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UNG_MIMIV
ID   UNG_MIMIV               Reviewed;         370 AA.
AC   Q5UPT2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Probable uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.-;
GN   Name=UNG; OrderedLocusNames=MIMI_L249;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
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   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50521.1; -; Genomic_DNA.
DR   RefSeq; YP_003986745.1; NC_014649.1.
DR   PDB; 5X55; X-ray; 2.30 A; A/B=1-370.
DR   PDB; 6LYD; X-ray; 2.60 A; A=95-370.
DR   PDB; 6LYE; X-ray; 3.10 A; A=95-370.
DR   PDBsum; 5X55; -.
DR   PDBsum; 6LYD; -.
DR   PDBsum; 6LYE; -.
DR   SMR; Q5UPT2; -.
DR   GeneID; 9924856; -.
DR   KEGG; vg:9924856; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   DisProt; DP01481; -.
DR   Gene3D; 3.40.470.10; -; 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   SUPFAM; SSF52141; SSF52141; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Probable uracil-DNA glycosylase"
FT                   /id="PRO_0000176176"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:6LYD"
FT   HELIX           125..128
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           135..142
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           146..159
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           168..170
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           173..177
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          185..191
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           219..230
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           244..248
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          251..257
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   TURN            267..272
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           273..286
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          291..296
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           297..303
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          311..316
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   TURN            321..325
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   STRAND          338..342
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:5X55"
FT   HELIX           350..360
FT                   /evidence="ECO:0007829|PDB:5X55"
SQ   SEQUENCE   370 AA;  42218 MW;  15D0E0CF1DB11A26 CRC64;
     MSKKNVDPFS DSDSSSEPPS IFSSDNEENS DVDNSVIIND KNTKSDEADI KYMDEDESSD
     SESESESKKK SKKSKKSKKS KKSVTKKKNN LLVGNRIITE YILIDANNYH FKSWIECFPD
     CKVNLKLLLF RPEWFDFFKY VESKTYFPQL ESKLSSYLEK RQRIVPYPEL LFNTMNVLPP
     GKIKVVILGQ DPYPGSCISG VPYAMGCSFS VPLNCPVPKS LANIYTNLIK FNHMRKAPKH
     GCLASWILQG TFMINSAFTT VLNESGVHAR TWESFTADLI DYLTDNYDDL IFVAWGAHAH
     KLCQRVDPKK HYIITSSHPS PYSVSNTMTS MSYGPNPKKV TYPSFNSVDH FGKINEHLKS
     RNKKPIFWDL
 
 
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