DPOLA_LEIDO
ID DPOLA_LEIDO Reviewed; 1339 AA.
AC O00874;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DNA polymerase alpha catalytic subunit;
DE EC=2.7.7.7;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/IN/80/DD8;
RX PubMed=9168968; DOI=10.1006/bbrc.1997.6583;
RA Luton K., Johnson A.M.;
RT "Cloning and sequence analysis of the DNA polymerase alpha gene of
RT Leishmania donovani: comparison with the human homologue.";
RL Biochem. Biophys. Res. Commun. 234:95-100(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; U78172; AAC47538.1; -; Genomic_DNA.
DR PIR; JC5508; JC5508.
DR AlphaFoldDB; O00874; -.
DR SMR; O00874; -.
DR PRIDE; O00874; -.
DR VEuPathDB; TriTrypDB:LdBPK_161640.1; -.
DR VEuPathDB; TriTrypDB:LdCL_160021400; -.
DR VEuPathDB; TriTrypDB:LDHU3_16.1960; -.
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; 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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 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..1339
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000046433"
FT ZN_FING 1179..1216
FT /note="CysA-type"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1243..1271
FT /note="CysB motif"
FT BINDING 1179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1339 AA; 150465 MW; 977332725EFF6F51 CRC64;
MSGGNDGASW RLSRKPNAPN FDETQEDQWR SLREEVLQSD EDENIPESGD LTIPQLPSAK
KAAKKLRKPP SGAKPTPKPK QQTLAQSMSD MDMERLLKRY RIDEDIDIAE DIDMSHLLQL
HSDSDDGGDA QEATLTADEF LARLARAEAA PAASIAKEKR ESGENVTVVA LKDELFNVER
DQSAKPPRPR PTPGAGGGAG YRNEETPKQA IELTATLAPQ MDAAQFVSPA VPYKSGEMTE
GLFYWFDARE QPHTLSVDPG SLFLFGKMAV EKNGRTSYLS CCVRVRNMYR SVFVLPKAGS
SQEDVVKEIN DICRNQGIEQ RRIKFVERYY AFEVPGVPHE KTQWAKLRYP GRYPPLNAKG
PFRHILIIMG ASSSLLELFL IKRKLKGPSF LRISGLVASA NRISHCALEF SVESPKNLRA
EDTKLPVPPF TLASIQIHTQ LDSKGACNEI LIASVAIYKD VNIENTIRYI PDNILTGVRP
ASMSTPLPID LESYCSAKGL PGVRRFANER ALLDWLAQQL GKIDADMMIG HNFLGFTLDI
LLRRYQELSI SSWSTIGRLD LKRLPRFQGT ATNVNQEKET CIGRLVVDSY SLSREHYKTV
NYRLLSLADQ MQLQGITKGS NNFEPGTSVL TPAMLSASRD IYDVLLQVCN CAVLSTAVVS
HLDVIRLTKR LTTIAGNLWS RTLFGARSER IEYLLLHTFH DLKFITPDRY VQNFKRGRDD
EEEEDGKRKA KYQGGMVLDP KCGLYSDYIL LLDFNSLYPS LIQEFNICFT TVDRESGSEI
DVPPPENLIC ASCAAAGLSA PCLHKCVLPK VIKSLVDSRR EVKRLMKIEK DANNLALLEI
RQKALKLTAN SMYGCLGFEY SRFHAQPLAE LVTRQGRLAL QSTVDLIPQL NPSLRVIYGD
TDSVMIQTGI KNDIKAVRDL GLDLKAKINK RYQSLEIDID GVFRAILLLK KKKYAALTVT
DWQGEGKTYK KEVKGLDMVR RDWCPLSKCV CDSVLSRVLN AEGSEDILDY VMNYMRDVSE
KVRAGRYTLD NFVISKSLTK EPEAYRGNSF PHATVALRMK QRKELVRVGD LIPYVICTGD
RLSDKAFHVE EVRQNSQLQI DSEWYLSVQI YPPVMRLCEH IQGFSNAQLS EAMGIACHTG
AKLEEEEAET MNDFSHSSLF QSRNLEECFP AALSLQVACT HCRLMTPINP HTRVMEVLAD
QERQRDRFDL YVCVSCRKSL PVDYVANCFT QTCYGIIRQF YQCGSAAAVK AVRTQFTYYR
ALFDVPHAPG CPARVKDAHY YQARRCLGVD RRLYTLAEAA DPAVQEVADP VDPLNAAAET
IYKRIDHLFI NLDSLFAGI
