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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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