UniProtKB - Q9GSR1 (DPOZ_DROME)
DNA polymerase zeta catalytic subunit
PolZ1
Functioni
As the catalytic subunit of the DNA polymerase zeta complex, plays a crucial role in translesion DNA synthesis (TLS) and various DNA repair mechanisms (PubMed:11267835, PubMed:16507570, PubMed:22532806, PubMed:15175013).
Lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function (PubMed:15175013).
During homologous recombination (HR) repair, has a overlapping role with the error-prone translesion polymerase eta to initiate repair synthesis which is completed by end joining or another polymerase that can bind and reinitiate synthesis (PubMed:22532806).
May participate in the Rrp1-dependent base excision repair (BER) pathway responsible for repair of DNA lesions that gives rise to apurinic/apyrimidinic (AP) sites (PubMed:16507570).
Unlike mammalian orthologs, it is not an error-prone polymerase (PubMed:15175013).
4 PublicationsCatalytic activityi
- EC:2.7.7.71 Publication
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 2041 | ZincBy similarity | 1 | |
Metal bindingi | 2045 | ZincBy similarity | 1 | |
Metal bindingi | 2054 | ZincBy similarity | 1 | |
Metal bindingi | 2057 | ZincBy similarity | 1 | |
Metal bindingi | 2086 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 2089 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 2098 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 2103 | Iron-sulfur (4Fe-4S)By similarity | 1 |
GO - Molecular functioni
- DNA binding Source: InterPro
- DNA-directed DNA polymerase activity Source: FlyBase
- iron-sulfur cluster binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- nucleotide binding Source: InterPro
GO - Biological processi
- DNA biosynthetic process Source: FlyBase
- DNA synthesis involved in DNA repair Source: FlyBase
- DNA synthesis involved in double-strand break repair via homologous recombination Source: FlyBase
- double-strand break repair via homologous recombination Source: GO_Central
- translesion synthesis Source: InterPro
Keywordsi
Molecular function | DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase |
Biological process | DNA damage, DNA repair, DNA synthesis |
Ligand | Iron, Iron-sulfur, Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-DME-110312, Translesion synthesis by REV1 R-DME-5655862, Translesion synthesis by POLK R-DME-5656121, Translesion synthesis by POLI |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:PolZ1Imported Synonyms:DmpolzetaImported, DNApol-zetaCurated, DNApolZ1Curated, mus2051 Publication, rev31 Publication ORF Names:CG1925Imported |
Organismi | Drosophila melanogaster (Fruit fly)Imported |
Taxonomic identifieri | 7227 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › |
Proteomesi |
|
Organism-specific databases
FlyBasei | FBgn0002891, PolZ1 |
VEuPathDBi | VectorBase:FBgn0002891 |
Subcellular locationi
Nucleus
- nucleus Source: GO_Central
Other locations
- zeta DNA polymerase complex Source: FlyBase
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 14 – 2130 | Missing in mus205; hypersensitive to alkylating agents and UV, but not sensitive to ionising radiation. In somatic cells, no effect on methyl methane sulfonate-induced mutations and homologous recombination. In germ cells, no effect on mutability by X-rays, NQO and alkylating agents. 1 PublicationAdd BLAST | 2117 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000448742 | 1 – 2130 | DNA polymerase zeta catalytic subunitAdd BLAST | 2130 |
Proteomic databases
PaxDbi | Q9GSR1 |
Expressioni
Developmental stagei
Gene expression databases
Bgeei | FBgn0002891, Expressed in female gonad and 18 other tissues |
ExpressionAtlasi | Q9GSR1, baseline and differential |
Interactioni
Subunit structurei
Catalytic subunit of the zeta DNA polymerase complex, which consists of PolZ1/DNApol-zeta and the accessory component PolZ2/Rev7 (PubMed:16507570, PubMed:15175013).
Interacts with the apurinic/apyrimidinic (AP) endonuclease Rrp1; the interaction is likely indirect and mediated via PolZ2 (PubMed:16507570).
