ID A0A261B0U0_9PELO Unreviewed; 1473 AA.
AC A0A261B0U0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE Flags: Fragment;
GN ORFNames=FL83_18203 {ECO:0000313|EMBL:OZG03942.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG03942.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG03942.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG03942.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG03942.1}.
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DR EMBL; NIPN01000191; OZG03942.1; -; Genomic_DNA.
DR STRING; 1503980.A0A261B0U0; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
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 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:UP000216463};
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 32..92
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 435..734
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 800..1236
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1275..1467
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG03942.1"
SQ SEQUENCE 1473 AA; 167474 MW; 1136BFE64FE0A1D6 CRC64;
MSDSENNADG DVRRSSRRCG VSAKKTKELS AMEQLKQARA SGRAYKPDIE VEDVYDTVDD
DEYEQIVSKR QNDNFVVDDD GMGYVDTGVD FEDDEYGDDY EDDVPRESSS KRGDKKTKKE
KKDKKKGAMH AFLSSTISKK AVVDESKVKA NLEDDEELKN ILEQLDQVDS DAEVEEQPIK
VSKNPFKRGR SVDSPTSDAI APRPIVKKSK TSNVTGLAPH RFQNSKNQVM AKTIPEPKSD
EDNDDDDYGV PDFDDLPPVS PIKAEVKTPL ISPQKEKNGK VPQEVLKMEV DNDEVETTGR
IKEVEDSLAK FRVMEDVWTE NSEEDSKEAI VAEVETGSES FYVMSGESED TKAIRMYWID
AYEDVHKANG TVYLFGRVKA SATSWESCSI VVKNICRKVY FMPRSHNLRT GEESNLAELH
KEIGDVLKNK FNTHEFKCKM VEKELIRDES FGNGGGTKTP LMEVLYPADK GKLPSDLKGN
TFSHTFNTSV TPLERLLIEK KFMGPGWIEL YNYAKPKAPT TNCKHEFEVD MEKMKNIRYL
EDDDLEKMKV SANSNLAIPS IKLFALNIVT TLNEKKENEI CMISVLINPK CDLSHPSGDP
KNFQRKCLIT KPSGGSLPYD IQKRLESGHI SSCVQTIANE KALLTRFLAL INEQEPDMVV
GHDLSATIAL LVSRLEKLKL PNWSRISRLK RSINIGKLGH SKSGQWELTA GRLMLDSKLA
AMELVKSRSF DLTELSQQIL QTTRREIYSS EIPHLYSESK DLISLINWSW HDLLLSIRLV
NHLNALPLYL QISQIVGGIT SRTMMGGRAE RNEYLLLHAF EKADLIAPDK YNSFDAKKKK
EQQSEDNAEV TEEKKSGKAQ YSGGLVLEPK KGLYETLILL LDFNSLYPSI IQEYNICYTT
LEYAKDSDEQ LSVPQNTDIE GVLPREIRKL VECRRNVKAL MKTERNEAKR KQLDIRQMAL
KLTANSMYGC LGFQYSRFYA KPLAALVTAK GREILMHSKD LVEKMGYSVV YGDTDSIMIN
TNSVDLVAAK KLGSEIKKAV NKCHRLLELD LDGVFKRMLL LKKKKYAALT INPDTKVETK
ELKGLDIVRR DWSQLAKETG TAVVDKILDA SLTRDEMISS IDDLLREIRQ KLDSGTIPLE
MFQISKQLTR NPEQYSDVKA QSHAAVAQRL NKSGKFHFRH NDIVEYLICD DGSDNAATQR
AYHRTEMTDN KDLKIDLLYY LAQQIHPVVS RLVEPIEETD AVRIAESLGL DSTNYRRAAA
AQASQRAAEE DCTWQQENYE LCEGVIVVCP YAECGETNVI RETFDSTTDP TCPRLLLSGC
SKCDKSWESS EHQAVIFNQI DRQLGEFVSR HHAAAFRCDE PTCEFKTRVQ TIKWCREGLE
CVRCSTGVLR REYTSKQLFD QQMFFRQIFD VETAIRKLSD SQKRASENRD RQRFTACRID
SMEIVNRINK KYLERNSYNR VDLSYIFAPM LKV
//
