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Database: UniProt
Entry: A0A176WP21_MARPO
LinkDB: A0A176WP21_MARPO
Original site: A0A176WP21_MARPO 
ID   A0A176WP21_MARPO        Unreviewed;       678 AA.
AC   A0A176WP21;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=XPG-I domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_3005s1320 {ECO:0000313|EMBL:OAE33986.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE33986.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE33986.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE33986.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAE33986.1}.
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DR   EMBL; LVLJ01000465; OAE33986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WP21; -.
DR   OrthoDB; 26655at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004520; F:DNA endonuclease activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09869; PIN_GEN1; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11081:SF59; FLAP ENDONUCLEASE GEN-LIKE 1; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          1..97
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          131..212
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          97..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  75750 MW;  F3014B8A2F4B1F4F CRC64;
     MGVGKGFWEQ LRPLARTEDL SFLRGKRLAV DLSYWLVQQQ TALKDHRVRK PHLRLTFFRV
     VKLVAKVGAL PVFVVDGEPP ALKQGVRMKR FKRFSSLCPP SPPHSPATTE SVSTRNGSFS
     ANVEECVILL ELLGMPVLRA EGEAESLCAI LNREGLVDAC VSPDSDVFVH GAKWVIKTLQ
     LDNKSKARPS LSVEESEVEL YRAEDIEASM GLRRNHLVAL ALLIGCDYMP EGVAGVGCAN
     AFQLIRSFPE SEILDRLRAW GRGEGPSEGE IEQGAQDDGS GREPSVAYDS EVQIRVTHCS
     KCGHPGNKKE HLNSGCGICF PSREDEYSFE KGCKPKPKGF LCSCPFCSQK ARSKLQTKAN
     AWWGKMCSKM AATPGFPNEE IIKIFLNSEI PTFEDVTGYA SSIKWHAPAM DELEMFLQKH
     LSWDSFYVRQ KALPLLSHFY LSDLADKYCK SSEELLNGAF APLCIHRIKI EHGEPLYVLK
     WKNMREGVDG EQWLGLKLNS TSPKHIEETV AKECRTDNEC VDLLSTEATE KEWCFTTDES
     MESIKAACPE LVEEFDRSQE AKQAARKKAS KRKKVEGIES AKRQSDITSF FKVEHDLHKN
     KLTESPQFER KCELGSPHTL ERTAAGLDYI DTEALVASLN SNSKSTTFSS TSPPLTRTRR
     RSFPTKVVRK LSYGEGAG
//
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