ID A0A1Y2EZV8_9FUNG Unreviewed; 1550 AA.
AC A0A1Y2EZV8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=PIN domain-like protein {ECO:0000313|EMBL:ORY77139.1};
GN ORFNames=LY90DRAFT_665398 {ECO:0000313|EMBL:ORY77139.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY77139.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY77139.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY77139.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-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:ORY77139.1}.
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DR EMBL; MCOG01000020; ORY77139.1; -; Genomic_DNA.
DR STRING; 1754190.A0A1Y2EZV8; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000193920; 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.
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:UP000193920}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1294..1363
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 898..938
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1250..1277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 434..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1550 AA; 180573 MW; 60083268C75F8951 CRC64;
MGVKGLWKLL HPAARPVQLE QLSDKVLAVD ASIWLHQFIK ALKDKEGKTL NNAHILGFFR
RICKFLFHNI KPVFVFDGAT PDLKINTIQT RRRRRIKRQE SVQRTAKKIL AAQIHLNALN
AIQSSTDENG NPINPNISPS SAKKKISNEM IKAIKLSNYE DRSRRDEYDL PPEPENVMDD
YRLASKNELN DLIRYDMDIN EIFDSKYFQS LPVDVQHKIV YEMKNKSRQN SYDRIERMIE
VASSALDFSK LQIKGAIYRN KLTEALLQFN REGSLFKGLS KNIASERNNE YILIKNDDKE
GGWSLKLENK DENREKTNLE NILSVEENFE DTLNKNRLGN KQNYTSASIY KRNDDKVVDL
LSDNTDSEDD DENIFDKFYK VGNDNENISS NQFSNKLKID SNNPLRNLRS EELLESSFTF
PLNKDFIQLN ENQENKNENE KENEKENEKN KKESENKEAN ILTTPERQKR FDDAIKKKLP
EITNGFLSQP YSLMRENDLD NLPSPLDISI NPKDPLMEKS EDDFIEYWID NATFDFKIEH
PDFFNIITDT VTEKPAEEIL KEWEGIYLDK INNKKLKHVK KEDDSDSDSD SDSDSDVAIV
DDDEKNDTHP VEETSEFFYE KFLLSTLKWK YNQLGQNEIP IQNKEIVTIS INENDSHRVD
KNIEINKILI FEDEDEDDMV IDNNDNYNID KINGKANEIS SNSFIDVDWD SVIIDSDHES
EKEVIDETNK PEKLSLGISI PIPHKNNENN NRNKNENNNE NLIKIKGESS WNNMDSFIDD
AFIEEEDEDD FLEKFYQQEK EKKKEKEPQI ISNYDFNQQL NKLKKYNESN KKENEKEENY
SKLLSRKRKL NNKENENNKK EEIKITEKLT SSPTKIDDDD DDDEVNFLLS PVIKKTKVNT
IENDSNLIKK ELQSLENLEE TNSNNKSVKD EKEKSESNLV DFNIKNDKNE DDKSQSSLFS
PISLVNSEND NLLDFKTESF PLSKLQTTND NKNNVIKNNE EILSSSLVLF SPKLEEDFMK
QKSPLENNKK NKNETKTETE IDTVQTNMNK NDINNDEIKN PSNLTQDREP EKKSIVKNKG
KEVMIEEDEK EDINIDEDDN NDFMVESQEY KFVAKSPIRP TNHFSSSSII IDSDSDDDFD
KELKQIENRN KNQAIASSSN SKVNIKNETL LISNNNNNNN NKLDSTIKND NPNNKNEIIN
INDEEEGDDD NNNNNVDEDD DDDRDSLIDV NTEIHDEDIE YARMISEISK KDISTIQNEL
EEEISNLKIE KIKEQKGSED ITSTMIYDCQ ELLRLFGIPY IVSPMEAEAQ CATLYSKKLV
DGIVTDDSDI FLFGGSEVYK NMFNQHQYVE CYKMSELEKE MKLNREKLIN MAYLLGSDYT
EGVKGFGIVH AMEIIKEWPG NDGLIEFKKW WENRILKGEI DPNENKLRKR IYKQCRRVDI
PDSFPDPQIK NAYLNPVCDE SDQAFVWGSP DLTSLKKFLN KKLLWDDNKI NNILVPIIKK
MEKNKMENNK DKKQTKLDQY FFNPKSIMES NKLHQSKRIK NVINQWSKKK
//
