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Database: UniProt
Entry: A0A222YY50_9CAUD
LinkDB: A0A222YY50_9CAUD
Original site: A0A222YY50_9CAUD 
ID   A0A222YY50_9CAUD        Unreviewed;       831 AA.
AC   A0A222YY50;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=161 {ECO:0000313|EMBL:ASR76205.1};
GN   ORFNames=PBI_BELLAMY_161 {ECO:0000313|EMBL:ASR76205.1};
OS   Synechococcus phage Bellamy.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Kyanoviridae; Bellamyvirus; Bellamyvirus bellamy.
OX   NCBI_TaxID=2023996 {ECO:0000313|EMBL:ASR76205.1, ECO:0000313|Proteomes:UP000221247};
RN   [1] {ECO:0000313|EMBL:ASR76205.1, ECO:0000313|Proteomes:UP000221247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kim H.J., Triplett B.A.;
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|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; MF351863; ASR76205.1; -; Genomic_DNA.
DR   Proteomes; UP000221247; Genome.
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:0004527; F:exonuclease activity; 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:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1280.300; -; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 3.40.1820.10; DnaQ-like 3'-5' exonuclease; 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; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221247};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          100..266
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          346..815
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   831 AA;  97527 MW;  72EE74AB61F42AA6 CRC64;
     MHFYTNVQLI GNQVLVRGVD NGKRYEHRDE FYPTLFVRSK RDSKYKTLNG EPVEPIKPGT
     VRECRDFYKK YDEVDGFPIY GNDRYVYQYI SEKYPQDEIK FDISQIKLVT LDIETTAEKG
     FPDVESASEE ILAITIQDYT TKQITTWGVK PFVNKQKNVT YHYCETEQKL LSSFINYWMQ
     DVPDVVTGWN IQLFDIPYIC KRLNRVLGEK LMKRFSNWGL VTEGEIYVQG RKHVTFDVGG
     LTQLDYLDLY KKFTYKAQES YRLDYIAEVE LGQKKLDHSE FDTFKDFYTH GWQKFIEYNI
     VDVELVDRLE DKMKLIELAL TMAYDAKVNY ADVFYQVRMW DNIIYNYLKK RDIVIPPKNR
     STKNEKYAGA YVKEPIPGKY DWVVSFDLNS LYPHLIMQYN ISPETLLDER HPTASVDRIL
     AEEINFELYK DNAVCPNGAM YRKDVRGFLP ELMDKMYGDR VIFKKKMIQA KKEYEKTPTK
     TLEKEIARCN NIQMAKKISL NSAYGAIGNQ YFRYYQLANA EAITLSGQVS IRWIEQKMND
     YLNKLLQTTE EDYVIASDTD SIYLNLGPLV NKFFGAKSSD KAAVVSLLNK ICEEKFEPYI
     DQCYQNLATY VSAYDQKMQM KRENIADRGI WTAKKRYILN VWDSEGVRYE DAKLKMMGIE
     AVKSSTPAPC RKMIKDALKL MMNGTEEDVI DFIDKSREEF KKLPPEQISF PRSVSDVVKY
     KSHSDIYIKG TPIHCRGALL YNHYILKNKL DNKYSLIQNG EKIKFCYLKK PNSIHENVIS
     FIQDFPKELD IDKYIDYDLQ FEKSFVEPLK AILDAIGWNV EKTVNLELFF S
//
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