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Protein

DNA polymerase alpha catalytic subunit

Gene

DNApol-alpha180

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polymerase alpha in a complex with DNA primase is a replicative polymerase. In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.1 Publication

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Degradation of single-stranded DNA. It acts progressively in a 3'- to 5'-direction, releasing nucleoside 5'-phosphates.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1296ZincBy similarity1
Metal bindingi1299ZincBy similarity1
Metal bindingi1324ZincBy similarity1
Metal bindingi1329ZincBy similarity1
Metal bindingi1362Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1367Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1385Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1388Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1296 – 1327CysA-typeAdd BLAST32

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair, DNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-174430. Telomere C-strand synthesis initiation.
R-DME-68952. DNA replication initiation.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69091. Polymerase switching.
R-DME-69166. Removal of the Flap Intermediate.
R-DME-69183. Processive synthesis on the lagging strand.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha catalytic subunit (EC:2.7.7.7)
Gene namesi
Name:DNApol-alpha180
Synonyms:DNApol-alpha, POLA
ORF Names:CG6349
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0259113. DNApol-alpha180.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL6039.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000464321 – 1488DNA polymerase alpha catalytic subunitAdd BLAST1488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei239Phosphoserine1 Publication1
Modified residuei262Phosphoserine1 Publication1
Modified residuei269Phosphoserine1 Publication1
Modified residuei314Phosphothreonine1 Publication1
Modified residuei317Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP26019.
PRIDEiP26019.

PTM databases

iPTMnetiP26019.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Highest level of zygotic expression seen in second-instar larva, level is reduced at other stages of development.1 Publication

Gene expression databases

BgeeiFBgn0259113.
GenevisibleiP26019. DM.

Interactioni

Protein-protein interaction databases

BioGridi67519. 14 interactors.
DIPiDIP-23937N.
IntActiP26019. 6 interactors.
MINTiMINT-206832.
STRINGi7227.FBpp0083514.

Chemistry databases

BindingDBiP26019.

Structurei

3D structure databases

ProteinModelPortaliP26019.
SMRiP26019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni638 – 758Contains conserved residues essential for 3' -> 5' exonuclease activitiesAdd BLAST121
Regioni675 – 734DNA-binding regionSequence analysisAdd BLAST60
Regioni1255 – 1380DNA-binding regionSequence analysisAdd BLAST126

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 103Nuclear localization signalSequence analysis8
Motifi1362 – 1388CysB motifAdd BLAST27

Domaini

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1296 – 1327CysA-typeAdd BLAST32

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
GeneTreeiENSGT00550000074891.
InParanoidiP26019.
KOiK02320.
OMAiFCVVSKP.
OrthoDBiEOG091G00RR.
PhylomeDBiP26019.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 1 hit.
InterProiView 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.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom_sf.
IPR012337. RNaseH-like_sf.
IPR036397. RNaseH_sf.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
PfamiView protein in Pfam
PF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
PRINTSiPR00106. DNAPOLB.
SMARTiView protein in SMART
SM00486. POLBc. 1 hit.
SUPFAMiSSF53098. SSF53098. 2 hits.
PROSITEiView protein in PROSITE
PS00116. DNA_POLYMERASE_B. 1 hit.

Sequencei

Sequence statusi: Complete.

P26019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESPSEPRA KRQRVDKNGR FAAMERLRQL KGTKNKCKVE DQVDDVYDVV
60 70 80 90 100
DEREYAKRAQ EKYGDDWIEE DGTGYAEDLR DFFEDEDEYS DGEEDRKDSK
110 120 130 140 150
KKKGVAPNSK KRPRENEKPV TGKASIKNLF SNAVPKKMDV KTSVKDDDIL
160 170 180 190 200
ADILGEIKEE PAATSEKAEK VIAPAKISVT SRKFDAAAAK EYMNSFLNNI
210 220 230 240 250
KVQEQERKKA EASSDNEMLE RILKPKAAVP NTKVAFFSSP TIKKEPMPEK
260 270 280 290 300
TPAKKATEDP FSDNEMDFSC LDDDENQFDV EKTQQTEKVS QTKTAAEKTS
310 320 330 340 350
QSKVAEKSAP KKETTGSPKE SESEDISRLL NNWESICQMD DDFEKSVLTT
360 370 380 390 400
EQDSTISSDQ QLRFWYWEAY EDPVKMPGEV FLFGRTADGK SVCLRVQNIN
410 420 430 440 450
RVLYLLPRQF LLDPISKEPT KQKVTVADIY KEFDSEVANQ LKLEFFRSRK
460 470 480 490 500
VTKSFAHHAI GIEVPQSCDY LEVHYDGKKP LPNLSADKKY NSIAHIFGAT
510 520 530 540 550
TNALERFLLD RKIKGPCWLQ VTGFKVSPTP MSWCNTEVTL TEPKNVELVQ
560 570 580 590 600
DKGKPAPPPP LTLLSLNVRT SMNPKTSRNE ICMISMLTHN RFHIDRPAPQ
610 620 630 640 650
PAFNRHMCAL TRPAVVSWPL DLNFEMAKYK STTVHKHDSE RALLSWFLAQ
660 670 680 690 700
YQKIDADLIV TFDSMDCQLN VITDQIVALK IPQWSRMGRL RLSQSFGKRL
710 720 730 740 750
LEHFVGRMVC DVKRSAEECI RARSYDLQTL CKQVLKLKES ERMEVNADDL
760 770 780 790 800
LEMYEKGESI TKLISLTMQD NSYLLRLMCE LNIMPLALQI TNICGNTMTR
810 820 830 840 850
TLQGGRSERN EFLLLHAFHE KNYIVPDKKP VSKRSGAGDT DATLSGADAT
860 870 880 890 900
MQTKKKAAYA GGLVLEPMRG LYEKYVLLMD FNSLYPSIIQ EYNICFTTVQ
910 920 930 940 950
QPVDADELPT LPDSKTEPGI LPLQLKRLVE SRKEVKKLMA APDLSPELQM
960 970 980 990 1000
QYHIRQMALK LTANSMYGCL GFAHSRFFAQ HLAALVTHKG REILTNTQQL
1010 1020 1030 1040 1050
VQKMNYDVVY GDTDSLMINT NITDYDQVYK IGHNIKQSVN KLYKQLELDI
1060 1070 1080 1090 1100
DGVFGCLLLL KKKKYAAIKL SKDSKGNLRR EQEHKGLDIV RRDWSQLAVM
1110 1120 1130 1140 1150
VGKAVLDEVL SEKPLEEKLD AVHAQLEKIK TQIAEGVVPL PLFVITKQLT
1160 1170 1180 1190 1200
RTPQEYANSA SLPHVQVALR MNRERNRRYK KGDMVDYVIC LDGTTNAAMQ
1210 1220 1230 1240 1250
RAYHLDELKT SEDKKLQLDT NYYLGHQIHP VVTRMVEVLE GTDASRIAEC
1260 1270 1280 1290 1300
LGMDPTKFRQ NAQRTQRENT EQSEGESLLK TTLQLYRLCE PFRFQCVTCK
1310 1320 1330 1340 1350
TEQLMASAYR PGPSNSHIAV LQQCAKSECQ TAPIQYLASV RNQLQLSMRQ
1360 1370 1380 1390 1400
YVQRFYKNWL VCDHPDCNFN TRTHSLRKKS HRPLCQKCRS GSLLRQYTER
1410 1420 1430 1440 1450
DLYNQLCYLR FMFDLGKQTL QQKPTLTPEL EQAYQLLYET VDQQLQSSSY
1460 1470 1480
VIISLSKLFA RSLAQMSLQP SVAQPQIEAI PSALADVV
Length:1,488
Mass (Da):169,903
Last modified:March 15, 2004 - v2
Checksum:i76C65EE2E2D5B065
GO

