ID   E9AR87_LEIMU            Unreviewed;      1161 AA.
AC   E9AR87;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative 5'-3' exonuclease {ECO:0000313|EMBL:CBZ25474.1};
DE            EC=3.1.11.- {ECO:0000313|EMBL:CBZ25474.1};
GN   ORFNames=LMXM_17_1150 {ECO:0000313|EMBL:CBZ25474.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ25474.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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DR   EMBL; FR799570; CBZ25474.1; -; Genomic_DNA.
DR   RefSeq; XP_003873980.1; XM_003873931.1.
DR   AlphaFoldDB; E9AR87; -.
DR   GeneID; 13450339; -.
DR   KEGG; lmi:LMXM_17_1150; -.
DR   VEuPathDB; TriTrypDB:LmxM.17.1150; -.
DR   OMA; WYYPFHH; -.
DR   OrthoDB; 150817at2759; -.
DR   PhylomeDB; E9AR87; -.
DR   Proteomes; UP000007259; Chromosome 17.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18673; PIN_XRN1-2-like; 1.
DR   Gene3D; 1.25.40.1050; -; 1.
DR   Gene3D; 3.40.50.12390; -; 2.
DR   InterPro; IPR027073; 5_3_exoribonuclease.
DR   InterPro; IPR041412; Xrn1_helical.
DR   InterPro; IPR004859; Xrn1_N.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR   PANTHER; PTHR12341:SF76; EXONUCLEASE XRNA, PUTATIVE-RELATED; 1.
DR   Pfam; PF17846; XRN_M; 2.
DR   Pfam; PF03159; XRN_N; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   4: Predicted;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:CBZ25474.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBZ25474.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   TRANSMEM        1055..1080
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1096..1127
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          353..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1161 AA;  123882 MW;  E8FCB93C5DE9CBED CRC64;
     MGVPKFAAWL TRKYPSMVMD SCPGDVHGLY IDLNGLIHPC CHDEHDPSVA LRTQEEKLRS
     ICLAIETLVV TVRPQRVIYI AIDGVVPRAK LNQQRARRYM SSAVPLTDTD KPTRGGSHKM
     SATIVAAIEK EFTQAECDGV ERELADVSQA LMGDVLYGGC AAMALAEDTT EKAEVHTLAA
     APWVTVPTLA SQGEKGACCA AAAQIGRQPA AAASPAKFDS NCISPGTAFM DAVATAVRDY
     IRRKLAPKES DGGGEAVAEA GASPAATCAH WAGLTVVFSD SNTAGEGEHK IFDFLRTQSA
     FPGFNGSGCH VIAGLDADLI FLSLSLHIPR VVILRDHKRS SYEQALLPDT AGGTLITKRV
     PPKAKPRPVR RPGVFSSSMS SIDSAAAPTA AAEDEVALAS GTASMAAPSD GTDEGGPFWG
     SEAHSSPASP ATVAPATAPP QHIADMVVEP SKGYEYFDVD VVGASVVSEV YQLCLENGMQ
     LRGDPLECAA NCVSANGFCF YRYKGTSSRE VDGGADFDGD GSGDAKAVSS AATKGGGRRR
     GKLDGKPKAP PPPFHPCTST SNSKIIDDFI VLGVLLGNDF LPHLPSVYCG ESAMDTLMDV
     YVRAVLPYGY LTGGEYEIQL LQLERLFRAY AAVEAARFRQ FVIQSGAMTP HDAATPELCS
     AADRRCWRDV YVRTTSLRDE AGAQAACRSY VEGMRFVWRY YSSISLQVSW AWYYPFHHAP
     LALDIADFLR AQGPQVQTTL AAPKLEWQPP SPFCQLLCIL PSPSCQLVPD ALRATMASPP
     AELADTFPRR WVVDRTGAYG KDHLATALLP FANVPRLQEL VAAASGTYTE AEQQRNALRS
     GHLVFEGQPA PPAKDSTDAS ADATPTAATA GNFTDPTASE RAERAPFPKP RRASPARKVP
     PVAGSAAAMM RGYRIQGSGL SVLSAGEKPA DMRDYTAIVC SSLVEVVPPL SRPRTYSYTV
     PIPSLTVLPD GSRLAAERPP QHRRGGRRPR HGSGAGPPDR SACAYAASNN AADAQAVTPA
     MLFGEFALCL VAMGILTAEV TLWRSLSVPS LLRSWPILLQ LCGIGAALVW LAFALGLAVA
     PKGRSAGSGL HRHSIFTGFA DWQCSACLSL NFSRNRRCFI CRAPYDPHRC VVLFSSRYPP
     EPPLMDPDHS AYAAYYSITA V
//