=BEWA_020440 {ECO:0000313|EMBL:AFZ79198.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ79198.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:AFZ79198.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:AFZ79198.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
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}.
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DR   EMBL; CP001669; AFZ79198.1; -; Genomic_DNA.
DR   RefSeq; XP_004828864.1; XM_004828807.1.
DR   AlphaFoldDB; L0AVC3; -.
DR   STRING; 1537102.L0AVC3; -.
DR   EnsemblProtists; AFZ79198; AFZ79198; BEWA_020440.
DR   GeneID; 15803903; -.
DR   KEGG; beq:BEWA_020440; -.
DR   VEuPathDB; PiroplasmaDB:BEWA_020440; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   OrthoDB; 227729at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000031512; Chromosome 1.
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   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1117
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003939274"
FT   DOMAIN          485..901
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          814..869
FT                   /note="Ubiquitin-activating enzyme SCCH"
FT                   /evidence="ECO:0000259|Pfam:PF10585"
SQ   SEQUENCE   1117 AA;  126895 MW;  B4E67614861E8F57 CRC64;
     MLALFIINVV IAVLLEIATC RSVNFKQDHV LTHGSDLRNP NPFLGNIKTN NISKLPGRQD
     SVHHGRNSKG KATSVVHSGI CRNLFSRVEL VLGSNALDSI SSANVLIVGA NELSNKVIAH
     FIRSGIGSIC IWDDDTQKSN RLVERISLLH PDANINILKS EPNFEKEAST YRAIVFLNQP
     LQSAIEANDR IHNKCKFVFA STIGAYGLVF SDFGTNHLVT TRSDDKYPEH SCKFTSAGNK
     TWLETTSKVQ KSFYSENDTV NLTYAHYLLN ENKGETDIQV LKCKVSRVVE ENNNVKLLID
     LDTRGWPQMT VSISKVDEPF FLDFAPLSHF IKSIFSKQSY FTLFLDKIFL SNPAGRLLIT
     PKSGNIFNND HLSVISSFLA FDQMAFNFTG TMDFDWNYHR YFIDLCRKIY PQCDDVIASN
     FNKLRHFHIP PIDFMVGAFV AQETIKGITN IFTPSELVLI DRSDLFLNKS GNVDFDIVKK
     VMSIVSNYSY LVVGAGALGC DYLRMLAEMS VSRVNVFDDD TVEISNLSRQ CLFTPDDVGK
     GKAESAIKNL NRLHDNTLKD YKYHKLLFTD SFETRAIVNS IWSDKTIALS AVDNMQGRIT
     LDNFCIENNI PLVEAGIHGM KCSTSIFIPH ITESYSSTMQ DKMLVNDKSS CTVKGIPKTI
     EDTVHYSMEL FSWLFDSQHV FINKFMMDPV KTLRQTMDHG HDYFLNAIQV IKDNCDILSS
     ESESEIDKKI LKWANKNYLK YIGYDSPLGD IWISSLIRLK TGCLTPKKCK KLTINESFID
     EIKSQVIRFL TAFKRKGNNS ELSKGSYEKC FRAISELFED KNVRKALESA NFSYSSIFFE
     ENREDCLDFI YATSNMRAFK YNIHQKDKLS ILGIAKAIVP AISTCVSIAA STSLLEVYRI
     AILSQYNIFG HDSDLKSTNF KNSKGIIGDI YLSLYNDDIS IWFSLSDKGL RCFNKNKLIA
     TLKPFNYLKS RNHCNYFNHH FFNLSIMKHF SNHPNPPYIF QVTNPNASLY GLSLSFWDYI
     LVDEQSAHFY NFKTHKNVFK KNGILVGELV KSIENMFDVI VEGFASPSGY ILINDLNNRS
     SLSDLFFSPT GQVVISILAY DRHSNKRIEL PDINYRM
//