DPOZ_BPPMB
ID DPOZ_BPPMB Reviewed; 625 AA.
AC A0A2L0V166;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=DNA polymerase DpoZ {ECO:0000250|UniProtKB:G3FFN8};
GN Name=dpoZ;
OS Salmonella phage PMBT28.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=2081904;
OH NCBI_TaxID=28901; Salmonella enterica (Salmonella choleraesuis).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29954894; DOI=10.1128/genomea.00568-18;
RA Koberg S., Brinks E., Albrecht V., Neve H., Franz C.M.A.P.;
RT "Complete Genome Sequence of the Novel Virulent Phage PMBT28 with Lytic
RT Activity against Thermotolerant Salmonella enterica subsp. enterica Serovar
RT Senftenberg ATCC 43845.";
RL Genome Announc. 6:0-0(2018).
CC -!- FUNCTION: DNA polymerase that preferentially incorporates the non-
CC canonical base aminoadenine/dZTP instead of adenine into the
CC synthesized DNA. More efficient in using dZTP instead of dATP as a
CC substrate. In addition to this preference for dZTP, the phage also
CC encodes a dATP triphosphohydrolase that removes dATP and its precursor
CC dADP from the nucleotide pool of the host.
CC {ECO:0000250|UniProtKB:A0A2H5BHJ5}.
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; Evidence={ECO:0000250|UniProtKB:A0A2H5BHJ5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + dZTP = diphosphate + DNA(n)-Z; Xref=Rhea:RHEA:67728,
CC Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17341, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:172931, ChEBI:CHEBI:172959, ChEBI:CHEBI:173112;
CC Evidence={ECO:0000250|UniProtKB:A0A2H5BHJ5};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. DpoZ
CC subfamily. {ECO:0000305}.
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DR EMBL; MG641885; AUZ95520.1; -; Genomic_DNA.
DR SMR; A0A2L0V166; -.
DR Proteomes; UP000241443; Genome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 3: Inferred from homology;
KW DNA replication; Reference proteome; Viral DNA replication.
FT CHAIN 1..625
FT /note="DNA polymerase DpoZ"
FT /id="PRO_0000453688"
FT REGION 324..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 70845 MW; BF8CE8D6EF5AD4AF CRC64;
MAIFPRLENY SEVAIDTETT GLDWFRNDKP FGVAIALPNG YSEYYDIRKD LAAYQWLRDS
VHKIRRAVNH NMKFDIHMLR KIDVHVNTRT AECTQIRAAL INEHLMSYSL DSLAKKYLKA
EKVDDIYEEL AKLFGGPATR KAQAPNFHRA PESMMRRYAK VDAELALQLW QWQEEEIARQ
DLHEVWRLEM RLQPHVIESE RVGIRVDEEL AHKRIGDLTK IVDQTRKEIN RLAGFEVNPN
PSGSIKRLFE PYKEGDQWYA KDGTPIGTTD AGQPSLGADA LKAIKHPAAG LILKCRKMIK
TRDTFISGHV LGNIVDGYVH PNINQTKGET GGDDSGTEGT GTGRLSYTRP ALQQIPSRDK
EVAALVRPIF LPDEGQQWTY GDLDQHEFRI FAHYANPKSL IDAYTENPDL DMHQIVADMT
GMPRSAPASG GANAKQINLA MVFNMGGGEL ASQMSLPYTW ETATFKGESE ARRFKKAGEE
ALAVMEKYYR AIPGVREVAR QASSLAKSRG YVKTMYGRKI RFPGGMFTYK ASGLVYQGTA
ADFNKRNICE IAEYIESECP HYRFLLNIHD EYSMSMVDEG DITVRHLKEM KRLVENKGLR
VPIRIDFGGL APNWWEATKM DAVTK