ID   DPOZ_BPSHA              Reviewed;         624 AA.
AC   A0A2H5BHJ5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=DNA polymerase DpoZ {ECO:0000303|PubMed:33926956};
GN   Name=dpoZ; ORFNames=SHab15497_00037;
OS   Acinetobacter phage SH-Ab 15497.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=2060946;
OH   NCBI_TaxID=470; Acinetobacter baumannii.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=31555825; DOI=10.1093/abbs/gmz094;
RA   Hua Y., Xu M., Wang R., Zhang Y., Zhu Z., Guo M., He P.;
RT   "Characterization and whole genome analysis of a novel bacteriophage SH-Ab
RT   15497 against multidrug resistant Acinetobacater baummanii.";
RL   Acta Biochim. Biophys. Sin. 51:1079-1081(2019).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=33926956; DOI=10.1126/science.abe6542;
RA   Pezo V., Jaziri F., Bourguignon P.Y., Louis D., Jacobs-Sera D.,
RA   Rozenski J., Pochet S., Herdewijn P., Hatfull G.F., Kaminski P.A.,
RA   Marliere P.;
RT   "Noncanonical DNA polymerization by aminoadenine-based siphoviruses.";
RL   Science 372:520-524(2021).
CC   -!- FUNCTION: DNA polymerase that preferentially incorporates the non-
CC       canonical base aminoadenine/dZTP instead of adenine into the
CC       synthesized DNA (PubMed:33926956). 29 times as efficient in using dZTP
CC       instead of dATP as a substrate (PubMed:33926956). In addition to this
CC       preference for dZTP, the phage also encodes a dATP triphosphohydrolase
CC       that removes dATP and its precursor dADP from the nucleotide pool of
CC       the host (PubMed:33926956). {ECO:0000269|PubMed:33926956}.
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:0000269|PubMed:33926956};
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:0000269|PubMed:33926956};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.3 uM for dZTP {ECO:0000269|PubMed:33926956};
CC         KM=21.4 uM for dATP {ECO:0000269|PubMed:33926956};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. DpoZ
CC       subfamily. {ECO:0000305}.
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DR   EMBL; MG674163; AUG85479.1; -; Genomic_DNA.
DR   SMR; A0A2H5BHJ5; -.
DR   Proteomes; UP000241732; 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:UniProtKB-KW.
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   1: Evidence at protein level;
KW   DNA replication; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transferase; Viral DNA replication.
FT   CHAIN           1..624
FT                   /note="DNA polymerase DpoZ"
FT                   /id="PRO_0000453687"
SQ   SEQUENCE   624 AA;  71000 MW;  C75215F333A37B8A CRC64;
     MAFPNIEQYP QISVDCESTG LEWYKEDRAF GVSIYLPTGD AEYYDIRKDR NAFHWMKDNL
     WKAKKIVNHN IKFDIHMLRA TGINLNPANC ECTMIRAALI DEHLLKYDLD SLLKKYLKMS
     KDNDIYADLA QIFGGQPTRK VQILNLHRAP VDLVARYANI DTEGAYKLWE WQEGEIERQD
     LHQVWQLERR LFRHIVEMER RGIRIDPNEA NRRAEELDRV TAETVAELNR LAGFEVNPNP
     SGSIKKLFNP KQNEAGIWVA RDGTPLPKTD SGAPSLGAKS LESMTDPCAK LILKARKLNK
     TKDTFIRGHV LGHAIQNGQD WFVHPNINQT KSDTGDGSEG TGTGRLSYTR PALQQIPSRD
     KEIASIVRPI FLPDRGQKWS YGDLDQHEFR IFAHYANPKD IIEAYAQNPD LDMHQIVADL
     TGMPRSATKA GEANAKQINL GMVFNMGAGE LASQMGLPFT IESVDFGDHV HDLKKAGPET
     LEIVENYYAK VQGVKEMARK ARTIAKSRGY VRTLMGRHIR FPRGMFTYKA SGLIFQGTAG
     DLNKLNICNI AEYLESECPY NRLLLNIHDE YSVSLEDDGK EIKHLKELQG LVQHRPELRV
     PIRIDFSHPA PNWWLATRAD LATK