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Database: UniProt
Entry: L1LFQ3_THEEQ
LinkDB: L1LFQ3_THEEQ
Original site: L1LFQ3_THEEQ 
ID   L1LFQ3_THEEQ            Unreviewed;       683 AA.
AC   L1LFQ3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Autophagy protein, putative {ECO:0000313|EMBL:EKX74104.1};
GN   ORFNames=BEWA_041420 {ECO:0000313|EMBL:EKX74104.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX74104.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:EKX74104.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:EKX74104.1,
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   -!- 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:EKX74104.1}.
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DR   EMBL; ACOU01000002; EKX74104.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1LFQ3; -.
DR   STRING; 1537102.L1LFQ3; -.
DR   EnsemblProtists; EKX74104; EKX74104; BEWA_041420.
DR   VEuPathDB; PiroplasmaDB:BEWA_041420; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   OrthoDB; 1128973at2759; -.
DR   Proteomes; UP000031512; Unassembled WGS sequence.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 1.
DR   InterPro; IPR032197; Atg7_N.
DR   InterPro; IPR042522; Atg7_N_1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR   Pfam; PF16420; ATG7_N; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512}.
FT   DOMAIN          4..188
FT                   /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16420"
FT   DOMAIN          361..587
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   683 AA;  76961 MW;  FA900C67C8C020B8 CRC64;
     MQLLRFIPQI YNIDVSFFIK LYENKLYRYK SSCSRVRLFG LFMLDGVLRL DKHSFEDKCC
     RFEDCKSNSG SLRDRRALEE TYLAETVDSV GYGEEKCSCV LVEGLLILSE SLEAFRNLDK
     EKEIRNILSV KGSNEDSSEF APKTQSVYRF SDSNRFVVFA FVDLKGHACH YSICSPLVYP
     ETPYTISSRS DVCSINKGDL DIILEFCKNN PLKCPIFVYN RSSGVVTNLF DCTFLDDTLS
     ITDETLRLED LFFCSLSNLE CGDALYRYWR SFLLQFTLAN GVFSKVVHVV IIGLSELERD
     GDVKYKLYGI WVPQEIKFER LSISHGFKGS QSGTKYEHYY SFSDYLDPRK VCKLDEELNL
     QLMTWRVVPE LKLDRISRLN VGIIGVGALG SSIARQLLSW GIGDFTIVDN GTVSNATRQG
     LYTHEDCLKR TPKVEAANTM IKRIRPDANV KSLFLRIPMP GHYESQEDIN NAVNAMEEIM
     DSCDVLFLST DSKESRWLPS LLASVRNFKG DNTPLVISVG LAFDSLMIIR HSFREFVGAC
     YFCSESSVLQ DTISGRPIDE TCTIVKPGIS TTCASLAVEL LVNLTQHESG FAAPHGSTSC
     LGCIPHSIRL SISDLKISQL FAEPSDSCIC CSNRIFSSFI NDEKFLQKVY KDTKYLAKVS
     GLTSIASKCG DYTIATDGDF IIL
//
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