ID A0A166MP87_EXIGL Unreviewed; 577 AA.
AC A0A166MP87;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=PIN domain-like protein {ECO:0000313|EMBL:KZV78250.1};
GN ORFNames=EXIGLDRAFT_782859 {ECO:0000313|EMBL:KZV79063.1},
GN EXIGLDRAFT_784101 {ECO:0000313|EMBL:KZV78250.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV78250.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV78250.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV78250.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427010; KZV78250.1; -; Genomic_DNA.
DR EMBL; KV426689; KZV79063.1; -; Genomic_DNA.
DR STRING; 1314781.A0A166MP87; -.
DR OrthoDB; 1615659at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0004520; F:DNA endonuclease activity; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR CDD; cd09870; PIN_YEN1; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR041177; GEN1_C.
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:SF71; ENDONUCLEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G13260)-RELATED; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF18380; GEN1_C; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
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 Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 1..106
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 116..193
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 439..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 63406 MW; 050E932AF32E5F99 CRC64;
MGVEGLWEIL KPAAKTESLT KLAVDAFVAN RNGHRGLRLG IDASIWSFHA QCAQRKNPLV
ENLALQVIFF RCANLLRLPL LPLFVFDGPE RPHTKRGKDI STRESQLTVD IQSIVRAFGF
GCHFAPGEAE AELAYLNCNG ILDAVLTDDV DAFIFGARVV IRNSTLSANQ SDPILNADGK
ADDDHVRMFT LDLFKADPIA LSPAGLILIA LLQGGDYDPG VKGFGIAIAQ GLAKGGFGEE
LLAASAIEDE DERNTALSQW CESIKAELRS NSRGQLATRH PALADRIPSE FPNPEIVRAY
THPEVSNSAG NFDLSLWRQD PDVGELARLC EQYFSWGYKK AILKRFRTII WPGATVRMLR
HSALWNDELR AAEQSISFVS TLTPVQSSPL RRINVNQLLE SLSKERTHAS TDGLREFRAA
LAEDQVRLLE QLVTAKILGT RPEPEGNPYA ADNEQDPSEQ SSRERTKAGV ATRLRMWIPA
ALLEHSVPEV MRTFQGSTSN RARAPRATAK GRKSAAASET SREVISPTTQ HRQELPRADV
GPVADNDMES SPTDDILIIL SSDEEPLIVV NGVIDLT
//
