ID A0A267FRH3_9PLAT Unreviewed; 1884 AA.
AC A0A267FRH3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=BOX15_Mlig012441g2 {ECO:0000313|EMBL:PAA76353.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA76353.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA76353.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA76353.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA76353.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-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 -!- 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}.
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:PAA76353.1}.
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DR EMBL; NIVC01000827; PAA76353.1; -; Genomic_DNA.
DR STRING; 282301.A0A267FRH3; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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: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 GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR CDD; cd05534; POLBc_zeta; 1.
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; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
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|RuleBase:RU000442};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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 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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
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 107..240
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1003..1127
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1278..1735
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1776..1861
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 197..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1884 AA; 200780 MW; E964F6B919E34E4C CRC64;
MSPAGASAFS MRIVSLETAM EQPVSGLDVT YSDFRSGQCS RVPVLRVFGS TPAGRKCCAH
VHGVFPYFYV PFEGCSGPRA DFLKAFAASL DKAINIAVRR SSSSTVMHVF CINVVLGRSF
YGFHANESEF MKIHMFNPKM VKKAADLLLG GSVMNKVFQP FESHIPFGLQ FLMDFNLYGM
NFLHASVARR RGCLGSDAEE EANEEPEAEG CPGQAADPSP APPATHCRVE VDISAVDILN
RLEVDDNLGS NPGLTALWEE EIERRQELLG ETPPSPPSSA STSTAGAARA WVAAPDSPDR
QGVEPTESED KWRRRFRRFL QERGLINATG FEDEAPAEET GAAEGAQVAD VKSGLGELAD
APSHAEVAEF DAEVASFTEE DVDDFLNGSA NSVDTEPVVD HSTESAESPG SPVPPADQDE
APKQPPPPLV SRASIDRVVA CSQSFLADSS DSSDGSDRDA ADADSADSEA TCEELASRML
DEFLVRSPSS SQVAGAAAAA EDPAQVEAEL NDSQRDLFAV EDYEDDNEDE EQRDEHRDEA
EEAAGQLDAA TLLQFVRMEE QDSVLAVAFD GGSDSDDEDD EDEEAGDEAG ISGPPQLDGA
LSSSDDSSSA GGGDDDGDFD ESPCRSSARQ RRGRAPQPPP PPPARRGRRL GLSMASRPAA
GSAAAASSMS SKSPPGPNGS SKAFKPVALR GGSGSGLSGR PMLLGKRRSV APPSPPSPPS
QPPPSSPPPL PPQPATTQSP SSASSLILSQ SLELASFTTS GQRLPTSTQQ HQQRLESSRS
NQASSNTQNL LAPNSPEPPS TLPKRQPAMA HVYAPLVAPP TASEVADSLD SFGLFPCRNP
PLRPDAAGVD DLRQFDSLAV GVAGLASFDR ASALAAASVS MSTSTAPLLR YRPLIDPPSR
DLVARSLKAA AAAAADKLAK PAAESATAAA EATVDDAFDT VSNSSSHRAY PRPAAAIGGS
GIGRKELLAR IRAKFRRSLS ETSAMSNSST SMSTSAAAAT TAAVVGDGLT LASLEVATAA
RPGLLPDPRN DAIVAAFLTV ADASEANPTA WRQHCLFVAA TDAEADPRIR GFASAATRFQ
AVRDEAALLE ALADNVRCAD PDIVLGFDTQ RASWGYLIDR AKQLQGPPES GGGGLPMAQL
LSRYRLLPHQ QQHRRRREPE ANCSSQSQQP EDGLAGSYEA QSDSLRIGGR VVINLWRLLR
YELSKLRSNS FEACAALVLN RRYPCYSSDV LWRMWQDGRD SWRVVEHLET RSCGSLRMLS
TLGLVSRTAE FARVFGIEFY HVLSRGSQYR VESMMLRLAK PLGLLPLSPS VQQRARQAAP
DAIPLTLEPR SGLHTDPVVV LDFQSLYPSI MIAYNYCFST CIGRAASITT CDPMAYEFGC
HRLMTDPGAY QRAAGHLNFS PLGIGFVDAS VQLGVISRMV EEILATRLMV KAAMKRYGGN
EPLLKLLDAR QLGLKLIANV TYGYTAASFS GRMPCVEVGD SIVRKARETL ERAIALVQAE
PSWRAQVIYG DTDSLFVLLP GRSRREAFEI GQAMARAVTA VNPKPVKLRF EKVYQPCLLL
TKKHYAGFMY ETADQLEPTF DAKGIETVRR DSCPAAGRIL GRSLRELFSS LDLSRVRQVV
EFELHRLHWG RSPLQELIIA REHRGCRNYS ERAAVPGLAV VRRRLAADPR AEPPLGYRVQ
FVVVRPSQPG QGLCARARSP EELLGAAGGG AGGPECLDRD YYASKQVLPP LHRALSLLGV
DVFAWNAGLA KPGALARLGV GGGAGAIGRF LGQGSCGACG QPGAIASGAS APPLCAECAR
APWAVGAALL SAAAGAEARA ARLAETCAVC QSGCLAPRLA PFEASANVDC RSADCPVAFE
RWAAGSPAAL RRLEEIRQIV EALL
//
