ID L2GW41_VAVCU Unreviewed; 1168 AA.
AC L2GW41;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=VCUG_00905 {ECO:0000313|EMBL:ELA47582.1};
OS Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Vavraia.
OX NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA47582.1, ECO:0000313|Proteomes:UP000011081};
RN [1] {ECO:0000313|Proteomes:UP000011081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vavraia culicis strain floridensis.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
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; GL877415; ELA47582.1; -; Genomic_DNA.
DR RefSeq; XP_008073927.1; XM_008075736.1.
DR AlphaFoldDB; L2GW41; -.
DR STRING; 948595.L2GW41; -.
DR GeneID; 19878788; -.
DR VEuPathDB; MicrosporidiaDB:VCUG_00905; -.
DR HOGENOM; CLU_000203_2_1_1; -.
DR InParanoid; L2GW41; -.
DR OMA; FITGVEM; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000011081; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0004527; F:exonuclease 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000011081};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 62..319
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 524..806
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 893..1043
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1079..1146
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 805..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 134040 MW; BE26BDBC1736C5EB CRC64;
MLVFQTNINS FTQTKESQTT TQIYIECMAN DAHLKLVVTD FFPYFYVKIE TDKNDILNFF
MSKNIDVVSH KLSIKKNVYG YISKNESFLK VFFKNIVVES AARRACENMY EIFDANIPFN
LQFMVDMGIV GMSYLEVDMD MESGQELRIE DAGGANGVFS TSLDVHNGNQ RIKRHKSEDE
ENTKYMDAIC STHRIGRVYH VSHRAIRPIL KDCMPVFKIL SFDLEVNNRE NKFPDSSIDE
IIQIGNTVKQ HEYKQTIFCQ RNTAGIAGVD VRSYDTEREM IEEWIKFVYY EDPDVFLGYN
ISGFDFDYII GRVRKLGVPF CLCRLYIDPS KDDTIARAID TSARMLRDVA KNETNLRLKQ
EIGQVVKNET SAVLETSKMG REEVNRTASN VLSGIESKGG RFATEHVMYD AIKDKFGECK
SCNNTRKEMF NDFHGRIVVD MLTVIKKEHK LRSYTLNNVS VHFLGMQKED LPYYLIKGLF
DGDDKTRRRI AVYCLKDTLL PLLIYEKLLI FITGVEMVRV LGVPIHWHFN RGISVKIFGL
ILREARKNGF VIPNVTVKDE GYMGAFVIEP ERGYYDEPIA VLDFASLYPS IIIAHNLCYS
TMLLGTKHGI DKSKDAEISP TGTYFVKKDV RVGLLPVILE KMLKKRKEVK EQMKNETNTF
MRTLLNARQN AFKVSANSVY GFTGSAVSRL PCIDISQSVT GYGREMIIKT KNVVESVFCR
DKGYDFDGRV IYGDTDSVMI RIRKENLSVD YVFEIAKEMA SKVSECFVKP VKLEFEKVYF
PYLLMNKKRY AGVIETREEI KDEVKVSEVK SDSRKSSSQT SQAKEAEENS GSKTEGNEIG
EVKTVKIKNE TAAADNLKNG VRNTVTDEEE TAINTVSTEN ERGVAKEPKK KYKIQRRMDT
KGIETVRRDN CKLVKSLIEE CLNLLLIQRD PERAKSFVKA VVRDLYLDRI DLGQLVISKT
LSKTNYAAKQ AHVELAERMK KRDNAVINIG DRIAYVIVDK GPNVIAYEKS EDPLYVLEKN
LPVDVNYYIE QQIMKPVHRL FDPLMDNVNE LFVGEHTATR KKGTLSGPMA QFVKKGITCL
LCKERGPILC RRCAPNYFSV YVGKIQEMKE KEDVYNKCWR ECQRCIRSVC TEVLCANKDC
PIFFMRSKVI REIGELDKQI KQLNSLEW
//
