ID   A0A194S4Y1_RHOGW        Unreviewed;       816 AA.
AC   A0A194S4Y1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=PIN domain-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RHOBADRAFT_53535 {ECO:0000313|EMBL:KPV75570.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV75570.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV75570.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV75570.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ474078; KPV75570.1; -; Genomic_DNA.
DR   RefSeq; XP_018271619.1; XM_018416884.1.
DR   AlphaFoldDB; A0A194S4Y1; -.
DR   STRING; 578459.A0A194S4Y1; -.
DR   GeneID; 28977332; -.
DR   OMA; VIECERQ; -.
DR   OrthoDB; 1430882at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR   CDD; cd09897; H3TH_FEN1-XPG-like; 1.
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; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11081:SF74; XPGN DOMAIN-CONTAINING PROTEIN; 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:UP000053890}.
FT   DOMAIN          1..118
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          481..561
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          261..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..816
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   816 AA;  85264 MW;  8A18150524DCE23C CRC64;
     MGVRDLGKII KARSPSSVTT YTSLAPFRGK RFAIDANLLT TKFHYAEAGT RPPDARLGGG
     APLGDGKGGG HSHARAWYWF LEALRKHGIH PVVVFDGDTR LAAKAPENER RRDARALQGA
     RAAAEGGRGA RLREVEAVMA RIADDERPAV VEGFRHVVER MWSRRDGSGG GELVPAVAAT
     GGEGSSAAAA AAAVEQRVSL TQIEALLAQD RQEVPPSSAP AGARPLVAPA EPLPLEAADS
     ATAAASKAAI RDIDRLLDVE QAPASAPASP STDPLPTTAD EPHPSPLANL ADADVSPSER
     PPLAHSPDVP PTVAVSPPIS PEAALSPSLA AALAASRLAN TAKLTSLAGP GPAASHGAIV
     AHVVALATLF AEYRADVLNP VYSRNQARVT EDEGRFFEGL LRYGTPAEAA ETAVAAASDA
     ASEDGRELGE KEEEEESPVP PTKDAELGDI IAQSDKYFDS HLKRSDGVPR AAFKEVRRLV
     AALGVPYLEP SPHDPHEAEG VCAALCTLGH ADYVVSEDLD AAVYGAPLLR FVTVTPAGTG
     REPKKPMTVL DPARLRDDLG LTRAEFVDFA LLCGTDFTDR VYKVGPVLAH KLIVTHSTIE
     RALAANDAGL KPALVLPEAM DREAYLERIR AARAIFNGVP QLPLPLAPSS SSTDSSSLSE
     PSSSSSTPSP STFLGSLTPS PPSPILPALL RSYGIHRSRH LSSRGTATAS PALSAALDDA
     DVDVDLGEDV DDVARGRELD ELEGAESGSS GLGLGLDEWA RAQEALDAAL VDDGDVLGQE
     WDGAVAGQED EGSEGEGGEG REPARSVSDE FERLYL
//