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UNG_MYCTU
ID   UNG_MYCTU               Reviewed;         227 AA.
AC   P9WFQ9; L0TBF3; P67071; P95119;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=Rv2976c; ORFNames=MTCY349.11;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or due to
CC       deamination of cytosine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC         DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45781.1; -; Genomic_DNA.
DR   PIR; E70672; E70672.
DR   RefSeq; NP_217492.1; NC_000962.3.
DR   RefSeq; WP_003899565.1; NZ_NVQJ01000015.1.
DR   PDB; 2ZHX; X-ray; 3.10 A; A/C/E/G/I/K/M=1-227.
DR   PDB; 3A7N; X-ray; 1.95 A; A=1-227.
DR   PDB; 4WPK; X-ray; 0.98 A; A=1-227.
DR   PDB; 4WPL; X-ray; 1.15 A; A=1-227.
DR   PDB; 4WRU; X-ray; 1.24 A; A=1-227.
DR   PDB; 4WRV; X-ray; 1.44 A; A=1-227.
DR   PDB; 4WRW; X-ray; 1.90 A; A=1-227.
DR   PDB; 4WRX; X-ray; 1.40 A; A=1-227.
DR   PDB; 4WRY; X-ray; 1.43 A; A=1-227.
DR   PDB; 4WRZ; X-ray; 1.19 A; A=1-227.
DR   PDB; 4WS0; X-ray; 1.97 A; A=1-227.
DR   PDB; 4WS1; X-ray; 1.40 A; A=1-227.
DR   PDB; 4WS2; X-ray; 1.13 A; A=1-227.
DR   PDB; 4WS3; X-ray; 1.40 A; A=1-227.
DR   PDB; 4WS4; X-ray; 1.18 A; A=1-227.
DR   PDB; 4WS5; X-ray; 1.40 A; A=1-227.
DR   PDB; 4WS6; X-ray; 1.10 A; A=1-227.
DR   PDB; 4WS7; X-ray; 1.88 A; A=1-227.
DR   PDB; 4WS8; X-ray; 1.40 A; A=1-227.
DR   PDBsum; 2ZHX; -.
DR   PDBsum; 3A7N; -.
DR   PDBsum; 4WPK; -.
DR   PDBsum; 4WPL; -.
DR   PDBsum; 4WRU; -.
DR   PDBsum; 4WRV; -.
DR   PDBsum; 4WRW; -.
DR   PDBsum; 4WRX; -.
DR   PDBsum; 4WRY; -.
DR   PDBsum; 4WRZ; -.
DR   PDBsum; 4WS0; -.
DR   PDBsum; 4WS1; -.
DR   PDBsum; 4WS2; -.
DR   PDBsum; 4WS3; -.
DR   PDBsum; 4WS4; -.
DR   PDBsum; 4WS5; -.
DR   PDBsum; 4WS6; -.
DR   PDBsum; 4WS7; -.
DR   PDBsum; 4WS8; -.
DR   AlphaFoldDB; P9WFQ9; -.
DR   SMR; P9WFQ9; -.
DR   STRING; 83332.Rv2976c; -.
DR   PaxDb; P9WFQ9; -.
DR   DNASU; 887410; -.
DR   GeneID; 45426965; -.
DR   GeneID; 887410; -.
DR   KEGG; mtu:Rv2976c; -.
DR   TubercuList; Rv2976c; -.
DR   eggNOG; COG0692; Bacteria.
DR   OMA; WEAVTEQ; -.
DR   PhylomeDB; P9WFQ9; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:MTBBASE.
DR   GO; GO:0006284; P:base-excision repair; IDA:MTBBASE.
DR   GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR002043; UDG_fam1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; DNA repair; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..227
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176119"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   TURN            1..3
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           12..17
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           22..38
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:2ZHX"
FT   HELIX           92..105
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           116..119
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   TURN            137..142
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           145..158
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           174..179
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:4WRX"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   TURN            194..203
FT                   /evidence="ECO:0007829|PDB:4WPK"
FT   HELIX           206..216
FT                   /evidence="ECO:0007829|PDB:4WPK"
SQ   SEQUENCE   227 AA;  24481 MW;  379B5DB72894A304 CRC64;
     MTARPLSELV ERGWAAALEP VADQVAHMGQ FLRAEIAAGR RYLPAGSNVL RAFTFPFDNV
     RVLIVGQDPY PTPGHAVGLS FSVAPDVRPW PRSLANIFDE YTADLGYPLP SNGDLTPWAQ
     RGVLLLNRVL TVRPSNPASH RGKGWEAVTE CAIRALAARA APLVAILWGR DASTLKPMLA
     AGNCVAIESP HPSPLSASRG FFGSRPFSRA NELLVGMGAE PIDWRLP
 
 
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