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Database: UniProt
Entry: A0A1U8D9B3_ALLSI
LinkDB: A0A1U8D9B3_ALLSI
Original site: A0A1U8D9B3_ALLSI 
ID   A0A1U8D9B3_ALLSI        Unreviewed;       998 AA.
AC   A0A1U8D9B3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DIS3-like exonuclease 1 {ECO:0000256|ARBA:ARBA00016366};
DE            EC=3.1.13.1 {ECO:0000256|ARBA:ARBA00012163};
GN   Name=DIS3L {ECO:0000313|RefSeq:XP_014373735.1,
GN   ECO:0000313|RefSeq:XP_025055308.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014373735.1};
RN   [1] {ECO:0000313|RefSeq:XP_014373735.1, ECO:0000313|RefSeq:XP_025055308.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001849};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family.
CC       {ECO:0000256|ARBA:ARBA00005785, ECO:0000256|RuleBase:RU003901}.
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DR   RefSeq; XP_014373735.1; XM_014518249.2.
DR   RefSeq; XP_025055308.1; XM_025199523.1.
DR   STRING; 38654.A0A1U8D9B3; -.
DR   GeneID; 102373465; -.
DR   KEGG; asn:102373465; -.
DR   CTD; 115752; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   OrthoDB; 945235at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   Gene3D; 2.40.50.690; -; 1.
DR   Gene3D; 2.40.50.700; -; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR033771; Rrp44_CSD1.
DR   PANTHER; PTHR23355:SF30; DIS3-LIKE EXONUCLEASE 1; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF17216; Rrp44_CSD1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Exonuclease {ECO:0000313|RefSeq:XP_014373735.1,
KW   ECO:0000313|RefSeq:XP_025055308.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_014373735.1,
KW   ECO:0000313|RefSeq:XP_025055308.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..998
FT                   /note="DIS3-like exonuclease 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041162111"
FT   DOMAIN          409..761
FT                   /note="Ribonuclease II/R"
FT                   /evidence="ECO:0000259|SMART:SM00955"
FT   COILED          940..972
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   998 AA;  113459 MW;  8AE38C2ECEB6F7E9 CRC64;
     MQRQRMLLQA GAWLAGAVLH CWLALHGRSN TAAAVGGSDD SRQYNKLRKL MKDARHDCIL
     FANEFQQHSY LPRERGESME KWQTRSIYNA AVWYYNHCLG QMPVVMVTED EDAIRQYGNE
     TEGVFVISFK NYLDNFWLDL KAAHELFDSI LQSRRERESE SQENNGKEYP EHLPMEVLEA
     GIKSGRYIQG ILNVNKHRAQ VEAFVRLQGA SRKKKDLQSD ILIYGTKARN RAIHGDVVAV
     ELLPLHEWKG RTVALCENEA DEKASGDTSS EPMPTGRVVG IIQKNWRDYV VTFPSKEESQ
     TQGKNVQKIL VTPWDYRIPK IRISTQQAEA LQDCRVIVRI DAWESTSVYP NGHFVRVLGR
     IGDLEGETAA ILVENGISVA PFSEVQMSEM PVSTLENPWR VNPEEELKRI DLRDTHLVFS
     IDPKGCEDVD DTLSVRALAN GNLELGVHIA DVTHFVPVNS YTDLEARARA TTYYLADRRY
     DMLPSVLSAD ICSLLSGVDR YAVSVMWELD KTSYEIQRVW YNRTIIRSAY KLHYEAAQAL
     LDGDLSGVDE ILELKELDER TRQQKLNELV WAIGKLTDIA RHVRAKRDSC GALELEGVEI
     RVLLDDKKNI HDLIPKQPLE VHETVAECMI LANHWVAKKI WEKFPQQAML RQHPPPRQEF
     FSELRECASA KGFVIDTWSN KALADSLDRA NDPLDPIVNK LLRSMATQAM SNALYFSTGS
     CSEEEFHHYG LALDKYTHFT SPIRRYADIA VHRLIVAATL KDTKENIKDS LFSNKDLDEL
     CSHINNRNRA AQRAQKQSTE LFQCMYFKDK VAEADERCVA DGVIYSIRTN GVLVFVPRYG
     IKAPAYLKNK EGLVISCQSD GSCEWKPGFL QRFQNRITST TTAGESVTLS LFEHITVKIL
     GQSSRCHADT LKLEIVSNTP YETTDADVSQ NSHVMKSDLV KEVTKSAEEA QLAQERARAE
     IIQEEYQEYC QTKGTSLYQL LEEIRDLDLL DVSAGNRA
//
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