ID A0A183MF80_9TREM Unreviewed; 1178 AA.
AC A0A183MF80;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000256|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000256|HAMAP-Rule:MF_03166};
GN ORFNames=SMRZ_LOCUS14705 {ECO:0000313|EMBL:VDP16474.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001470601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0001470601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP16474.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDP16474.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03166}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_03166};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC Rule:MF_03166}.
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DR EMBL; UZAI01016813; VDP16474.1; -; Genomic_DNA.
DR STRING; 48269.A0A183MF80; -.
DR WBParaSite; SMRZ_0001470601-mRNA-1; SMRZ_0001470601-mRNA-1; SMRZ_0001470601.
DR Proteomes; UP000277204; Unassembled WGS sequence.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR NCBIfam; TIGR00628; ung; 1.
DR PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03166};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03166};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03166};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03166};
KW Reference proteome {ECO:0000313|Proteomes:UP000277204}.
FT DOMAIN 998..1164
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..237
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 381..436
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1013
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166"
SQ SEQUENCE 1178 AA; 133036 MW; CAD23EAF1725196E CRC64;
MISLHIAFYN AINSKHFNNS NTLTTVNNVK NIGARFVKGK FLDYGKRFKV LWSQRGIGVN
QISPETVGMR ELNALIADDS CKTRKALPKR PVPEGESSES SEEIKSPRSS SFDSLVISRL
EEKEELQHLN DRFANYIEHL HKNIFNKEFS GHIDLLTNSL KNEMDDYVKV FSNEVELLRQ
NLDKTSLELT NAKIQLKKST SDLDETIKQL ERSKANETEM GNKIASLNVQ LSQLQNQLNV
CNNYKTDYDS LMDQHKMLKS QLENETLLHT DTKNKLLTAL EQLEFKNQLL AKQGVLVILR
ELVLPDGFDL VSPSFTERNI WNSESIQSHL TSIIKSVEAN SHDKLCHLLS EIRSQMTIQY
DQAKNKIKEG LKVSDAEKLR SNSLEQDLKN KITECQRLSQ LVSSQSSDLY NCRHELETTR
KQLKDFEQQL KFNEDKLHGI ISQHRSEIER LLELLTDKST ECTELAGIKI QLDAELAMYR
KLLEGEESRL HLSPTEKILK GKPIVRTNIT PTKRTYSDMC TSLLKSRQQS TGSCLHDVDL
DHADTNNIVQ SYPLTTERKI SEISDSHSKI INIDLNLHSS DLSTFPSSSS LIGDSLRITC
RADGPIHFSS ADPGEGLLRI YNASEDAIDL SNWHLYAGPT HEGSSDYVKL YTFHKSQTLQ
PHTELQVFLC FACEPSQVSS AKRVRPDVSA ILHLITPVSV WNPYSSLIAL QDSTGSVRAT
CEMESYSRKS DKISTSDVVA VDDREDGSSD KVSSVCSDDD FTSNNDPQQQ TVEDNNLNKS
VVKITRLSEE TTRSFQSHGE YFDLPKHVSS VRFRSDIWPN EASSSKLSQS SQRTLTSFFS
RTSTTPTQGE LKRKLSSSEC EGGDSDPPSK LLFSDENKSP TTGTISPSTT NTPNIKPLSP
MNNHSFNLIS NTKHLFKSTE LDKSVINKML AECRRRLTNR SNKNVLNLIQ GISNEWFVIL
LEQIEHDKFQ QLADFITKEQ NSGVTIYPPI EQIFTWTKLC LPTDIHVVIL GQDPYHGPRQ
AHGLAFSVCR PVPAPPSLIN MYKEISSSMN LTNSNDNWPP KHGDLTGWAK QGVLLLNAVL
TVRSSAPNSH KDKGWEFLTD AAIRYLNKNR NNLVFMLWGA NAQKQGQSID RKRHLVLNAP
HPSPLSANRG FFGCGHFIKA NEYLKQHGIK PIDWTKLD
//
