ID A0A1M6H873_9ACTN Unreviewed; 382 AA.
AC A0A1M6H873;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=DNA-formamidopyrimidine glycosylase {ECO:0000313|EMBL:SHJ18364.1};
DE Flags: Fragment;
GN ORFNames=SAMN02745244_01901 {ECO:0000313|EMBL:SHJ18364.1};
OS Tessaracoccus bendigoensis DSM 12906.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ18364.1, ECO:0000313|Proteomes:UP000184512};
RN [1] {ECO:0000313|EMBL:SHJ18364.1, ECO:0000313|Proteomes:UP000184512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ18364.1,
RC ECO:0000313|Proteomes:UP000184512};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FQZG01000031; SHJ18364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6H873; -.
DR STRING; 1123357.SAMN02745244_01901; -.
DR Proteomes; UP000184512; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:InterPro.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.8.50; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR007267; GtrA_DPMS_TM.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1.
DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR Pfam; PF04138; GtrA; 1.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184512};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..92
FT /note="DNA glycosylase/AP lyase H2TH DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01232"
FT REGION 120..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SHJ18364.1"
SQ SEQUENCE 382 AA; 42720 MW; 8333BE19C25EF977 CRC64;
ALDPFDPRFD QSAVARRMRA RHTTVKRAIL DQRLISGVGN IYADEALWRA RIHFEQPTAD
LGPRKAVQLI RSAHEVMAEA LEQGGTSFDS LYVDIDGESG YFARSLNVYG RAGQACRRCG
TPRRDDHQRP SAAGSVRRLT RPVLGTPGQP PPRRHARQPV SIESSAAPLS CEAVHEPQLI
PLPEVQACPE GSQMIRELTR RYGNTMRQLV KFGVVGGSGV LVNMVVTVVM NKLNGGSINA
QNILFAIKGT PFNIRFTVLV WIVAFLVANL YNFQLNRWWT FKSSKHAGWW KEFWPFLAVG
SVAALVGMFL KIAMTNPSSP FFLPEPHFHE ETGLRSREYW SQLIAILITM PINFIVNKLW
TFRSVRGHAP VHTDAAEVQA AE
//
