ID A0A0N0ICD1_9GAMM Unreviewed; 783 AA.
AC A0A0N0ICD1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=M992_0097 {ECO:0000313|EMBL:KPD04401.1};
OS Moellerella wisconsensis ATCC 35017.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Moellerella.
OX NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD04401.1, ECO:0000313|Proteomes:UP000053226};
RN [1] {ECO:0000313|EMBL:KPD04401.1, ECO:0000313|Proteomes:UP000053226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD04401.1,
RC ECO:0000313|Proteomes:UP000053226};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (JUL-2015) 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,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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:KPD04401.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGAA01000002; KPD04401.1; -; Genomic_DNA.
DR RefSeq; WP_047255153.1; NZ_LGAA01000002.1.
DR AlphaFoldDB; A0A0N0ICD1; -.
DR GeneID; 79716113; -.
DR OrthoDB; 5807460at2; -.
DR Proteomes; UP000053226; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05784; DNA_polB_II_exo; 1.
DR CDD; cd05537; POLBc_Pol_II; 1.
DR Gene3D; 2.40.50.590; -; 2.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF21474; DNApolII_N; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000053226};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 382..756
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 783 AA; 90208 MW; 50B0C1218C36A3EF CRC64;
MTLSSSPPEK GFVISRHWKD TPEGVQVSYW LLTENGPRYV TVPTQQAIGF IATHSRQYVA
PVLAQYQGVE LRSLALKDFN QHPVDGIYCR QYRQLLQIEK QLVTLGYKVY ETDIRPADRY
LMERFITAPV WFSPLGKQRY QLKPCEHYRP NIRCVSLDIE TSQHGELYSI GLSGCDDDVV
FMLGPDQGPA HSSEYRLEYL SSRPALIEQL NLWFQKNDPD AIIGWNLIQF DLRILQQHAE
RYGLILKLGR NNKALEWREH GFKPGVFFAA AEGRLIIDGI EALKTATWSF SSFSLEFVAQ
SLLGEGKSID TPYDRMDEIN RRFQHDKPAL AHYNIQDCIL VTRIFAATHL IEFLLERASV
TGLNADRSGG SVAAFSHLYI PRLHRVGYVA PNQGEKIEEA SPGGFVMDSQ PGLYDSVIVL
DYKSLYPSII RTFMIDPVGM IEGLAQPELS HSIPGFRHAW FSRQTHCLPA IVSQIWQARD
RAKVTANAPL SQALKIIMNA FYGVLGSAGC RFFDPRLASS ITLRGHEIMR KTRELIESQG
YQVIYGDTDS TFIWLKQPHS EQQAKQIGYQ LRDFINQWWQ QHLQSTLNID SVLELEFETH
YRRFLMPTIR GTEQGSKKRY AGLSGDKMIF KGLETIRSDW TPLAKTFQTE LYTRIFHQQP
YREFILEYVH KIRRGELDEH LIYRKRLRRK LSDYQRNVPP HVRAARLADD FNLRHQRPQQ
YQNGGWISYI MTQAGPEPLE VTTAAPDYEH YINKQIMPIA DAILPFLQDD FTTLLTGQMS
MPF
//