2 PublicationsProtein-protein interaction databases
IntActi | Q9GSR1, 1 interactor |
STRINGi | 7227.FBpp0087907 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 528 – 635 | DisorderedSequence analysisAdd BLAST | 108 | |
Regioni | 734 – 891 | DisorderedSequence analysisAdd BLAST | 158 | |
Regioni | 927 – 954 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 1189 – 1243 | DisorderedSequence analysisAdd BLAST | 55 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 2086 – 2103 | CysB motifBy similarityAdd BLAST | 18 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 553 – 585 | Polar residuesSequence analysisAdd BLAST | 33 | |
Compositional biasi | 599 – 613 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 621 – 635 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 734 – 762 | Basic and acidic residuesSequence analysisAdd BLAST | 29 | |
Compositional biasi | 763 – 791 | Polar residuesSequence analysisAdd BLAST | 29 | |
Compositional biasi | 798 – 838 | Polar residuesSequence analysisAdd BLAST | 41 | |
Compositional biasi | 839 – 862 | Basic and acidic residuesSequence analysisAdd BLAST | 24 | |
Compositional biasi | 1189 – 1204 | Polar residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 1222 – 1243 | Polar residuesSequence analysisAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0968, Eukaryota |
GeneTreei | ENSGT00940000169521 |
HOGENOMi | CLU_000203_3_1_1 |
InParanoidi | Q9GSR1 |
OMAi | CYSELRG |
OrthoDBi | 20210at2759 |
PhylomeDBi | Q9GSR1 |
Family and domain databases
Gene3Di | 1.10.132.60, 1 hit 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro IPR006172, DNA-dir_DNA_pol_B IPR017964, DNA-dir_DNA_pol_B_CS IPR006133, DNA-dir_DNA_pol_B_exonuc IPR006134, DNA-dir_DNA_pol_B_multi_dom IPR043502, DNA/RNA_pol_sf IPR042087, DNA_pol_B_thumb IPR023211, DNA_pol_palm_dom_sf IPR030559, PolZ_Rev3 IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf IPR025687, Znf-C4pol |
PANTHERi | PTHR45812, PTHR45812, 1 hit |
Pfami | View protein in Pfam PF00136, DNA_pol_B, 1 hit PF03104, DNA_pol_B_exo1, 2 hits PF14260, zf-C4pol, 1 hit |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MAAAGEAIDG VYSVRLVIAD FYMEKPQFGM DPCYSELRGK EIKRVPVIRV
60 70 80 90 100
FGGNSRGQKT CMHVHGVFPY LYIPYDKKDF ESLERGILQM AMHLDKAINI
110 120 130 140 150
SLGQGSSNAQ HVFKIQLVKG IPFYGYHRVE HQFLKIYMFN PRFVRRAANL
160 170 180 190 200
LQSGAILSKN FSPHESHVPY ILQFMIDYNL YGMSYVHVPL EVLKFRRNHD
210 220 230 240 250
DDVIPYANVK QAQLLDITTA KKVACSALEV DVSSNFILNR FQLVAKSKSN
260 270 280 290 300
HTNPGIEAIW NDEKLRRQKL VEKHTDAGDE EKAEAVPVLE LPPTQERHQI
310 320 330 340 350
EIAESDIFYR TALESKLMTL EQSTLSEQTL SDQTILPQAT MQTTMPGTKA
360 370 380 390 400
QKRRFNLQKL LANAVYPEEC SQDQQQLLVN ASFIQNHVTC GYSSSVSLST
410 420 430 440 450
SKDESDDLDE TVVDEELILS LTQPHGAIPH DATLREEDLE LLDALQLLEE
460 470 480 490 500
QNESESHVDL DSSLAPLSQH KKFELTPELL DKETAATAAL FDEDVDSDED
510 520 530 540 550
ADQETRHDFS TVLDDVDELL LKLTQSQPAE SKELKASSKL PQIDGADDRL
560 570 580 590 600
QRTPIKSISS KSKSSPSKTP TTPIGQKSLP KSPRTPKTSA AKKYAPLALT
610 620 630 640 650
IGSSSSKKSN DEFAGRPSNP RLSLQLDQGT GTGTLRPEIS LRKKLAMSEM
660 670 680 690 700
RRKSFEDSFV LLKNDCTPVR STRRSTSNLD KTHIICSLTP RDRNPGLSDM
710 720 730 740 750
