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Database: UniProt
Entry: A0A1I0ST20_9SPHI
LinkDB: A0A1I0ST20_9SPHI
Original site: A0A1I0ST20_9SPHI 
ID   A0A1I0ST20_9SPHI        Unreviewed;       935 AA.
AC   A0A1I0ST20;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=SAMN04488511_103119 {ECO:0000313|EMBL:SFA42670.1};
OS   Pedobacter suwonensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA42670.1, ECO:0000313|Proteomes:UP000198836};
RN   [1] {ECO:0000313|Proteomes:UP000198836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18130 {ECO:0000313|Proteomes:UP000198836};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; FOJM01000003; SFA42670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0ST20; -.
DR   STRING; 332999.SAMN04488511_103119; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000198836; Unassembled WGS sequence.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          342..523
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          692..899
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   935 AA;  104600 MW;  705039F4A235F85F CRC64;
     MNKKLFLLDG MALMYRAHFA LSKNPRFTST GINTSAVMGF TNTLLDVLKK EKPTHIAVVF
     DTDAPTERHT SFEAYKAHRQ AMPEDLAAAM PYVLKLITGF NIPVITSDGY EADDIIGTMA
     KKAEQKGYQV YCMTPDKDFA QLVSENIFIY KPARMGNDME ILGVKEVLAK WEVENVLQVI
     DILGLWGDAV DNIPGIPGIG EKTAKALIKQ YGSMENIIAH SHELKGKQRE NVENFAEQGL
     ISKKLATILL DVPVELDEAS LELCDPSRDL LEPLFTELEF RTLGRRVFGD EFSVTTARFQ
     EGTQTDLFGN QSGETIQYTN TLEEEPAEKL PAKTIENTEH DYQLVDSAEQ RADLIKLLLA
     EKRISFDTET TGTDANMADL VGLSFSIKPG TGYYIPVPAE RAAAQSIIDE FRAVLENEAI
     EKIGQNTKYD ILVLKWYGVE VKGKVFDTML AHYLIDPDTR HGMDVLSENY LGYSPISITK
     LIGAKGKNQL TMRDVPVADV VDYAAEDADV TLRLAHIFEP KLKELNAAKL AEEIENPLVY
     VLADIEKEGV RIDIETLQAY SKELETEIIK FEQNVYDKAG IKFNLASPKQ LGEVLFDKLQ
     LDPKAKKTKT GQYQTGEDIL MALASKSDIV QDILDFRQLQ KLKSTYVDAL PLMVNPKTGR
     VHTSYNQAVA ATGRLSSNNP NLQNIPIRTE RGREVRKAFI ARDENHILLS ADYSQIELRI
     IAEISKEENM LDAFSKGIDI HTATAAKVYG VSIEEVDGTQ RRNAKAVNFG IIYGQSAFGL
     SQNLGIPRKE AAEIIEQYFA QYPGIKRYMS DTMNFARENG YVETIMGRRR YLRDINSANQ
     TVRGFAERNA INAPIQGSAA DMIKIAMINI HKEMKAQNLQ STMTMQVHDE LVFDVLRSEK
     EAMKAIIQDK MANAIKLTVP IVVEIGEGNN WLEAH
//
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