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MUT7_AEDAE
ID   MUT7_AEDAE              Reviewed;         719 AA.
AC   Q179T2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Exonuclease mut-7 homolog;
DE            EC=3.1.-.-;
DE   AltName: Full=Exonuclease 3'-5' domain-containing protein 3 homolog;
GN   ORFNames=AAEL005527;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
CC   -!- FUNCTION: Possesses 3'-5' exoribonuclease activity. Required for 3'-end
CC       trimming of AGO1-bound miRNAs (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the mut-7 family. {ECO:0000305}.
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DR   EMBL; CH477346; EAT42986.1; -; Genomic_DNA.
DR   RefSeq; XP_001651037.1; XM_001650987.1.
DR   PDB; 7JW2; X-ray; 1.50 A; A/B=427-652.
DR   PDB; 7JW3; X-ray; 3.05 A; A/B/C=25-405.
DR   PDBsum; 7JW2; -.
DR   PDBsum; 7JW3; -.
DR   AlphaFoldDB; Q179T2; -.
DR   SMR; Q179T2; -.
DR   STRING; 7159.AAEL005527-PA; -.
DR   PRIDE; Q179T2; -.
DR   GeneID; 5579811; -.
DR   KEGG; aag:5579811; -.
DR   VEuPathDB; VectorBase:AAEL005527; -.
DR   eggNOG; KOG2207; Eukaryota.
DR   HOGENOM; CLU_437604_0_0_1; -.
DR   InParanoid; Q179T2; -.
DR   OMA; CSNWANR; -.
DR   OrthoDB; 1295758at2759; -.
DR   PhylomeDB; Q179T2; -.
DR   Proteomes; UP000008820; Chromosome 1.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd06146; mut-7_like_exo; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR037432; Mut-7_DEDDy_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   SMART; SM00474; 35EXOc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..719
FT                   /note="Exonuclease mut-7 homolog"
FT                   /id="PRO_0000319060"
FT   DOMAIN          575..629
FT                   /note="3'-5' exonuclease"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           80..93
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           99..111
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           115..124
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           137..151
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           162..172
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           178..188
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           190..196
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           198..206
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           210..219
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   TURN            228..231
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           232..237
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           241..249
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           252..266
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           272..283
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           295..307
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:7JW3"
FT   HELIX           434..436
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          437..440
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           443..453
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          457..465
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          469..471
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          475..481
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          486..490
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           491..494
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           498..507
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   TURN            508..510
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          514..520
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           522..531
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          540..542
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          547..549
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           550..557
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           576..584
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   TURN            591..594
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   STRAND          599..601
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           604..630
FT                   /evidence="ECO:0007829|PDB:7JW2"
FT   HELIX           635..642
FT                   /evidence="ECO:0007829|PDB:7JW2"
SQ   SEQUENCE   719 AA;  83457 MW;  996EDC512FC52FD8 CRC64;
     MSKSNNVAPP CRQDQLGFVP AGYDSDNNSE DEMLMVMPNA STSSGESGRC FDDERIKIVP
     HIGWRAGIGD RDFDIELDEN IANWFEGFRD SFKTFKKGPL ISQRLQMFYM NTRNPYEWSL
     KLFANCPDHN SPKSNSLAYT VLEEMRNFKK HYNLGTDQLV DDNLRMVAFN FVAKQGHCLL
     FRMVVDIFEF LQCRDLFIPK VREMIARKQY KEAGQIAIDL ELFEEFDEHD FVMPLFMQDK
     ISIAEDYLNK AERLQGPVVQ LLDSFFDKRQ SVESHCSRYI TEHEVTDVYY SKLHQKPLSK
     LVQRLAKNYN IPRQFTPNVN KMKNFGALQF LVHKRYYEKS LNKDSWDEMV RDTVSETDRE
     LQLELVCLCS NFNDQPEAAK WAFHYQLKRS DLPLLVQDYI LEQEGNKQAP RTDFDDEQWD
     APDSEPAHTL RLDESHVHLV DSKDKFYAML SDLCRQSMIA FDSEWKPTFG GANEVSLIQL
     ATWDDVYMID VMVSQLEPLD WAALAKNVFN RDDVLKLSFA PSTDISMFQK ALPSFNVMYS
     SQSTSAILDL QLLWRHVERF DSFRFPYHEE SVNQNLANLV RLCLGKKLDK SNQFSNWAQR
     PLRKEQLRYA ALDAFCLLEI YDAIEKQLTH IQLDPNEILN ALLNDVRPPS DSGTRRAGRQ
     DGSSGSRRNH RDKYNKRHAY AEDSNSGNSS RAHQNRTKSK GAGLREQQTF EGPNTKSVL
 
 
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