DPOLA_STENO
ID DPOLA_STENO Reviewed; 1492 AA.
AC Q94636;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA polymerase alpha catalytic subunit;
DE EC=2.7.7.7;
OS Sterkiella nova (Ciliate) (Oxytricha nova).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Sterkiella.
OX NCBI_TaxID=200597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8039700; DOI=10.1016/0378-1119(94)90373-5;
RA Mansour S.J., Hoffman D.C., Prescott D.M.;
RT "A gene-sized DNA molecule encoding the catalytic subunit of DNA polymerase
RT alpha in the macronucleus of Oxytricha nova.";
RL Gene 144:155-161(1994).
CC -!- FUNCTION: Polymerase alpha in a complex with DNA primase is a
CC replicative polymerase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC beta, gamma, delta, and epsilon which are responsible for different
CC reactions of DNA synthesis.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U02001; AAA21587.1; -; Genomic_DNA.
DR PIR; T18560; T18560.
DR AlphaFoldDB; Q94636; -.
DR SMR; Q94636; -.
DR PRIDE; Q94636; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 1.10.3200.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1492
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000046434"
FT ZN_FING 1314..1344
FT /note="CysA-type"
FT REGION 34..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1375..1398
FT /note="CysB motif"
FT COMPBIAS 34..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
SQ SEQUENCE 1492 AA; 171825 MW; CEF02003A6DB279A CRC64;
MIKHILQVEE TKKIFEEIDD NEYEKIQDSR KNDDFIVDDD GYGYRDHGGE IWDRDGDVEE
VGKKKKKKQN NHDPNENIMN YMMPASTLKK KSNAASTNPS AQQKPKVSVE QSRDIMNNLF
QQLDAKDVDE LEDVNEAKNM FVQEMNRPVA FNKEEDFNNR YSVTLESREE QERRRQSEQL
KQQANIGQNQ SDVNPFSKKR KLDEFQQVQA NSYQSKQNSH SVSKSKPGDH EMANHADGVD
LNLLAIDDTK MTDSHPSEII TQNQRASAVS SVNQQIMEST NGKNQLEKND TEWQQMKEKN
AVFNQDLRMN DNALMSNQQD YPLPLNEDGT LSFYWIDAHE ENNGADLFVF GKIYQHEERK
FVSCSIKVNG MQRELFVLPK MSGKSRAAMT TEEEKEQARK VMMELEGVRK RFPAITKWRC
KPVTRKYAFE LPIQHGEHQF VKIKYDATFP SLPSTVQGNT FECIFGANQS MLESFILKRK
IRGPCWMTIR NPQKVTDFRR TWCKQEILVS NPKDIEITLD DLNKTELPPL TSVTFAIKTC
RSSQNTNEIA MLSCIVNENI SQEGPSKIDV HKSFTLLRKL DGKPMPIEYE RAFRDKKDSF
IQFFQHERQL IEAFVAKIYQ LDPDLMVAHN LCGGMFDLLL ARIQMLKISH WSRIGRLKKN
QIPNKKSDQS GANYGGSQWI PRQVTCGRLL VDTFLTAKEL IRETNYDLTH LAKVQLQKDR
IDFDDDLLPT FYVQMAKLFQ LIDHTEKDAY LTLQLMNHLQ VIPLTKQLTN IAGNLWFRSL
QNARAERNEM LLLHEFKKKK FVLPDKKQLN AKDLKKNMFA DEYEEGDGKT KGGKRKKAAY
AGGLVIEPKA GFYDNIILLL DFNSLYPSII QEYNLCFTTV NRRPTKNFDG SEMKNQYKKG
ENGEEEVDIE EADLPDKNVN LKDAVLPMVL RDLVQKRKAV KDKMKTEKDH VKLSQLEIRQ
KAIKLTANSM YGCLGFGSSR FHAQAIAALI TRTGRETLLR TKDIAENKLG FNVVYGDTDS
IMINTGSNQL QQALEMGKRL KGEVNCLYKC LEIEIDGVFK SLLLLKKKKY AALKYENFLS
PAEVKVVQEM KGLDMVRRDW CPLSKRVGRY VLDQILSGKQ REEVVLNLNE FLSNIGNELK
EGTIKLNEFI ITKQITKAIS DYNDIKGQPH VAVAKRLRDQ GKSENQLVNN FIPYVICQQT
YGDTTKSSTA LSDKAYHPDE VISSRGKVTI DSDWYVSTQL LPPITRLIEH IEGIEVEFVA
QCLGLDPKKY RYHSEKKNTD NPTDDPLIVS NPVLQTETER SLKNRTVAEL NIKCPHCAHN
YHFPGILVPS SNNTELTGLA CVKCNQRIPD AYMLNRLNLF LKQLTALYYL GMKECKEPQC
GMKTNQLLLN NKCIVKGCKG KMNSEYSELR INDTLRYLEG LFNVKKFLIE NEKYRKKYEK
PELVPNFQSF KELQKKVESF MIRSGYNKVD LGNIFGFMSK GANPHQQKMS IF