FETEDGKQLP PKKVVRKTRW STRNQDIESL PKAGCEIERP HRSEGSALDE
760 770 780 790 800
LKPRRSARHK VNSANPDECS SEIQTTGPRV TTTSLDRPQK KARLSQSPKE
810 820 830 840 850
NTKTSMNGTV ALEKATKDSS SNSESPHQQE NSVSEQIEYL ESKPKKSDET
860 870 880 890 900
ARSCDEKLQR ELIPQEPAGI SPGDSANSTE EITFSPCHDE AIESDTESDY
910 920 930 940 950
IVTKLRKTPN LKRLRWSIRS ELLNKQFTPS SGIRPPETET TPQLSPKSNE
960 970 980 990 1000
SNTPELMRSF YEHSLIVNSP SVFSDFLDSP EIHMDSPRSA PPSPDSNSFV
1010 1020 1030 1040 1050
IAPLELPPSY DEVVSGSRKM DIPEYEFQKP YYSNPSDVSK VTEVGFLVLH
1060 1070 1080 1090 1100
IPGNKLNDCD PFQSILGNDR GLASWRRRQL IAIGGLAMLQ RHRGEQKVRE
1110 1120 1130 1140 1150
YFSTQQRIAI EPAQLAPTWQ EAKIWLKAKE LLRQREEPKK SSDDIDSPIK
1160 1170 1180 1190 1200
IKRQKITMML QAEEGDGGSG DEDAGEELDC SLSLTPLSQA KDKCKATPTS
1210 1220 1230 1240 1250
SKARETGKSR LKRGTRLSFI GSQDEEPPSS QSSEQSVSSS AAQAELDRSS
1260 1270 1280 1290 1300
FLRQLEGSSQ DRQHDLSFGL SHATLDNTFG FKVNLENLQQ AKADIDCNHL
1310 1320 1330 1340 1350
TIITLEVFVS TRGDLQPDPM HDEIRCLFYA IEHSLPDEKL PSKACGYIMV
1360 1370 1380 1390 1400
NTVQDLLSEG PFHGIDRDIE VQVVTSEAEA FEALLALCER WDADIYAGYE
1410 1420 1430 1440 1450
IEMSSWGYVI DRAKHLCFNI APLLSRVPTQ KVRDFVDEDR EQFTDLDVEM
1460 1470 1480 1490 1500
KLCGRILLDV WRLMRSEIAL TSYTFENVMY HILHKRCPWH TAKSLTEWFG
1510 1520 1530 1540 1550
SPCTRWIVME YYLERVRGTL TLLDQLDLLG RTSEMAKLIG IQFYEVLSRG
1560 1570 1580 1590 1600
SQFRVESMML RIAKPKNLVP LSPSVQARAH MRAPEYLALI MEPQSRFYAD
1610 1620 1630 1640 1650
PLIVLDFQSL YPSMIIAYNY CFSTCLGRVE HLGGSSPFEF GASQLRVSRQ
1660 1670 1680 1690 1700
MLQKLLEHDL VTVSPCGVVF VKREVREGIL PRMLTEILDT RQMVKQSMKL
1710 1720 1730 1740 1750
HKDSSALQRI LHSRQLGLKL MANVTYGYTA ANFSGRMPSV EVGDSVVSKG
1760 1770 1780 1790 1800
RETLERAIKL VENNEEWKVR VVYGDTDSMF VLVPGRNRAE AFRIGEEIAK
1810 1820 1830 1840 1850
AVTEMNPQPV KLKLEKVYQP CMLQTKKRYV GYMYETADQE QPVYEAKGIE
1860 1870 1880 1890 1900
TVRRDGCPAV AKMLEKVLRI LFETQDVSKI KAYVCRQFTK LLSGRANLQD
1910 1920 1930 1940 1950
LIFAKEFRGL NGYKPTACVP ALELTRKWMQ KDPRHVPRRG ERVPFIIVNG
1960 1970 1980 1990 2000
PPGMQLIRLV RSPHDILANE GHKINAIYYI TKAIIPPLNR CLLLIGANVH
2010 2020 2030 2040 2050
DWFASLPRKL LMTPAVGTAN ELAGARGAKS TISQYFSTTS CVIDCGRQTK
2060 2070 2080 2090 2100
AGICPDCLKN ATTCVVVLSD KTARLERGYQ LTRQICQACC GRLGSLQCDS
2110 2120 2130
LDCPVLYVLE GKRRELQQIE HWNKLLEHHF
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 92 | M → V in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 339 | A → V in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 394 | S → N in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 536 | A → V in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 584 | R → H in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 677 | S → R in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 854 | C → R in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 887 | C → S in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1021 | D → G in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1176 | E → D in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1206 | T → R in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1213 | R → P in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1238 | S → F in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1524 | D → E in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1611 | Y → H in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 1852 | V → E in AAG30223 (PubMed:11267835).Curated | 1 | |
