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Database: UniProt
Entry: A0A345KWL5_9CAUD
LinkDB: A0A345KWL5_9CAUD
Original site: A0A345KWL5_9CAUD 
ID   A0A345KWL5_9CAUD        Unreviewed;       607 AA.
AC   A0A345KWL5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=DNA polymerase I {ECO:0000313|EMBL:AXH47417.1};
GN   Name=53 {ECO:0000313|EMBL:AXH47417.1};
GN   ORFNames=SEA_HANGMAN_53 {ECO:0000313|EMBL:AXH47417.1};
OS   Mycobacterium phage Hangman.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Bclasvirinae; Coopervirus; Coopervirus brownCNA.
OX   NCBI_TaxID=2250299 {ECO:0000313|EMBL:AXH47417.1, ECO:0000313|Proteomes:UP000257782};
RN   [1] {ECO:0000313|EMBL:AXH47417.1, ECO:0000313|Proteomes:UP000257782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Akers M.E., Baldus K., Bryant G.N., Cevasco M.E., Chichester A.M.,
RA   Largen K.M., Lehmann E.J., Majewski M., Pires N., Ricci K.D., Smith R.L.,
RA   Tancini M.E., Williams D.C., Butela K.A., Garlena R.A., Russell D.A.,
RA   Pope W.H., Jacobs-Sera D., Hatfull G.F.;
RL   Submitted (JUN-2018) 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};
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DR   EMBL; MH513970; AXH47417.1; -; Genomic_DNA.
DR   Proteomes; UP000257782; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004527; F:exonuclease 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; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
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; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00023109};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          392..570
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   607 AA;  66742 MW;  E26F6BC610E4532C CRC64;
     MTTTAIPRVP SRSWYDPVLD ATMHTGANAV RAADQFCTRL PHRSTPIAFD IETPGLDNVF
     TINCVTAAWD WPDGGTQTIL LDPARDEEHY EVAVALLHAA RTVAFHNVPF DAPPLYHAGL
     INDNTIRRIV DTLLITRFAV PDVMVPKNLT ALSVRHLGLD DDKGGLERAF KAAGYKTQQA
     GFEGMDITSP VYRYGAMADT VATLRVEPLM RAKALHWATD HPFATYGATT VGEAEELLAT
     QETVHRVMLR RSAVGLAVDR AYLDRYAEQV DIDRNLAIAE LAAHGLEGGS GKGAKLVEYL
     HERGELPANW PRTPTKKLRA TKADLDGLDH PLAAAQRKLA QIDKVMGYLE KVSRQASVTG
     RCHPQVSTLG ASATGRMAYG SPELQQFPKD ARAIITDDGQ GLTSIDWSQI EPVTMALMAK
     DHAFLAPFEA GEDLYEPIQR SAGIDRPTAK VVLLGTMYGL GIAKLARQIG HTEESAAQIR
     RQMFEAMKGC ERWMRKVQNV AETYGRVVTA GGRILPVDQG YEYKAVNYAI QGSAYDVLAN
     SIVEMDRRGI GDHLQLAMHD ELVVDTEVAE EVQQIMLTPP EFLITWAERV PVLRTDRADM
     GSAWAKV
//
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