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Database: UniProt
Entry: A0A151M8W6_ALLMI
LinkDB: A0A151M8W6_ALLMI
Original site: A0A151M8W6_ALLMI 
ID   A0A151M8W6_ALLMI        Unreviewed;      1050 AA.
AC   A0A151M8W6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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|EMBL:KYO20953.1};
GN   ORFNames=Y1Q_0001285 {ECO:0000313|EMBL:KYO20953.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO20953.1};
RN   [1] {ECO:0000313|EMBL:KYO20953.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO20953.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO20953.1}.
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DR   EMBL; AKHW03006295; KYO20953.1; -; Genomic_DNA.
DR   RefSeq; XP_014461496.2; XM_014606010.2.
DR   AlphaFoldDB; A0A151M8W6; -.
DR   STRING; 8496.A0A151M8W6; -.
DR   GeneID; 102559473; -.
DR   KEGG; amj:102559473; -.
DR   CTD; 115752; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   OrthoDB; 945235at2759; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
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   CDD; cd09862; PIN_Rrp44-like; 1.
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|EMBL:KYO20953.1};
KW   Hydrolase {ECO:0000313|EMBL:KYO20953.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          462..814
FT                   /note="Ribonuclease II/R"
FT                   /evidence="ECO:0000259|SMART:SM00955"
FT   COILED          993..1025
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1050 AA;  119897 MW;  D5FAC2524728E96E CRC64;
     MQRAEKVVQL RGPPGRAVRV VREHYLRPDV PCRSALCRAA CARDGKLLSD DVTHYVVPDW
     KVVQDYLEIL EFPELKGIIF MQTACQAVQH QRGRRQYNKL RNLMKDARHD CILFANEFQQ
     HSYLPRERGE SMEKWQTRSI YNAAVWYYNH CLGQMPVVMV TEDEDAIRQY GNETEGVFVI
     SFKNYLDNFW LDLKAAHELF DSILQSRRER ESESQENNGK EYPEHLPMEV LEAGIKSGRY
     IQGILNVNKH RAQMEAFVRL QGASRKKKDL QSDILIYGTK ARNRAIHGDV VAVELLPLHE
     WKGRTVALCE NEADEKASGD TSSEPMPTGR VVGIIQKNWR DYVVTFPSKE ESQTQGKNVQ
     KILVTPWDYR IPKIRISTQQ AEALQDCRVI VRIDAWESTS VYPNGHFVRV LGRIGDLEGE
     IAAILVENGI SVAPFSEVQM SEMPVSTLEN PWRVNPEEEL KRVDLRDTHL VFSIDPKGCE
     DVDDTLSVRA LANGNLELGV HIADVTHFVP VNSYTDLEAR ARATTYYLAD RRYDMLPSVL
     SADICSLLSG VDRYAVSVMW ELDKTSYEIQ RVWYNRTIIR SAYKLHYEAA QALLDGDLSG
     VDEILELKEL DERTRQQKLN ELVWAIGKLT DIARHVRAKR DSCGALELEG VEIRVLLDDK
     KNIHDLIPKQ PLEVHETVAE CMILANHWVA KKIWEKFPQQ AVLRQHPPPR QEFFSELREC
     ASAKGFVIDT WSNKALADSL DRANDPLDPI VNKLLRSMAT QAMSNALYFS TGSCSEEEFH
     HYGLALDKYT HFTSPIRRYA DIAVHRLIVA ATLKDTKENI KDSLFSNKDL DELCSHINNR
     NRAAQRAQKQ STELFQCMYF KDKVAEADER CVADGVIYSI RTNGVLVFVP RYGIKAPAYL
     KNKEGLVISC QSDGSCEWKP GFLQHFQNRI TSTTTAGESV TLSLFEHITV KILGQSSRCH
     ADTLKLEIVS NTPYETANAD VSQNSHVMKS DLVKEVTKSA EEAQLAQERA RAEIIQEEYQ
     EYCQTKGTSL YQLLEEIRDL DLLDVTEHEV
//
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