ID A0A1R1YAC5_9FUNG Unreviewed; 1386 AA.
AC A0A1R1YAC5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=DNA repair protein rad13 {ECO:0000313|EMBL:OMJ23891.1};
GN ORFNames=AYI70_g1954 {ECO:0000313|EMBL:OMJ23891.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ23891.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ23891.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ23891.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMJ23891.1}.
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DR EMBL; LSSN01000453; OMJ23891.1; -; Genomic_DNA.
DR STRING; 133412.A0A1R1YAC5; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; 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; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1020..1088
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 130..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 154428 MW; 58F93A368A7B0DAC CRC64;
MGVAGLWKIV NDDLKPIRLE VLEGKRLAID ASIWIHQFVK AMRDKSGIEI ENGHISGFFK
RICKLLHYGI LPIFVFDGAP PKIKKNTMAQ RRSRQNDQER RIKIAAGKLL SSKLKSHILK
DVIQSSIVNK NKDFDGTSPE PSKNIIKKLT PNSGGKRTRD EYELPGVDLN QEHGSIIGQI
KGNSPDIRLP TLEEAEASNF WGKIISDRKT ISGYETGIFD FDGDDSNLQS SSNQSNLDRI
NKSSEIDNIL KSIDIDSSEF LELPHDIQYA ILKELKDHSR QTSFKRLKSM VENSKTAMDF
SQMQLENLMK RNKFMQGYMG VSGAKHRIMS TKPVDGVKVS SVASQRDVQY ILIRSEGPTG
GWKLGAPNAK IDEYDSNESS PSNNNRIDLT HYSDDESKND KIFDFLSPSL KKNRNYQHHT
ELLNLDSSVN KNANSYTIDN TASTIQDSNT MTISSSDSDD FEDVKLPLDN QELLSSNETN
KTFTLSNTSS KMPIFKIPQS RKPEIKSISP KNSQSSQNDS PTTMKSKTIL QDSFFGSSSS
DLDDSDIDSG SMNSFFFDEL MAEKSSENTP ENIIPISKSI ESSTEKTGKI NLMKKLINNT
HLIPKKNNII AASSCKSGSI FEESDNEEDT ENIYENSTTI ESIPSIPDSK FIQGSANSSK
INPAINLDIP SETKSEYSSI EKPPTTFSID KPKASPNVTA QDIDDALDSS TIDLTSQPLE
VIEKEIQFNN GVDQFKYNED KTHGNINIVN PVEIKENSIK ILKPKIAHTL LSSNDIDLNL
DSPNTKNNDL IGANSNNSIL ISKLKTPIDI KPTESILVTE TKTEQNTIPL ENSSKYNDKP
EENANNFDIN NSEDFKSIKL ENREALTPIS ALEDKDSQAR RGAASEDHKN KVMTPSSKTL
PEIRSVNSDP NSIIKTPNSN PGDNYTPSKK YVFSPFSPSS VESLLSENSI EKKDFLFPSR
PNNSISDISP STSLISKFKS VHGDLSKQIE ENNRTLYQAR RDAAVSITDT ILDDIRTLLG
IFKIPYLTAP EEAESSCAIL EIKGHVDGVV TDDSDVLLFG AKNVYRNFFN QEKTVMKYEY
NGFSRTRLIF YSYFLGSDYT IGVNGIGPTT VSVIYSFFGT FRDAFRMSDK KVTNIGEVDV
PDKFKSLDLD KILFSDDPDE NETKSELLVT LLSHFYKFSK MSKESNLVVY KGAPKTLAKL
AALANKIEFP PGFPDIKISQ AYYNPSVIEV KQKKTFSGNF FKNKNLSKGS EHLNTLTSGD
QQVFENFEWG VPDLDLIQTY MFEKVDMGLE KVEKAVLPIV KKIIDRKQGA NGMSKSNTKL
FNKNMGKKTL FGNSSFNINN SLFGSSQSSS ANSSGSGTNR NGPLSQNSEN TGDNPKSKNN
TPSWFL
//
