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Database: UniProt
Entry: A0A1C9EHI0_9CAUD
LinkDB: A0A1C9EHI0_9CAUD
Original site: A0A1C9EHI0_9CAUD 
ID   A0A1C9EHI0_9CAUD        Unreviewed;      1133 AA.
AC   A0A1C9EHI0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=SEA_TONENILI_231 {ECO:0000313|EMBL:AON96951.1};
OS   Mycobacterium phage Tonenili.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Ceeclamvirinae; Bixzunavirus; Bixzunavirus tonenili.
OX   NCBI_TaxID=1891703 {ECO:0000313|EMBL:AON96951.1, ECO:0000313|Proteomes:UP000204231};
RN   [1] {ECO:0000313|EMBL:AON96951.1, ECO:0000313|Proteomes:UP000204231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Acevedo E., Azhar M., Golebiewska U.P., Grzywna D., Guardiola R.,
RA   Jackson O., John N., Kanavatsas C., Khan S., Leong J., Mansilla E.,
RA   Muladjanov Y., Nouel J., Oh S., Oppedisano M., Sajid A., Samper M.,
RA   Ugbeva O., Delesalle V.A., Garlena R.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2016) 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; KX752698; AON96951.1; -; Genomic_DNA.
DR   RefSeq; YP_009288064.1; NC_031080.1.
DR   GeneID; 29066629; -.
DR   KEGG; vg:29066629; -.
DR   Proteomes; UP000204231; Genome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   NCBIfam; TIGR00594; polc; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..75
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  127332 MW;  14952115F702A1C7 CRC64;
     MSSGKAALHN HSETSILDGR SRPEEMAARA KDCGDESVAI TDHDDVGGHF RFQKACQDAG
     VKPILGAEQR WMHNIADSRD RKTGGSDSSH IVLLAENNTG LRNLWALSSL AYEPEQFYKK
     PQLEPRLLRA HREGLWASDG CMLTRFAEYV VNDQDDLARQ EWAVLLNIFG DHFYSELHTW
     QFIDPISPEQ QALNAKMTKI NQAKVRFAKE MGVPLVVVND AHYAYERQWK EHRAIWDMST
     GSWKKDQVEE RGHAADWMMN ADEIRHYMGL HGVGASVIEE AMKNSGWIAE QCNAEINGTL
     LAMPRLYATD AEDAAAFRRS IEEGFKKFVV DKGLPESVYR ERLEYEAKLI IDKNMAGYFN
     VVADYVLAAR NGTYHQAITG DPKPKPCLCG PGRGSAGGSL VTYVMGITSI DPIKYDLMFE
     RFINPDRPDF PDIDVDFQKS KKSLVKQYLG KRYGEDNVVS IGTRTHSRPR QMLQDLCRAE
     GIPFKEMKQM IDLVEQVDQI APFEEGMELP EDEEPPTWDE VLQEIGGDLA PYAKKYPELF
     DKMGKMVNMV RGVGVHPAGV LVNTDPVFPG LIPTRRKGGV DVRATQFDMY EIETLGGVKD
     DLLANKGLDV LDIARDLIYE RHGVWIDYDG FGFGVPEDCP PDKVIALNDD KYLSDPAIYE
     QIDRGQTAGL FQVNTPAGTK LAMRFKPRSV VDMADLASIN RPGVTRVPGL LDKYIERRHG
     RDPVTYDHPL MESITGPSSS MNTYGILVYQ EQLIRTAKEL AGFTPGEAER LRKGIGKKKM
     EIINELEPKF LDGCMANPEF VRLGGTRKVA DRIWQSLKAA GAYAFNKSHG VGYALQPCQE
     AWVKHYYFDE FITGCLVVHT DKTIRFLREC RQRKRPVLPP DVNQSGAGFT LTDEGIRFGL
     TDISGIGDAA MPDILAKRPF KDLDDFLTRA SKGGGAKKGV VDALIKVGAF DFTGEHRQVM
     LEKVYRHRRG LSAPVKWAKM TLDEQVAEIA DKRRIKPEDY PIYDFDDPQV IHDLEVEMLG
     TFVSHDPMAK YARMIEGVCI RHPMDYDDYE VGAQFVVGGK LVKARTHQQK NGKQMAFLAV
     HWNEEDFEIL AFADAWARCR PLLKIGSPVA CQVIKLRGGA ASLSTVERLD TIV
//
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