Sequence conflicti | 2025 | A → P in AAG30223 (PubMed:11267835).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF298215 mRNA Translation: AAG30223.1 AE013599 Genomic DNA Translation: AAF59191.2 AF298216 Genomic DNA Translation: AAG30224.1 AY058689 mRNA Translation: AAL13918.1 |
RefSeqi | NP_524881.2, NM_080142.3 |
Genome annotation databases
EnsemblMetazoai | FBtr0088831; FBpp0087907; FBgn0002891 |
GeneIDi | 47186 |
KEGGi | dme:Dmel_CG1925 |
UCSCi | CG1925-RA, d. melanogaster |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF298215 mRNA Translation: AAG30223.1 AE013599 Genomic DNA Translation: AAF59191.2 AF298216 Genomic DNA Translation: AAG30224.1 AY058689 mRNA Translation: AAL13918.1 |
RefSeqi | NP_524881.2, NM_080142.3 |
3D structure databases
AlphaFoldDBi | Q9GSR1 |
SMRi | Q9GSR1 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | Q9GSR1, 1 interactor |
STRINGi | 7227.FBpp0087907 |
Proteomic databases
PaxDbi | Q9GSR1 |
Genome annotation databases
EnsemblMetazoai | FBtr0088831; FBpp0087907; FBgn0002891 |
GeneIDi | 47186 |
KEGGi | dme:Dmel_CG1925 |
UCSCi | CG1925-RA, d. melanogaster |
Organism-specific databases
CTDi | 47186 |
FlyBasei | FBgn0002891, PolZ1 |
VEuPathDBi | VectorBase:FBgn0002891 |
Phylogenomic databases
eggNOGi | KOG0968, Eukaryota |
GeneTreei | ENSGT00940000169521 |
HOGENOMi | CLU_000203_3_1_1 |
InParanoidi | Q9GSR1 |
OMAi | CYSELRG |
OrthoDBi | 20210at2759 |
PhylomeDBi | Q9GSR1 |
Enzyme and pathway databases
Reactomei | R-DME-110312, Translesion synthesis by REV1 R-DME-5655862, Translesion synthesis by POLK R-DME-5656121, Translesion synthesis by POLI |
Miscellaneous databases
BioGRID-ORCSi | 47186, 0 hits in 3 CRISPR screens |
GenomeRNAii | 47186 |
PROi | PR:Q9GSR1 |
Gene expression databases
Bgeei | FBgn0002891, Expressed in female gonad and 18 other tissues |
ExpressionAtlasi | Q9GSR1, baseline and differential |
Family and domain databases
Gene3Di | 1.10.132.60, 1 hit 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro IPR006172, DNA-dir_DNA_pol_B IPR017964, DNA-dir_DNA_pol_B_CS IPR006133, DNA-dir_DNA_pol_B_exonuc IPR006134, DNA-dir_DNA_pol_B_multi_dom IPR043502, DNA/RNA_pol_sf IPR042087, DNA_pol_B_thumb IPR023211, DNA_pol_palm_dom_sf IPR030559, PolZ_Rev3 IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf IPR025687, Znf-C4pol |
PANTHERi | PTHR45812, PTHR45812, 1 hit |
Pfami | View protein in Pfam PF00136, DNA_pol_B, 1 hit PF03104, DNA_pol_B_exo1, 2 hits PF14260, zf-C4pol, 1 hit |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DPOZ_DROME | |
Accessioni | Q9GSR1Primary (citable) accession number: Q9GSR1 Secondary accession number(s): Q95TM2, Q9GSR2, Q9V319 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 11, 2019 |
Last sequence update: | March 1, 2001 | |
Last modified: | May 25, 2022 | |
This is version 185 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Drosophila annotation project |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Drosophila
Drosophila: entries, gene names and cross-references to FlyBase - SIMILARITY comments
Index of protein domains and families