ID A0A384BBJ4_BALAS Unreviewed; 1201 AA.
AC A0A384BBJ4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=DNA repair protein complementing XP-G cells isoform X1 {ECO:0000313|RefSeq:XP_007196858.1};
GN Name=ERCC5 {ECO:0000313|RefSeq:XP_007196858.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007196858.1};
RN [1] {ECO:0000313|RefSeq:XP_007196858.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007196858.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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}.
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DR RefSeq; XP_007196858.1; XM_007196796.2.
DR AlphaFoldDB; A0A384BBJ4; -.
DR STRING; 310752.A0A384BBJ4; -.
DR KEGG; bacu:103017632; -.
DR CTD; 2073; -.
DR InParanoid; A0A384BBJ4; -.
DR OrthoDB; 178636at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 NCBIfam; TIGR00600; rad2; 1.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
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:UP000261681}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 794..863
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 309..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 133827 MW; 03AE571773CEFE7B CRC64;
MGVQGLWKLL ECSGRQVNPE TLEGKVLAVD ISIWLNQALK GVRDRHGNSM ENAHLLTLFH
RLCKLLFFRI RPVFVFDGDA PLLKKQTLAK RRQRKDLATT DSKKTTEKLL KTFLKRQVIK
TALKSKREEA LPSLTQVQRE DDIYVLPPLQ EAEKNSSEEE DEKEWQERMN QKQALQEAFF
QNPHAVDIES EDFSSLPPEI KHEILTDMKE FTKRRRTLFE AMPEESNDFS QYQLKGLLKK
NYLNQHIENV QKEMNQQHSG QIQRQYEDEG GFLKEVESRR VVSEDTSHYI LIKGIQAKKV
AEVDSESLPS CSEMHSRSSD LKSSPCEKLE PKEEPDASPP SPRTLLAVQA VLLGGSSEDE
LESETCRLRH ERRAPATARA GSVSPLTLLA IQRALDDDDE DVTVRARSDV RTGGAGARKP
KPLQSSSDEE TEEGPKMRDG EGAPLAAASH AASVSLAEEP VTSADAEKER TESAHLPRTA
FCQGSDSSVP KEQMSSIPPV KEAFQTSDEA AVTDGKDPVP LENTVVLPRD APGLQSGPER
IPTPPSPSSV SRSGTHTKVL ELQQGLLLPP ESKYDTSVLS SDDETESEKN PAPEGTVSLQ
KSSDTLSVPL ETISDLGNVA SVNAEEHENF LKTIQEHETV ESAGQGLISV PASMEPTETD
SEESESDGSF IEVQSINSSD ELQAELHEAS RPPSGQDEEE PVGTEKQEAT GDSQGLPRDN
SEREAVDLEP PEETEKDADD LLNEWQDVDL EELETLESNL LTQQNSLKAQ KQQQERVAAT
VTGQMFQESQ ELLRLFGIPY IEAPMEAEAQ CAILDLTDQT SGTITDDSDI WLFGARHVYK
NFFNKNKFVE YYQYVDFHNQ LGLDRNKLIN LAYLLGSDYT EGIPTVGCVT AMEILNEFPG
HGLEPLLRFS EWWHEAQKNK KIRPNPYDTK VKKKLRKLQL TPGFPNLAVA DAYLKPVVDE
SKGSFLWGKP DLDKIREFCQ RYFGWNRMKT DESLFPVLKQ LNVQQTQLRI DSFFRLAQQE
KQEAKGIKSQ RLNRAVTCML RKEREEAASE IEAVSVAMEK DSEFLDEAKG KTQKRGTTNR
WKESSSPKRK RLSDSKRGHE CGGFLGEAYL SQSSDASSGG DEEYFPVANV QRGKAAVEST
VSSAGAQSTA RPAPGRDGGA ATSSSSDDGG EKAEPVLVTA RSVFGKKEGK RRSTRGRKRK
I
//
