DPOZ_BPVC8
ID DPOZ_BPVC8 Reviewed; 633 AA.
AC G3FFN8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=DNA polymerase DpoZ {ECO:0000303|PubMed:33926956};
GN Name=dpoZ; ORFNames=phiVC8_p29 {ECO:0000312|EMBL:AEM62926.1};
OS Vibrio phage phiVC8.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Enhodamvirus.
OX NCBI_TaxID=1076759;
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27000701; DOI=10.1186/s12985-016-0490-x;
RA Solis-Sanchez A., Hernandez-Chinas U., Navarro-Ocana A., De la Mora J.,
RA Xicohtencatl-Cortes J., Eslava-Campos C.;
RT "Genetic characterization of OVC8 lytic phage for Vibrio cholerae O1.";
RL Virol. J. 13:47-47(2016).
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. 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: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=0.1 uM for dZTP {ECO:0000269|PubMed:33926956};
CC KM=4.5 uM for dATP {ECO:0000269|PubMed:33926956};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. DpoZ
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JF712866; AEM62926.1; -; Genomic_DNA.
DR RefSeq; YP_009140158.1; NC_027118.1.
DR PDB; 7PBK; X-ray; 2.80 A; A/B=1-633.
DR PDBsum; 7PBK; -.
DR SMR; G3FFN8; -.
DR GeneID; 24366413; -.
DR KEGG; vg:24366413; -.
DR Proteomes; UP000008906; 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 3D-structure; DNA replication; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..633
FT /note="DNA polymerase DpoZ"
FT /id="PRO_0000453679"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:7PBK"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7PBK"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 173..201
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 204..223
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 229..254
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 308..324
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 463..469
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 494..506
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 546..570
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 592..603
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:7PBK"
FT STRAND 614..622
FT /evidence="ECO:0007829|PDB:7PBK"
FT HELIX 623..627
FT /evidence="ECO:0007829|PDB:7PBK"
SQ SEQUENCE 633 AA; 71216 MW; 478E14F1E5C9ED95 CRC64;
MKLDWERTGR RMGFIDLSKY EVWSYDTECT GLQYKVDKVF GFSIATPDGQ SGYFDVREQP
ESLQWLAEQV EPYKGTIVCH NASFDYRMSL HSGIKLPLSQ IDDTGIRACC INEHESTIFP
WTRGRAGDYS LDYLAKKYVG AQKYAEIYDE LAALFGGKAT RKTQMPNLYR APSGLVRKYA
CPDAELTLEL WLEQEELIKK RGLERIVAFE RKVMPTLIRT EARGVRVDLD YAEQAIFKMD
GVVRENQAKM FALAGREFNP NSPKQVREVF GAKEEGGVWK SRDGTILERT ATGNPCLDAD
ALRSMTDPLA AAVLELRSNI KTKDTFLAKH VVEHSVGGRV YPNINQMKGE DGGTGTGRLS
YTGPALQQIP SRNKRIAAII KPAFLPEEGQ LWLDSDMASF EVRIFAHLVA AYNPAIAKAY
AENPELDLHQ WVGDLMGIPR NASYSGQPNA KQMNLGMIFN RGDGAVADSL GMPWEWCEFT
DKKGELIRYK KAGREAKSII AAYHSQIQGV KTLATRAQKI AEERGWIQTA HGRRLRFPNG
YKSYKASGIL IQATAADENK ENWLRIEDAL GSDGSMILNT HDSYSMSVDE NWKPIWERVK
KAVERQTLRV PLLLEFDGVG KNWAEAKGLI DVH
