ID A0A2V5IPH2_9MICC Unreviewed; 922 AA.
AC A0A2V5IPH2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CVS30_10275 {ECO:0000313|EMBL:PYI38498.1};
OS Arthrobacter psychrolactophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=92442 {ECO:0000313|EMBL:PYI38498.1, ECO:0000313|Proteomes:UP000247980};
RN [1] {ECO:0000313|EMBL:PYI38498.1, ECO:0000313|Proteomes:UP000247980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:PYI38498.1,
RC ECO:0000313|Proteomes:UP000247980};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PYI38498.1}.
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DR EMBL; QJVC01000008; PYI38498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IPH2; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000247980; 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; cd06140; DNA_polA_I_Bacillus_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; 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 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.
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:UP000247980};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 38..298
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 342..511
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 678..885
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 922 AA; 100289 MW; 2FF5465AD42B63D2 CRC64;
MMTRLALVSE SAKTAPQSSA SPSPLASPVF GLQEGATPRL LVLDGHSMAF RAFYAMPVDK
FVTQAGQYTN AVHGFTAMLL TMIRQQKPTH VVVAFDLDTP TFRSLDYTEY KGGRNKTPEE
FYGQIDLIIK VMEAMRIPTI SVDGFEADDI IATLSTQGET AGWDVVVVSG DRDAFQLITD
KVSVLYPKKG ISDIPPMDAA AVEAKYFVSP ARYSDLAALV GETADNLPGV PGVGPKTAAK
WINLYGGLEG IFENIDAIGG KVGDSLRAHI EDVKRNRRLN HLLRDMELPV ALEDTVLQSP
DRDAVEELFD ALEFNQLRKR LFDLFGEEEA LDAGATHEVP AHQLVSDAAA LNAWVEATTG
LVAVDVVSEK VGLAHEATAV ALVGQESAVV VDLGTADAAL DSALAAWLLS DAPKVVHEYK
EALKALSVRG LSLGGVVDDT SLSGYLIQPD RRSYELAELS QVHLKVSFEA EATADAGQLD
LGLESEKKYD EAVQRGYVAL LLSEYFAPLL QERSAAVLLR ELELPLAAIL ARMELTGIDV
SQERLAVLLD DFTTAMNAAK EAAYAAIGHE VNLGSPKQLQ EVLFEELALP KTKKIKTGFT
TDAASLKWLL EKTGHEFLAQ LMAHREASKL KQMVETLKKS LAEDGRIHTT YAQNVAATGR
LSSNNPNLQN IPIRTEEGRR VRDIFVVSEG YECLLAADYS QIEMRIMAHL SGDAGLIQAY
AEGEDLHRYV GSHVFGVAPE DVTSAMRSKV KAMSYGLAYG LTSFGLSKQL EISVDEARTL
VKDYFDRFGG VRDYLRGVVE QARKDGFTST IEGRRRYLPD LSSSDRQLRE LAERIALNSP
IQGSAADIIK HAMLGVAAQL QAQELKSRML LQVHDELILE IWPGELETVK ALVIAQMGAA
ADLLVPLEVQ VGVGSSWNDA GH
//
