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Database: UniProt
Entry: A0A1J8QJM1_9AGAM
LinkDB: A0A1J8QJM1_9AGAM
Original site: A0A1J8QJM1_9AGAM 
ID   A0A1J8QJM1_9AGAM        Unreviewed;      1160 AA.
AC   A0A1J8QJM1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=PIN domain-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AZE42_03967 {ECO:0000313|EMBL:OJA13616.1};
OS   Rhizopogon vesiculosus.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA13616.1, ECO:0000313|Proteomes:UP000183567};
RN   [1] {ECO:0000313|EMBL:OJA13616.1, ECO:0000313|Proteomes:UP000183567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA13616.1,
RC   ECO:0000313|Proteomes:UP000183567};
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC       {ECO:0000256|ARBA:ARBA00005283}.
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:OJA13616.1}.
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DR   EMBL; LVVM01004089; OJA13616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J8QJM1; -.
DR   STRING; 180088.A0A1J8QJM1; -.
DR   OrthoDB; 5479162at2759; -.
DR   Proteomes; UP000183567; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd09904; H3TH_XPG; 1.
DR   CDD; cd09868; PIN_XPG_RAD2; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 2.
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; IPR001044; XPG/Rad2_eukaryotes.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR   PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   PRINTS; PR00066; XRODRMPGMNTG.
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.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183567}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          770..839
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          154..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          729..760
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        168..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1093..1107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1160 AA;  128409 MW;  3775D996421930AF CRC64;
     MGVKSLWSLL SPVGRPVPLE TIEGKVLAID SSIWIYQFQA TMRDKDGRAL VNAHVLGFLR
     RICKLLFYGI RPVFVFDGGA PALKRNTISE RKKKKSGAAA TYAKVAERLL AAQLRREALV
     HAPASHPPSS KGKQKAPSGP VVLDENAVYL EDIDGSAPKT PAKKKAEQTP PSSKKKNRFH
     DHDPYRLPEV DLEARIANVT RSQAPDPRLA TEEELRAFIE EMRPEDFDVT SEAFRELPTE
     VQYEIVGDLR LKSRQTSYTR LQNMLRKAVT PLDFSREQIK NLKQRNALTQ QLLTTTDSIG
     KAHITIPVRI ASERNREYVL VKNEGADGGW VLGIRDEGTR SKPIEIDQEE PTLQSDSEED
     MEMEEVSIPG IGTPDPDLRE FQSSMALHAI GQRSQPFVPK PVQRRIKSTP LFELDDDDDI
     PRPPIRDEFD DIEVALAIQA SLEDHAADYN PSTSEPSSSK LGPPATPQPK PALQTHDSDD
     DLYTSPSRLE TALSIAGAGP PRRISGALHD LSPQISFGKA PLLVSPKIVS HPLPSVQSSS
     PESDESMDEV LPVPVSQSLE APDRLAAPAV VSTHPEPPQS PQVVHNAELD SDEDMEEVVV
     IDEGHDQESL DSSTPVTLSA PEAVVVAKER RASPHPSFQL SETLEDHSLL SSSGVVTSRA
     PIPENDDESA IEWSRSPSPV HGAVPESTEQ GVSATSAAAE TWDAAQEMDP HVEQGEFARF
     MSQVKGKDLE VVRHEIDEEI RTLNQQKKAA MRDSEDITQQ MISQIMLMLR LFGIPYITAP
     MEAEAQCAEL VSLGLVEGII TDDSDVFLFG GMRVFKNMFN QSKTVECFLL SDLSRELGLE
     RDTLIHLAYL LGSDYVEGLS GVGPVVAMEL LKEFPGEDGL HKFKDWWSKV QSGRDREEDN
     KTRFRNRFKK KFKDLYLPLE WPNPLVRDAY YHPTVDSSEE PFKWGMPDLD ALRHFLHEEL
     GWIQSKVDDL LLPIIQIMNK RNQAASMNRQ GNLTSFFDVA PGSGSYAPKK RQAYGSKRLQ
     QVVTDFRKQQ AQRKRGSTST AAPDEADDLI PEDDHEPAIK KRKTGAKQKS QTKTIIGAAQ
     QKRPRSVARG KSRGSHTRAS TSRAGAEPGS ESGDDYVGND DGPSATKASK PHLRPRARPV
     TKGNRKPDRY DGLAADSEGS
//
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