Sequence cautioni

The sequence AAL48000 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA14340 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAA32745 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti99S → L in S48157 (PubMed:1429896).Curated1
Sequence conflicti117E → A in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti117E → A in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti137K → KK in S48157 (PubMed:1429896).Curated1
Sequence conflicti148D → DD in S48157 (PubMed:1429896).Curated1
Sequence conflicti200I → M in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti200I → M in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti210 – 227AEASS…LKPKA → RRPVAITRCWSAFSPRQ in S48157 (PubMed:1429896).CuratedAdd BLAST18
Sequence conflicti364F → L in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti364F → L in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti376M → I in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti376M → I in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti379E → Q in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti379E → Q in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti478K → N in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti478K → N in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti739E → G in S48157 (PubMed:1429896).Curated1
Sequence conflicti818 – 819FH → ST in BAA14340 (PubMed:1923767).Curated2
Sequence conflicti818 – 819FH → ST in BAA32745 (PubMed:9858578).Curated2
Sequence conflicti819H → Y in AAL48000 (PubMed:12537569).Curated1
Sequence conflicti842A → R in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti842A → R in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti881F → L in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti881F → L in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti897 – 898TT → NP in BAA14340 (PubMed:1923767).Curated2
Sequence conflicti897 – 898TT → NP in BAA32745 (PubMed:9858578).Curated2
Sequence conflicti992 – 993EI → D in BAA14340 (PubMed:1923767).Curated2
Sequence conflicti992 – 993EI → D in BAA32745 (PubMed:9858578).Curated2
Sequence conflicti1155 – 1157EYA → DYR in BAA14340 (PubMed:1923767).Curated3
Sequence conflicti1155 – 1157EYA → DYR in BAA32745 (PubMed:9858578).Curated3
Sequence conflicti1178R → L in S48157 (PubMed:1429896).Curated1
Sequence conflicti1187 – 1189YVI → LCD in BAA14340 (PubMed:1923767).Curated3
Sequence conflicti1187 – 1189YVI → LCD in BAA32745 (PubMed:9858578).Curated3
Sequence conflicti1197 – 1205AAMQRAYHL → WPCSEHTIS in S48157 (PubMed:1429896).Curated9
Sequence conflicti1222 – 1223YY → LL in S48157 (PubMed:1429896).Curated2
Sequence conflicti1292 – 1310FRFQC…ASAYR → SASSALPVRRSSWRLRTD in S48157 (PubMed:1429896).CuratedAdd BLAST19
Sequence conflicti1325 – 1351AKSEC…SMRQY → VSPSAKRHRFSTWQACAILQ LSM in BAA14340 (PubMed:1923767).CuratedAdd BLAST27
Sequence conflicti1392S → T in S48157 (PubMed:1429896).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90310 Genomic DNA. Translation: BAA14340.1. Sequence problems.
S48157 mRNA. No translation available.
AB011813 Genomic DNA. Translation: BAA32745.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55908.2.
AY070529 mRNA. Translation: AAL48000.1. Different initiation.
PIRiS28079.
RefSeqiNP_536736.2. NM_080488.3.
UniGeneiDm.1592.

Genome annotation databases

EnsemblMetazoaiFBtr0084115; FBpp0083514; FBgn0259113.
GeneIDi42553.
KEGGidme:Dmel_CG6349.

Similar proteinsi

Entry informationi

Entry nameiDPOLA_DROME
AccessioniPrimary (citable) accession number: P26019
Secondary accession number(s): O77034, Q8T992, Q9VD90
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: November 22, 2017
This is version 172 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families