ID   L1LED3_THEEQ            Unreviewed;      1237 AA.
AC   L1LED3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Amine oxidase, flavin-containing family member protein {ECO:0000313|EMBL:EKX73706.1};
DE            EC=1.13.12.3 {ECO:0000313|EMBL:EKX73706.1};
DE            EC=1.4.3.4 {ECO:0000313|EMBL:EKX73706.1};
GN   ORFNames=BEWA_037420 {ECO:0000313|EMBL:EKX73706.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX73706.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:EKX73706.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:EKX73706.1,
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:EKX73706.1}.
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DR   EMBL; ACOU01000002; EKX73706.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1LED3; -.
DR   STRING; 1537102.L1LED3; -.
DR   EnsemblProtists; EKX73706; EKX73706; BEWA_037420.
DR   VEuPathDB; PiroplasmaDB:BEWA_037420; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   OrthoDB; 230475at2759; -.
DR   Proteomes; UP000031512; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097621; F:monoamine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050361; F:tryptophan 2-monooxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:EKX73706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          1119..1168
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
SQ   SEQUENCE   1237 AA;  141482 MW;  981B45F4CA88A070 CRC64;
     MKRKGFHVSL DSFCLVLFFL IYTCSDFYTS HFHIYVTGKG SIDEDDKHKE LQRWIFLYFS
     LTDEQKEEIE TCAIVKESSK FHDGSSSSDS ILDKGTLDYW KRVVSELKSR FTLQNIRLIW
     NNIGRSVKLR VRIRDSDVIG EDGSTFRIQQ LKTMKKYRAN AYDRSVVIRD GGVNKAFQVA
     VTHRNEVFSS LDLEPPYDSP KYFRSKDNIS YTNSGRSQRY LQTVNNILDF GGLIKSKTST
     AKVIDNKLVP LKAEGFVPVK RKKSISQTQN KKTNRMDENF KVKDWNLDEL SKILIYPKPS
     PINVKFRGSF VDLPTEVVDV LVVGAGIAGL TAANYLKTCG LSVCLVEARN RIGGRAFTSS
     FPTRILPNGQ VLDEVSVDLG ANYLHCCNIL DGKHLNDEKV YMFHPAKDVR VKRKWSKSLL
     GLARELKPRV SDVAGGANWE PTVYTSWYND ITGEKINLQS VVKANMIGEK IRLRAAKKVI
     ALKRDLKDDC FTLSPSMNLS YDDASTSTST LSALSKYDCK GGNTPPKWYV SEGLYREFLG
     QKSSEYARNM YLKVEKDATP TCSVGPGRKA LWDIYIESFR EVFDELTSCG NNLSEVELKL
     IFIIMQSRLG YNSDLRETCI SMCRLPIIDD EIDLSSTYLS KKNVQSYGRF ISDTFDQVNK
     VNIVPFDTCT DSDKIVIDGW DWLLGHLSSD LDDVIHLNTK AVNISTDDEF GYVKATVCPS
     DGVLNNLVTH VRAKYAIICV PSTILSSDTN YNETCTNKIS FNPPLDSRKC QALERYRMGH
     HNKVILRFSP KDVFWPDDEL QFNCLDDRFQ FMNLHAYGKD GCLLAHSFPP FPITWNEIER
     DEDIVRQCLE LLQRMFCISS EQMPFPVDAI VTRWYNDPYS MGSYSYPHTN AVDDDIIHLK
     SPHPKLNPRI LFAGEYLSNS YYQCVDGAFD TAMRAAEDVA HIAFRRPYPF PINQHTPSLD
     GLLNPLFYEK YLNIPIPVLE PQFIGYYLTD GSDERLSDSR FSNVIQDIVF TEDKYKDASL
     VETELEILKR VNSAVSRDGL SIRSFQALYK SISVDMQELK ENNYWNKPLE AASILLASMW
     RACKEYKGET DQSVLNTRTQ MFSEKMCQAV CELTGLRHDY ICWACLRGGE VLLCDNAECN
     KVWHVECVPC DLKPIDTNLW MCPSCVGCDI KVSCCPRNTF LQRGEYAADE AIQLYWIRRG
     SWWRVKVVLS LCRRVYERIL FCKRKVSRMS RQSIFSA
//