ID   U6GVF1_9EIME            Unreviewed;       858 AA.
AC   U6GVF1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Endonuclease/exonuclease/phosphatase domain-containing protein, putative {ECO:0000313|EMBL:CDI84241.1};
GN   ORFNames=EPH_0012230 {ECO:0000313|EMBL:CDI84241.1};
OS   Eimeria praecox.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI84241.1};
RN   [1] {ECO:0000313|EMBL:CDI84241.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI84241.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI84241.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI84241.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC       {ECO:0000256|ARBA:ARBA00006335}.
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DR   EMBL; HG692721; CDI84241.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6GVF1; -.
DR   EnsemblProtists; CDI84241; CDI84241; EPH_0012230.
DR   VEuPathDB; ToxoDB:EPH_0012230; -.
DR   OrthoDB; 197020at2759; -.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0043603; P:amide metabolic process; IEA:UniProt.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR038772; Sph/SMPD2-like.
DR   PANTHER; PTHR16320:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G01540); 1.
DR   PANTHER; PTHR16320; SPHINGOMYELINASE FAMILY MEMBER; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000313|EMBL:CDI84241.1};
KW   Exonuclease {ECO:0000313|EMBL:CDI84241.1};
KW   Hydrolase {ECO:0000313|EMBL:CDI84241.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nuclease {ECO:0000313|EMBL:CDI84241.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          157..315
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   REGION          63..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  92518 MW;  0D4BA1D5FA99ADA9 CRC64;
     MPAIAAGELP ELCNASEAAV VAPSSCTETD VEGETANPLL QGEYHKESDI GAQNETACVE
     GEHRGGKMHA QSAPGGCTEG CVGPTQAPGE NHSNPQDAQP TTSGAEAAAP RGGVSWTQAE
     GRAYQARLDE LVLLSFNAGL LEYKLCGLRV YQNPPFTQRR LHHIPAALLS TGADIICLQE
     VYGDNHADFI IESTRHKLPF VGRRTSGGRF SLHNGLMVLS KYPILHTQFH KFEDVTYIER
     CFASKGMLEV AVDVPSIGVI AIFNIHLASG AVDPESRYVE DVRAAEIRQL LKACDAAADR
     GHVPLVIGDL NAAPHLCASN YKCFVERGWR DCWLHVHGHQ RHLLQHHLLH QQQLLEEQQL
     DDQGIELHDR HIRRDLFVRV RRQRRMKLRR GPELGAPQLP PQAPPQGTAT SARAKAVQQS
     HLGSSQATSP RVPTVSSDAD SSDAEREQKQ QLLGQRHNQG ECVPHRNGGP RGQSIVRSSS
     TAQRGTNTYF GGMRNYSSNR EAGRSSPADT SRDLSRGGSM ELCSSSSSDA TAAGPRRTPG
     RSKSALGGRT DDKEEIPPVK GLLGGYFGRA GGGVQLPLAF ELPAAAAWAH REFFLTAKRR
     LIEQQQKWLG GGDKAPVLDV RLSLSAPQHH QRGVDATPLA SDCSLASCST ALTAARSGDT
     ALVPAKAWRS GFLVPHPVDN QWPNEGADGT VADWLLSDTD EETESGEGRD AIIQCAPDED
     RASSASCSRR DFTWDPENPL NSIGPHAGCH GLRCDYVFLP PHQFAGGLYP FLPVAADILM
     RDPRVLVDAC CFGCFGEVML VTLSDHYAVR ITLRRSTDAD IADFWGSCAA EAAALRSAGG
     AAGDHRSADQ AASLKAND
//