ID A0A3Q0KIQ0_SCHMA Unreviewed; 1259 AA.
AC A0A3Q0KIQ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_087010.1};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_087010.1}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_087010.1};
RG WormBaseParasite;
RL Submitted (DEC-2018) 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|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 AlphaFoldDB; A0A3Q0KIQ0; -.
DR STRING; 6183.A0A3Q0KIQ0; -.
DR EnsemblMetazoa; Smp_087010.1; Smp_087010.1; Smp_087010.
DR WBParaSite; Smp_087010.1; Smp_087010.1; Smp_087010.
DR InParanoid; A0A3Q0KIQ0; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR ExpressionAtlas; A0A3Q0KIQ0; baseline and differential.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:UniProt.
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 CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 1.
DR Gene3D; 2.40.50.730; -; 2.
DR Gene3D; 6.10.140.1540; -; 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; 2.
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 NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
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; 1.
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:UP000008854};
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 275..616
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 680..1125
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1164..1237
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 142346 MW; 7782B0F827DCD6B2 CRC64;
MSNKRPSFVP QKGPGSFKKP RGNHDDAPEP SKFEQELMLL DDIETEDIAL VDESSALSHL
DVQTNSHWPR RKLEKLDPNK DVMLCCLNTP LQGFPFFGFE GAQLELRKTW AAMSNKRPSF
VPQKGPGSFK KPRGNHDDAP EPSKFEQELM LLDDIETEDI ALVDESSALS HLDVQTNSHW
PRRKLEKLDP NKDGITFQQF DVSHYKGEHL PGMPGATQSP VPIIRLFGIT EKGHSVCAHV
HGFLPYFYVP APKDFSTDHL SAFREALNSM LLKEKSKEFE GLQHLVLRVT CEEKQNIYGF
HGNRSLPFLR ITLALPRLIA PAKRILDNGL SFADYSLQSY PAFEANIDFE IRFMTDTQMT
GCSWVEAPTQ KYHLRDSTQK LDDMKKAINQ KSNHSVNSST ISTTNGCNGV NDQSTLLTNQ
TRCQIEFDIA WDALIVHSPE GQWSNIAPLR ILSFDIECAS RKGVFPVPDK DPVIQIANMV
INYGETTPFI RNVFTLNTCA PIVGSQVISH QTEKELLAKW SAFVREVDPD IITGYNIQNF
DLPYLINRAN TLKVDGFEFL GRIRGARSTI REAMTQSKQM GRRENKFVNI DGRVQFDLLQ
ILFRDYKLRS YTLNAVSYHF LEEQKEDVHH NVITDLQNGD AQTRRRLAVY CLKDAYLPLR
LLDKLMCIVN NIEMARVTGV PLTYLLTRGQ QVKVVSQLLR KAHEHGYLLP TYQSQQGDEF
VGATVLEPRK GFYNEPIATL DFASLYPSIM MAHNLCYTTL LQVNTTPHGS TGGGIQALVQ
RYNLTDEDYI KTPTGAYFVK SHICHGILPE ILQQLLSARK KAKAELAKET DPLRKRVLDG
RQLALKISAN SVYGFTGAQV GKLPCLEISA SVTSFGRLMI EQTKLHVEKK FTIANGYKHD
AVVIYGDTDS VMCKFGVSTV TEAMELGRQA AEIISEEFPK PIRLEFEKVY CPYLLINKKR
YAGLYFTKPD RHDKMDCKGI ETVRRDNSPL VANLINACLE RILIDRDPNA AISYAQSVIS
DLLCNRIDIS QLVISKELTK TDEEYTGKQA HVELAAKMRK RDPGSAPNLG DRVPYVITAV
GGKNTAAYAK AEDPLYVLEH NVPIDTKYYL ENQLANPLLR IFEPILGEVK AKSVLLNGEH
TRVKAVVHST VGQLSAFTKV RASCIGCRTL LPADKTDSAL CKYCESRASE IYQKEIVQLN
LLEKKFTSLW TECQRCQQSI HEEVICTSRD CPIFYMRMKS RKDVDEAYKT IQRFGNPNW
//
