DNA repair protein complementing XP-G cells homolog - Xenopus laevis (African clawed frog)

Preferred order of sections

Names and origin

Protein names

Recommended name:
DNA repair protein complementing XP-G cells homolog
EC=3.1.-.-

Alternative name(s):
Xeroderma pigmentosum group G-complementing protein homolog

Gene names

Name:	ercc5
Synonyms:	xpg, xpgc

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	1196 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too By similarity.
Cofactor	Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1196

1196

DNA repair protein complementing XP-G cells homolog

PRO_0000154033

Regions

Region

1 – 95

95

N-domain

Region

786 – 914

129

I-domain

Motif

936 – 952

17

Nuclear localization signal Potential

Motif

1079 – 1095

17

Nuclear localization signal Potential

Sites

Metal binding

30

1

Magnesium 1 By similarity

Metal binding

77

1

Magnesium 1 By similarity

Metal binding

822

1

Magnesium 1 By similarity

Metal binding

824

1

Magnesium 1 By similarity

Metal binding

843

1

Magnesium 2 By similarity

Metal binding

845

1

Magnesium 2 By similarity

Metal binding

894

1

Magnesium 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P14629 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 1F1CE1891A3C0623
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FASTA

1,196

134,207

        10         20         30         40         50         60 
MGVQGLWKLL ECSGRPINPG TLEGKILAVD ISIWLNQAVK GARDRQGNAI QNAHLLTLFH 

        70         80         90        100        110        120 
RLCKLLFFRI RPIFVFDGEA PLLKRQTLAK RRQRTDKASN DARKTNEKLL RTFLKRQAIK 

       130        140        150        160        170        180 
AALSGNKQSN EELPSFSQVP RKETEDLYIL PPLEDNENNS SEEEEEREWE ERMNQKQRLQ 

       190        200        210        220        230        240 
EDFFANPSSV DIESEEFKSL PPEVKHEILT DMKDFTKRRR TLFEAMPEDS SDFSQYQLKG 

       250        260        270        280        290        300 
LLKKNDLNKC IDNVRKELNQ QYSGEVQAQF ESEGGFLKEV ETRRLVSEDD SHYILIKGIQ 

       310        320        330        340        350        360 
SKQEEKKVDS PPQSITFNSS QTPKTYLDLK LASAHKTKPL QTSSAEAAPP SPRTLFAIQE 

       370        380        390        400        410        420 
AMAESWDHEK HEKPSVSGCE AEGNVSPRTL QAIYQVLAED EAGESNKIKV VLQSDEERKP 

       430        440        450        460        470        480 
KTKVLVISSS DEEDDCLNYQ DGTKTTLGAS LIKSISPSSM QCQESTADSL PNYTRSKPVS 

       490        500        510        520        530        540 
QIEEPMADHN LQGDNCNVPN AKDKLIVPPS LGNVDKPIIL SNTIPVNSEF RIPLLPVNMS 

       550        560        570        580        590        600 
MRETVIIPNN TGSLGSSRYI SLERDATKQG FSDNPVGDLV RSPDEPALNA SSALSDRKTS 

       610        620        630        640        650        660 
ATQSLLCNNI ECTEQSMVQG CSNTLDVTQT TQPSGGSEVN KPAEYNPQDK KVFGSNDSSA 

       670        680        690        700        710        720 
MYVPMTPESI IVSDEEFVNE KEDSDSDDSF IEVDSEFSTS NSQHVVFKEP GDTRETATNF 

       730        740        750        760        770        780 
QAVEEGNSGS QDIPLEHDSG EPHEQSNSEE SKDLDDVSNE WQDISVEELE SLENNLYVQQ 

       790        800        810        820        830        840 
TSLQAQQQQQ ERIAATVTGQ MCLESQELLQ LFGIPYIVAP MEAEAQCAIL DLTDQTSGTI 

       850        860        870        880        890        900 
TDDSDIWLFG ARHVYKNFFS QNKHVEYYQY ADIHNQLGLD RSKLINLAYL LGSDYTEGIP 

       910        920        930        940        950        960 
TVGYVSAMEI LNEFPGQGLE PLVKFKEWWS EAQKDKKMRP NPNDTKVKKK LRLLDLQQSF 

       970        980        990       1000       1010       1020 
PNPAVASAYL KPVVDESKSA FSWGRPDLEQ IREFCESRFG WYRLKTDEVL LPVLKQLNAQ 

      1030       1040       1050       1060       1070       1080 
QTQLRIDSFF RLEQHEAAGL KSQRLRRAVT CMKRKERDVE AEEVEAAVAV MERECTNQRK 

      1090       1100       1110       1120       1130       1140 
GQKTNTKSQG TKRRKPTECS QEDQDPGGGF IGIELKTLSS KAYSSDGSSS DAEDLPSGLI 

      1150       1160       1170       1180       1190 
DKQSQSGIVG RQKASNKVES SSSSDDEDRT VMVTAKPVFQ GKKTKSKTMK ETVKRK

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References

[1]	"Complementation of the DNA repair defect in Xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2." Scherly D., Nouspikel T., Corlet J., Ucla C., Bairoch A., Clarkson S.G. Nature 363:182-185(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X69977 mRNA. Translation: CAA49597.1.
PIR	S35994.
UniGene	Xl.39.
3D structure databases
ProteinModelPortal	P14629.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Xenbase	XB-GENE-960384. ercc5.
Phylogenomic databases
HOVERGEN	HBG051501.
Family and domain databases
InterPro	IPR020045. 5-3_exonuclease_C. IPR008918. HhH2. IPR006086. XPG-I_dom. IPR006084. XPG/Rad2. IPR001044. XPG/Rad2_eukaryotes. IPR019974. XPG_CS. IPR006085. XPG_DNA_repair_N. [Graphical view]
PANTHER	PTHR11081. PTHR11081. 1 hit. PTHR11081:SF1. PTHR11081:SF1. 1 hit.
Pfam	PF00867. XPG_I. 1 hit. PF00752. XPG_N. 1 hit. [Graphical view]
PRINTS	PR00853. XPGRADSUPER. PR00066. XRODRMPGMNTG.
SMART	SM00279. HhH2. 1 hit. SM00484. XPGI. 1 hit. SM00485. XPGN. 1 hit. [Graphical view]
SUPFAM	SSF47807. 5_3_exo_C. 1 hit.
TIGRFAMs	TIGR00600. rad2. 1 hit.
PROSITE	PS00841. XPG_1. 1 hit. PS00842. XPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ERCC5_XENLA

Accession

Primary (citable) accession number: P14629

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents