ID A0A369RWT2_9METZ Unreviewed; 1503 AA.
AC A0A369RWT2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE Flags: Fragment;
GN ORFNames=TrispH2_008143 {ECO:0000313|EMBL:RDD39147.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD39147.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD39147.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD39147.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD39147.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:RDD39147.1}.
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DR EMBL; NOWV01000146; RDD39147.1; -; Genomic_DNA.
DR STRING; 287889.A0A369RWT2; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
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 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:UP000253843};
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 60..121
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 472..774
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 840..1284
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1324..1493
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDD39147.1"
SQ SEQUENCE 1503 AA; 172045 MW; 60964C6AD2869253 CRC64;
HPTPTFWRQI YFSSLLTTDD ITRMMVTSEK QNETVDDSNN TASRRSLRAK TKSKADRAIE
SLRKAKEDGG RYKYQLEKHS NIYEEVDEVE YSRIVTSRQE DEWIVDDDGT GYADHGREVF
DDDFDQEDTE MDSANKYSGG NKQKRDSFGH PSAKKQKKLA MKPIQSMFLA SSKKTQNNKN
VKLENDDLLD DILQEIEKKD PVPNANKSDR TPSNPRNQKQ LTGAAMKRRL YVREPIDVQP
EKSKVKRVDN ISSFKNSRID RNLTEAYTAS SLPVIKKEPG IYREPSLPDS SIKQEIDSHT
ENYIPAVKES DDFTSNDDLD IVMNDIDAFP DCENTDTVNP EEENVNAVKN DRLRHLSTSS
DFISNHDLEL MTDETLHNSD FQKVDSMATT TPTIPVDEID GEKYIDFFWF DAYEDPSLQK
GIIYLFGKVK TKENAYASCC LIVKNIERDI YILPRKTRLD TDGSDSGIEV TMKDVYEEFS
EICNKNKIMT FRSRVTKKRY AFELKDVPVE SEYLHVKYSA ALPQIKSDMQ GQTFSHVFGT
NTSSLESFLL HNKIMGPNWL RIRNPQFPSQ KVSYCRSEIC VDDPETIKVL QGNELPKMTI
LSFSMKTIIN PKTHENEIVA IAAVTHQSFY FDKPPPKSLF EGHFVVIRNL VDHNIPMGFR
DFMKQKNINL EISSTERALL SFWLAKVQQI DPDIIVGHNI CGFDIDVILH RMNTCKVSLW
SRIGRIKRHA MPKLSSTVGG FGFADRSACC GRLICDAKTS AKELIRVKSY DLTELTSYVL
KAKRFDINQD EIADKFNSVG DLFALVNHTF MDATFALRIV YELNALPLAL QITNIVGNVL
SRTLLGGRSE RNEFLLLHAF SEKDFVCPDK SFKKKQQFNE EFEDHDDAAK SNNRRKKPAY
SGGLVLEPKK GFYDKYILLL DFNSLYPTII QEFNICLTTV DRHHLAADEN NDNELECEYP
SPDLEPGVLP LILKGLVERR REVKGLMKSC KDELAYKQYD IRQKALKLTA NSLYGCLGFS
NSRFYAKPLA ALVTSKGREI LTKAKELVEN QMLLEVIYGD TDSIMINTNS TNLDEAYNLG
HKVKAEINKS HRLLEIDIDG VFKSMLLLKK KKYAALAIQK NEDGTLSEVK ELKGLDIVRR
DWCQLAKDVG NYALSQILSS DSRENIVDKI HSYLTEVGDD VRSGRIDIDK YIILKTLSKS
PNDYPDKKSL PHIHVALWMQ TENRRVQIGD AVPYVICDDG SQLNVAQRAF HPDQFRRSDS
LKIDFKYYLA YQIHPVVSRL CDPIEGTDSA RIADCLGLDG SQYKHKSYSA EQNESDAMLG
DMHMSLEEQF KNVEPLKISC PKCKVTEDFA GAYNKTTKQS GLVCPHCNSN YNVVTIQNKV
VSEIRKFIKT YYQNWMQCDD PSCDYKMRQA PYFISGRTIR CPACERGHLT LTYSEKSLYN
QILYYQHLFD IDQIEKGIRI DQNIKADFKN LYGTVNKIIS RNGYSEINLS KLFQRLFTGP
AKR
//
