ID K7ET21_PONAB Unreviewed; 1640 AA.
AC K7ET21;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000023689.2};
GN Name=BIVM {ECO:0000313|Ensembl:ENSPPYP00000023689.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000023689.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000023689.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000023689.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; K7ET21; -.
DR Ensembl; ENSPPYT00000032954.2; ENSPPYP00000023689.2; ENSPPYG00000005485.3.
DR eggNOG; KOG2520; Eukaryota.
DR GeneTree; ENSGT00510000048601; -.
DR InParanoid; K7ET21; -.
DR OMA; KNEPANP; -.
DR TreeFam; TF101235; -.
DR Proteomes; UP000001595; Chromosome 13.
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:UP000001595}.
FT DOMAIN 469..552
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1231..1300
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1640
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1640 AA; 184563 MW; F887D8289858100C CRC64;
MPNVAETERS NDSGNGEHKS ERKSPEDNLQ GAVKSFCTSA SGAPLGPKGD GHYPWSCPVT
HTREKIYAIC SDYAFLNQAT SIYKTPNPSR SSCLPDSTSL SAGNNSSRYI GIPNSTSEII
YNEENSLENL SNSLGKLPLA WEIDKSEFDG VTTNSKHKSG NAKKQFSKRK TSDKKGRYQK
ECPQHSPLED IKQRKVLDLR RWYCISRPQY KTSCGISSLI SCWNFLYSTM GAGNLPPITQ
EEALHILGFQ PPFEDIRFGP FTGNTTLMRW FRQINDHFHV KGCSYVLYKP HGKNKTAGET
ASGALSKLTR GLKDESLAYI YHCQNHYFCP IGFEATPVKA NKAFSRGPLS PQEVEYWILI
GESSRKHPAI HCKKWADIVT DLNTQNPEYL DIRHLERGLQ YRKTKKVGGN LHCIIAFQRL
NWQRFGLWNF PFGTIRQESQ PPTHAQGIAK SESEDNISKK QHGRLGRSFS ASFHQDSAWK
KMSNISIWLN QALKGVRDRH GNSVENPHLL TLFHRLCKLL FFRIRPIFVF DGDAPLLKKQ
TLVKRRQRKD LASGDSRKTT EKLLKTFLKR QAIKTAFRSK RDEALPSLTQ VRRENDIYVL
PPLQEEEKHS SEEEDEKEWQ ERMNQKQALQ EEFFHNPQAI DIESEDFSSL PPEVKHEILT
DMKEFTKRRR TLFEAMPEES NDFSQYQLKG LLKKNYLNQH IEHVQKEMNQ QHSGHIRRQY
EDEGGFLKEV ESRRVVSEDT SHYILIKGIQ AKTVAEVDSE SLPSSSKMHS MSFDMKSSPC
EKLKTEKEPD ATPPSPRTLL AMQAALLGSS SEEELESENR RQAHGRNAPA AVDEGSISPR
TLSAIQRALD DDEDVKVCAG DDVQTGGPGA EETHINSSTE DRDEGLKVRD GKGIPFTATL
ASSSVNSAEE HVASTNEGRE LTDSVPKEQM SLVHMGTEAF PISDESMVKD RKDQLPLESA
VVRHSDTLGL PNGRELTPAS PTCTNSVSKK ETHAEVLEQQ KELCPYESKF DSSVLSSDNE
TKCKPNSASE VIGPVSLQET SSIISIPSEA VANVENVVSF NAKEHENFLE TIQEQQTTES
AGQDLISIPK AVEPMEIDSE ESESDGSFIE VQSVISDEEL QAELPETSKP LSEQGEEELI
GTREEEAPAE SESLPRDHSE REDVDGEPQE AEKDAEDLLH EWQDINLEEL ETLESNLLAQ
QNSLKAQKQQ QERIAATVTG QMFLESQELL RLFGIPYIQA PMEAEAQCAI LDLTDQTSGT
ITDDSDIWLF GARHVYKNFF NKNKFVEYYQ YVDFHNQLGL DRNKLINLAY LLGSDYTEGI
PTVGCVTAME ILNEFPGHGL EPLLKFSEWW HEAQKNPKIR PNPYDTKVKK KLRTLQLTPG
FPNPAVAEAY LKPVVDDSKG SFLWGKPDLD KIREFCQRYF GWNRTKTDES LFPVLKQLDA
QQTQLRIDSF FRLAQQEKED AKHIKSQRLN RAVTCMLRKE REAAASEIEA VSVAMEKEFE
LLDKAKGKTQ KRGITNTLEE SSSLKRKRLS DSKGKNTCGG FLGETCLSES SDGSSSEDAE
SSSLMNVQGR RAAKEPKTSA SDLQNSVKEA PVKNGGATTS SSSDSDDDGG KEKMVLVTAR
SVFGKKRGKL RRARGRKRKT
//
