Y2191_MYCTO
ID Y2191_MYCTO Reviewed; 645 AA.
AC P9WLJ0; L0TAG2; Q10384;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Putative bifunctional exonuclease/endonuclease protein MT2247 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
GN OrderedLocusNames=MT2247;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- DOMAIN: Seems to contain an N-terminal exonuclease domain and a C-
CC terminal UvrC-like endonuclease domain. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK46533.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK46533.1; ALT_INIT; Genomic_DNA.
DR PIR; H70783; H70783.
DR RefSeq; WP_003901350.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WLJ0; -.
DR SMR; P9WLJ0; -.
DR EnsemblBacteria; AAK46533; AAK46533; MT2247.
DR KEGG; mtc:MT2247; -.
DR PATRIC; fig|83331.31.peg.2423; -.
DR HOGENOM; CLU_022933_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.1440.10; -; 1.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR TIGRFAMs; TIGR00573; dnaq; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 4: Predicted;
KW Endonuclease; Exonuclease; Hydrolase; Multifunctional enzyme; Nuclease.
FT CHAIN 1..645
FT /note="Putative bifunctional exonuclease/endonuclease
FT protein MT2247"
FT /id="PRO_0000427470"
FT DOMAIN 44..207
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 248..326
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
FT REGION 603..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 69180 MW; EA89B536EE678A77 CRC64;
MQGPNVAAMG ATGGTQLSFA DLAHAQGAAW TPADEMSLRE TTFVVVDLET TGGRTTGNDA
TPPDAITEIG AVKVCGGAVL GEFATLVNPQ HSIPPQIVRL TGITTAMVGN APTIDAVLPM
FFEFAGDSVL VAHNAGFDIG FLRAAARRCD ITWPQPQVLC TMRLARRVLS RDEAPSVRLA
ALARLFAVAS NPTHRALDDA RATVDVLHAL IERVGNQGVH TYAELRSYLP NVTQAQRCKR
VLAETLPHRP GVYLFRGPSG EVLYVGTAAD LRRRVSQYFN GTDRRKRMTE MVMLASSIDH
VECAHPLEAG VRELRMLSTH APPYNRRSKF PYRWWWVALT DEAFPRLSVI RAPRHDRVVG
PFRSRSKAAE TAALLARCTG LRTCTTRLTR SARHGPACPE LEVSACPAAR DVTAAQYAEA
VLRAAALIGG LDNAALAAAV QQVTELAERR RYESAARLRD HLATAIEALW HGQRLRALAA
LPELIAAKPD GPREGGYQLA VIRHGQLAAA GRAPRGVPPM PVVDAIRRGA QAILPTPAPL
GGALVEEIAL IARWLAEPGV RIVGVSNDAA GLASPVRSAG PWAAWAATAR SAQLAGEQLS
RGWQSDLPTE PHPSREQLFG RTGVDCRTGP PQPLLPGRQP FSTAG