DPOLA_OXYTR
ID DPOLA_OXYTR Reviewed; 1513 AA.
AC Q27152;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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 Oxytricha trifallax (Sterkiella histriomuscorum).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Sterkiella.
OX NCBI_TaxID=94289;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9302325; DOI=10.1007/pl00006234;
RA Hoffman D.C., Prescott D.M.;
RT "Phylogenetic relationships among hypotrichous ciliates determined with the
RT macronuclear gene encoding the large, catalytic subunit of DNA polymerase
RT alpha.";
RL J. Mol. Evol. 45:301-310(1997).
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}.
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DR EMBL; U59426; AAB57771.1; -; Genomic_DNA.
DR PIR; T28158; T28158.
DR AlphaFoldDB; Q27152; -.
DR SMR; Q27152; -.
DR PRIDE; Q27152; -.
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..1513
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000046435"
FT ZN_FING 1344..1373
FT /note="CysA-type"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1404..1427
FT /note="CysB motif"
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 1347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
SQ SEQUENCE 1513 AA; 173059 MW; 4DF832EDCFC4416E CRC64;
MFHLLLENEE IQFSNSFAQF YLQVDEAKKI FDEIDDDEYD KIQDQRKNDD FIVDDDGYGY
RDHGGEIWER DDHPEDGGKK KKKSSMYVFS FSPKFIAQPL FLQPNEQSIT AFMKPKSTIN
RPGAVTNSSA QIKQKPKVSA EQSKDIMNNL FQELDSKDVD ELQDVNNSAV VTELNKPIAF
NQNDMLTSKY AVTLETRQEV EQKRVTEQIQ AQAQIGQNQQ SSNPFSKKRK FEEISTNQNA
NASDSKRVSN QTNDNLNKVE TQVISMLKVA NPQIKVTSKL ARMDDSMKID QTSAQKNQIE
QTVNHSKLQR YNQNQMMSGI KLDNRTSKPI RNLEIWNQVL ANTQEFPLPL NENGTLSFYW
IDAHEENNGT DLYIFGKIYQ PQMRQFVSCS MKVNGMQREL YALPKMRGKA RGALTVEEEK
QQVRAVMMEL DDIRKKRFPQ ISKWRCKPVN RKYAFEMPIQ HGEHQFLKIK YDSTMPPLPS
TIQGNTFECI FGSTQSMLEL FILKRKIRGP CWMTIKNPTK VTDFKKTWCR QGIVIDNPKN
VEVTLEDLNK QELPPLTSLT FSFKTTRAQQ NTNEIAMISC LINTNIAQEG PSQVERTQSF
TLLRKLDGKP MPYDFDQKVK QRKENIIQKF ENERQMIEAF IAKVFIVDPD LVVAHNLCGG
MFDLLLARIQ YLKVNHWSRI GRLKKTQIPN KKLDFGGSSY GGSQWIPRQV TCGRLLVDTF
LSAKELVRET SYDLTYLAKV QLKKDRQDFD DELLPTLYIT SERLFSLIDH TEKDAYLTIQ
LMNHLAIIPL TLQLTNIAGN LWFRSLQNAR AERNEMLLLH EFKKKKFILP DKKAPFAKDF
KRNMFADEFE ELKSGKGPKK GGKRKKAAYA GGLVIEPKAG FYDNIILLLD FNSLYPSIIQ
EYNLCFTTVN RRPTKNFDGS EVKSQFKAAG TDANEGNEVE EADLPDKNVN VKDAVLPNVL
RDLVQKRKAV KEKMKNEKDA VKLSQLEIRQ KAIKLTANSM YGCLGFGSSR FHAQAIAALI
TKTGRDTLLR TKDIAENKLG FNVVYGDTDS IMINTGTNQL QQSLEMGKRP QGLKLIALYK
CLEIEIDGVF KSLLLLKKKK YAALKYEGFG TPDAKVVQEV KGLDMVRRDW CPLSKNVGNF
VLNQILSGKQ REDVVLNLNE YLSDIGEKMK NNGITLDQFI ITKQLTKAIS EYSDIKGQPH
VAVAQRLKNQ GKSESDLVNN FIPYVIGAQP FDPSKTNPAL AGKAYHPEEV VSSKGKILLD
IEWYITMQVL PPITRLIEHI DGIDVEFVAQ CLGVDPKKYK YHSSEKKTGE TNNDDGTLIQ
NPILQTETER SLKGRTIAEL TIKCPHCSES YHFPGIFQDG KNNTLSGLLC IKCTQPIPEA
YIQNRVTLFL KQLLTLYYQG NKQCQEPACG AVSRQLLYNN KCINLACKLK NDTRYTEQKT
NDTLRYLQGL FNVKKYIQEN QKNGCVHKTV EEVPNFDAFA RMQGKVDDIM IRSKYNKVDL
SSIFNFMKLG KQQ
