ID   A0A0L0DA10_THETB        Unreviewed;      1315 AA.
AC   A0A0L0DA10;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Inositol 5-phosphatase {ECO:0000313|EMBL:KNC49184.1};
GN   ORFNames=AMSG_05165 {ECO:0000313|EMBL:KNC49184.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC49184.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC49184.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC49184.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL349453; KNC49184.1; -; Genomic_DNA.
DR   RefSeq; XP_013758204.1; XM_013902750.1.
DR   STRING; 461836.A0A0L0DA10; -.
DR   EnsemblProtists; KNC49184; KNC49184; AMSG_05165.
DR   GeneID; 25564634; -.
DR   eggNOG; KOG0565; Eukaryota.
DR   eggNOG; KOG3277; Eukaryota.
DR   OrthoDB; 996872at2759; -.
DR   Proteomes; UP000054408; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR007853; Znf_DNL-typ.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF275; LD06095P; 1.
DR   Pfam; PF05180; zf-DNL; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS51501; ZF_DNL; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00834};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00834};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00834}.
FT   DOMAIN          1194..1294
FT                   /note="DNL-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51501"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1168..1193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          93..126
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1278..1312
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        151..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1315 AA;  143461 MW;  DB9233B72781319C CRC64;
     MMAMAETGPG RTPEGAGESG SATRATFMTD ADESHAKDAH PEEIHARAVG SECVLEMVHA
     PPRDELKAAR AAQEELRIKA LETRRAFDAK RRKVEKEVEA ERARVKAEAA AEEQRLAAVA
     QRLRRRRLRA ASASLRMASK TGSLAVHPPQ GPQGPQSPHA PSAPRPATSP LPMIPLPPDV
     ALMRSPVRRV ADTQVARKMR LRQAALAQAR AVFRRDRARL AKEARAARSR LDSRRRVVNK
     KRAVELKILA REERVAVNNV AFDRARARVE ARTTWGIGPF PATPRLTTVL DDQTTRLVRS
     NIAKRRLRHM ATTLYQDTLH WSIEPPQANS RIRRGSVSPD YGTEGILSPE AADVSSNRDE
     WVSLQDADGS VYYLHLATNT RSSERPTTGR IVSPRQVGGS GATRSSSGRK KHKKKIDRIR
     YPTGDPESMG STSDEMHSRS RSRSQNERVS GSSSSDSDSD SKSDGCTAGD DGSISSYSGE
     VSVSEPSSPS AAASRPDNGS ESDNGPPKPT LVSAGSSGLA PSTSTSSPPK EVAMPSYADW
     ESLQSVELMT FATMDNKSMT LRPKRRASRA GSVAAAESKA AAEAAAAAAD ASPVVPLAET
     RVRRTEAKSI QRFDVYVLKG SGFFKGFKPR VLEVNIKRQS FAIIQTRRKG EKRKELRAAD
     VWRFEKCKSD ANKLYIVFEG KTPTYTVLCL SPSWRDLVYE TLWATHIDAG NKIGQLSFPL
     SVWVGSWNMG NAPPPDSLGD YLPTGEHDMY AFCVQECKYV PLDAHGKKIP CETRDHWYDY
     VQEALGPGYV VLCKHSLWEI RLVVAVRSCH YNKIMDVEFS KVATGIANVA GNKGGVAVSF
     NFFETSFCFI GAHLAAHQSK IAERNADYAN IVAGLRLGTN KEFDITNVAD YVFWCGDLNY
     RIELPRDAVI EFNLLRSWDV LFANDQLQAQ IAADAAFVGF TEATLDFPCT YKYARNTRTY
     AAGKHPRIPA WCDRIMWKCE SPTYQPDLVY FTDCKSIMTS DHAPVSALFT VSVQVPYRPE
     HWDRVALPCA LLLSDISVSL VQPASKAKPG DSFLAVWAPF LPGSHSLGLR SSVVKKSWEP
     HWDGDSLPLL RPSLSEPDFI AKQSIILAVI DAKSGTSRGE AKLPLGPHIR LPDDDETAPD
     APFSLRLLKG GLVTGSISGS IALNIRGGAR TPSLTPRDPS SLAGGSGDGG AVDDPDGTLM
     MVFTCDVCET RSAKTFSRHA YHHGVVLVRC DGCQSHHLVA DNLGWTDAGG SGAPPGTLEA
     ILKAKGKELR KLDGADALEY VADHANELES TLEALKARIE RQAKAKAEAQ AEDKA
//