ID   A0A0B7F9M7_THACB        Unreviewed;       587 AA.
AC   A0A0B7F9M7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Endonuclease/exonuclease/phosphatase domain-containing protein {ECO:0000259|Pfam:PF03372};
GN   Name=ISC {ECO:0000313|EMBL:CEL54245.1};
GN   ORFNames=RSOLAG1IB_06893 {ECO:0000313|EMBL:CEL54245.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL54245.1, ECO:0000313|Proteomes:UP000059188};
RN   [1] {ECO:0000313|EMBL:CEL54245.1, ECO:0000313|Proteomes:UP000059188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL54245.1};
RA   Wibberg Daniel;
RL   Submitted (NOV-2014) 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; LN679115; CEL54245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7F9M7; -.
DR   STRING; 1108050.A0A0B7F9M7; -.
DR   Proteomes; UP000059188; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..587
FT                   /note="Endonuclease/exonuclease/phosphatase domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002114034"
FT   TRANSMEM        425..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        534..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..356
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   REGION          453..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..516
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  62813 MW;  BE4DDC482677A9BC CRC64;
     MVCWRLVFAS VLATGSAFVA AAPAQAVLEL SGVERLPTPA TVQTSNATLA AADRDETNIR
     VLTFNCWGLR FVSQHRLART TAIADRILNA SPAYDVVALQ ELWLKSDHAL VAEAVASVLP
     YSTVFYSGAF GSGLSLFSRY PIEQAQMHPF ALAGDPIDVL GGDWFVGKGV AAATLAHPVL
     GHVELLTSHM FARGGETGTV LQQAHRLIGA WEYSQLIRRA AELGRYVIVA GDFNAVDGSA
     PLEFIRAHAK VQDAWWSTHN LTTPAVPIVF PIPKEGAATS ALAAIHQHGV TADSPLNSWS
     SGKPLDAMAR RHLGKRLDYV LYRGPDARAQ FELVASEAKV VMTERMADLG VSLSDHFGVE
     VLLEITPAGV STQPQQPEFV EIDATETLPP LPIPPPVART RALVLHDTLH VLHAAIPASY
     AASTAYLTTG LACAFSLIAL AVAAGAVGWG PNAKRYRPRV GRSNTDNASP VRVERKRPRA
     YTTPAPTHPT DTQSQSQSQP QTPLSSPPPP PHALRLPFLP SSSSGKSRPI QAPWWLGIVL
     VLVGGLLAAA GITLLYAGVL FGRWERNAIW DVIDQMERLG SRGGIGQ
//