ID A0A1W2BRI6_9SPHI Unreviewed; 938 AA.
AC A0A1W2BRI6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=SAMN04488101_102739 {ECO:0000313|EMBL:SMC75590.1};
OS Pedobacter nyackensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=475255 {ECO:0000313|EMBL:SMC75590.1, ECO:0000313|Proteomes:UP000192678};
RN [1] {ECO:0000313|EMBL:SMC75590.1, ECO:0000313|Proteomes:UP000192678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19625 {ECO:0000313|EMBL:SMC75590.1,
RC ECO:0000313|Proteomes:UP000192678};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWYB01000002; SMC75590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2BRI6; -.
DR STRING; 475255.SAMN04488101_102739; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000192678; 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 Reference proteome {ECO:0000313|Proteomes:UP000192678};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 345..526
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 695..902
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 938 AA; 105152 MW; 453CB957E71CC56D CRC64;
MKKLFLLDGM ALIYRAHFAL SKNPRFTSTG INTSAVMGFA NTLMEVLKKE NPTHIAVVFD
TAAPTERHTD FEAYKAHRES MPEDLSAALP YVFKLIEGFK IPVITKDGYE ADDIIGTLAK
EAEKEGFQVY CMTPDKDFAQ LVSDNIFIYK PARMGNDMEV LGVKEVLAKW EIERVEQVID
ILGLWGDAVD NIPGIPGIGE KTAKSLIKQY GSVENIIAHS HELKGKQREN VETYAEQGLI
SKKLATIILN VPVEFDEKSL EVETPSRELL EPLFAELEFR TIGKRVFGDD FIRSTTTMVS
QQTDLFGNVV GEYRQVEVVV APPPPVFPEQ VTVPLRTIED TEHDYKLADT PELRKSLIEL
LQQQEQIAFD TETTGTDANL ADLVGLSFSV KPGEGYYVPV PAQREEAQQI VDEFKPVLEN
ENIVKIGQNI KYDILILKWY GIAVKGRLFD TMLAHYLIDP DTRHNMDVLS ENYLNYTPIS
ITALIGSKGK SQGNMRDVPA EKVVDYAAED ADVTLQLADV FTPLLKELNA ENLATEVENP
LVYVLADIEF EGVRIDMDTL INYSKELELD IRKFEQNVYD KCGVKFNLAS PKQLGEVLFD
KLQLDPKAKK TKTGQYQTGE DVLLALAHKS DIVQDILDFR QLQKLKSTYV DALPLLVNPK
TGRVHTSFNQ AVAATGRLSS NNPNLQNIPI RTERGREVRK AFIPRDENHI LLSADYSQIE
LRIIAEISKE ENMLEAFNKG IDIHTATAAK VYGVSIEEVD STQRRNAKAV NFGIIYGQSA
FGLSQSLGIP RKEAAAIIDQ YFAQYPGIKQ FMSDTMNSAR ENGFVETILG RRRYLRDINS
ANATVRGFAE RNAINAPIQG SAADLIKVAM INIHRDIQEQ GLQSKMTMQV HDELVFDVLK
TEVEAMKKII SHRMKTAIKT TVPIEIEIGE GNNWLAAH
//
