ID W5M1E0_LEPOC Unreviewed; 1486 AA.
AC W5M1E0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002197.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002197.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; AHAT01003330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015196960.1; XM_015341474.1.
DR STRING; 7918.ENSLOCP00000002197; -.
DR Ensembl; ENSLOCT00000002202.1; ENSLOCP00000002197.1; ENSLOCG00000001836.1.
DR GeneID; 102689247; -.
DR KEGG; loc:102689247; -.
DR CTD; 5422; -.
DR eggNOG; KOG0970; Eukaryota.
DR GeneTree; ENSGT00550000074891; -.
DR HOGENOM; CLU_001718_0_0_1; -.
DR InParanoid; W5M1E0; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 5477697at2759; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000001836; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF90234; Zinc finger domain of DNA polymerase-alpha; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 43..104
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 436..734
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 799..1251
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1291..1479
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 167220 MW; DB32F62AF9CCCFC1 CRC64;
MAPVSTSDKD ADNHDGDAGD SCGIAVSRSR REKKEKTGRR SALEQLKRAK KGEKVKYEVE
ELTSVYEEVD EEQYSRLVRE RQDDDWIIDD DGTGYVEDGR EIFDEDLDGD ALDRAPRGKG
GDRSTGSKER KSVKKAAVSK PSSIKSMFMA NSAKSKEKDV DLSKDDLLGD LLQDLHSEKS
PVLTPPPVIA LKKKKPAGVP PNPFSVRTPT PKAPAVTPSR PVSSAGRRAA ADLCPGARAR
IAPLETPDTA DAKRVKVEEQ ELPQAGGAAA DLVFDEGDFD EPMEEGDEGA AGGSSTAEVK
EELEPRAAVK EEVERPDGAL QRAAAAPEAS CWERMEGDGG TEPAVDVQVD SSRLPLVVGP
DGEQVFRFYW LDAFEDQYNQ PGVVYLFGKV WIEPAQAHVS CCVAVKNVER SMYILPREHK
VNLKTGEESD VRVTMMDVYQ EFSELSEKYK IMKFKSKKAV KNYAFEIPDV PSQAEYLEVR
YSAEMPQLPS DLRGETFSHV FGTNTSSLEH FLLGRKIRGP CWLDIRAPQL CSPSVSWCKV
EAVATKCELV SVVKDLPPPP LVVMAISMKT AQNAKTHHNE IMSLAALVHQ GFPMDRAPPQ
PPFQTHFCAI SKPSDCIFPY DFKEAVNRKN AKVEIAATER TLLGFFLAKV HKIDPDVIVG
HNIYGFDLEV LLQRISVCKV PHWSKIGRLR RSAMPKLGGR SGFAEKNAAC GRMICDVEIS
AKELIRCKSY HLSELVAQIL KTERVTIPQD NLKSYYSDSA RLLYLLENTW MDAKFILQIM
CELNVLPLAL QITSIAGNVM SRTLMGGRSE RNEFLLLHAF HERDYIVPDK QVFRKLQQDP
GDDEEEVDLG KGKSRKVRKK AAYAGGLVLD PKVGFYDKFV LLLDFNSLYP SIIQEFNICF
TTVHRVAPGS QKRTEDEEQD DIPELPDPDL EMGVLPKEIR KLVERRRQVK QMMKQPDLNP
DLYLQYDIRQ KALKLTANSM YGCLGFSFSR FYAKPLAALV THKGREILMH TKDMVQKMNL
DVIYGDTDSI MINTNSTNLE EVFKLGNKVK SEVNKLYKLL EIDIDGIFKS LLLLKKKKYA
ALLVESTGDG HYTTKQELKG LDIVRRDWSD LAKDCGNYVI GQILSDQPRD TIVENIQRRL
MEIGESVVNG TVPLSQFEIH KALTKDPQDY PDKKSLPHVH VALWINSQGG RKVKAGDTVS
YIICQDGSNL GASQRAYALE QLQKQDALSL DTQYYLSQQV HPVVARICEP IEGIDSALIA
TWLGLDPAQF RAHQQYQRDD ENEALLGAPA QLTDEEKYRD CERFKFACPR CRTENVYDAV
FEGAGEHLQP SLMRCCGDQC EASPISFRAE ISNKLVLDIR RHIRKYYSGW LVCEEQACQN
RTQRLPLAFS RSGPMCPACM KATLRPEYSE KALYNQLCFY RYIFDWDYAY AKCLQSEERA
TVKQNRWSNL RDVYVKLRDV VEQTLATSGY SEVNLSKLFQ AFASFK
//
