ID K0IYJ9_AMPXN Unreviewed; 1428 AA.
AC K0IYJ9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000256|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000256|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00356,
GN ECO:0000313|EMBL:BAM47595.1};
GN OrderedLocusNames=AXY_14630 {ECO:0000313|EMBL:BAM47595.1};
OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS / NBRC 15112 / Ep01).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM47595.1, ECO:0000313|Proteomes:UP000006294};
RN [1] {ECO:0000313|EMBL:BAM47595.1, ECO:0000313|Proteomes:UP000006294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC Ep01 {ECO:0000313|Proteomes:UP000006294};
RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity.
CC {ECO:0000256|ARBA:ARBA00003452, ECO:0000256|HAMAP-Rule:MF_00356}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
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DR EMBL; AP012050; BAM47595.1; -; Genomic_DNA.
DR RefSeq; WP_015010194.1; NC_018704.1.
DR STRING; 698758.AXY_14630; -.
DR KEGG; axl:AXY_14630; -.
DR PATRIC; fig|698758.3.peg.1459; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000006294; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd06127; DEDDh; 1.
DR CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR CDD; cd04484; polC_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 2.
DR Gene3D; 6.10.140.1510; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR024754; DNA_PolC-like_N_II.
DR InterPro; IPR028112; DNA_PolC-type_N_I.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00573; dnaq; 1.
DR NCBIfam; TIGR01405; polC_Gram_pos; 1.
DR PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF14480; DNA_pol3_a_NI; 1.
DR Pfam; PF11490; DNA_pol3_a_NII; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 2.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00356};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00356}; Reference proteome {ECO:0000313|Proteomes:UP000006294};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 328..395
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 413..579
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1428 AA; 163023 MW; BFE3E1ECF73CD4B6 CRC64;
MGLSSHEKMN VLLDQINLNV NEQRQYFDQS MLLKLEVFKQ EKRWNFQFQL ESILPIELFK
QFRSKLQEAF KMVATVTFTL NYNDQSISPK VMCDYWQDFI TQEQELSPAY ADHLKECQPK
TDNGQLHIQA RNSAEATVIK NRLTPLFKQY CQQYGLPIWQ LNVYVENEQE QIEKFNEQKA
LEDKLLVKKA METKKEQEKS QENKDELIQI GYPIKEPAVQ MSDIFEEEKR VILQGYIFDV
ETRDLRSGRQ LLMIKMTDYT DSFTVKMFSR NDQDKELFAK IKKGIWVKVR GSIQTDNFSN
ELTMMLSDLN QITYTPKQDR APENEKRVEL HSHTMMSQMD AVVSAKDLVE RAAKWGHPAI
AITDHAVAQA FPEAHLAGLK HGIKVIYGVE VNLVDDGVPI AYNPVDRDLK DATYVVFDVE
TTGLSAVYDT IIELAAVKIK NGEIIDKFER FANPHQPLSQ TIIDLTGITD DMLQDAPEVE
EVLQEFHDWI GDGILVAHNA GFDIGFINQG FQRIDLEKVK NPVIDTLELS RFILPQLKSH
RLNILCKHYG IELTQHHRAI YDTEATAYLL WKLVKEAEEK GITNHNQFNQ HMGEGNAYQR
ARPYHATLLA KNEIGLKNLY KLISMAHVDY FYRVPRLPRS KIIEHREGIL IGSACQQGEV
FETMMQKSIE EAEKVADFYD YIEVQPPANY YPLIEQELVQ NEAQIYEIIR NIVDLADTLN
KPCVATGNVH YLDKEDKFYR QILIKSQKGN PLSRRSLPDV PFRTTDEMLE CFNFLDDDKA
KEIVVTNTQK LANDIEAISP VKKDLYTPNI EGADKEIRDM SYASARKLYG EELPDIVVER
MEKELKSIIG HGFAVIYLIS HKLVKKSLDD GYLVGSRGSV GSSLIATLTE ITEVNPLPPH
YRCPNCCHHE FFTDGQYASG YDLKDKDCPN CGTLYKKDGQ DIPFETFLGF KGDKVPDIDL
NFSGTYQPVA HNYTKELFGE DKVFRAGTIG TIAEKTAYGY VKGYANDHNL HIKNTEVDRL
VLGCTGVKRT TGQHPGGIIV VPEDMDIYDF TPIQYPADDK NSEWLTTHFD FHSIDANLLK
LDILGHDDPT MIRMLEDLSG IDPKDIPVDD EKVMKIFSSP EVLGVTPEQI LCKTGTLGVP
EFGTRFVRQM LEDTNPSTFG ELVIISGLSH GTDVWLGNAQ ELINQGICEL SDVIGCRDDI
MVYLMHQGLD ASLAFQIMES VRKGKGLTDE WVVEMKKHDV PDWYIDSCRK IKYMFPKAHA
SAYVLMALRI AYFKVHHPIL FYAAYFTVRA SDFELDTMIQ GSSAIRKRIE EIYAKGNDAT
PKEKSLVVVL ELALEMNERG FSFAKVDLYR SSATEFLVDG NQLIPPFNAI DGLGTNAALN
IVKAREEGEF LSKEDLRERS RISRTVLDYL DNHGCLEGME EKNQLSLF
//
