ID A0A0M1N032_9MOLU Unreviewed; 1294 AA.
AC A0A0M1N032;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:KOR75516.1};
GN ORFNames=CPX_001475 {ECO:0000313|EMBL:KOR75516.1};
OS Candidatus Phytoplasma pruni.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrIII (X-disease group).
OX NCBI_TaxID=479893 {ECO:0000313|EMBL:KOR75516.1, ECO:0000313|Proteomes:UP000037386};
RN [1] {ECO:0000313|Proteomes:UP000037386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CX {ECO:0000313|Proteomes:UP000037386};
RA Lee I.-M., Bottner-Parker K.D., Shao J., Gundersen-Rindal D.E., Zhao Y.,
RA Davis R.E.;
RT "Draft genome sequence of 'Candidatus Phytoplasma Pruni' strain CX, a plant
RT pathogenic bacterium.";
RL Submitted (MAY-2015) 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|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
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:KOR75516.1}.
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DR EMBL; LHCF01000005; KOR75516.1; -; Genomic_DNA.
DR STRING; 479893.CPX_001475; -.
DR PATRIC; fig|479893.3.peg.262; -.
DR Proteomes; UP000037386; Unassembled WGS sequence.
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; cd07432; PHP_HisPPase; 1.
DR CDD; cd07435; PHP_PolIIIA_POLC; 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; 2.
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; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
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; PF07733; DNA_pol3_alpha; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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:UP000037386};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 109..176
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 200..371
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1294 AA; 149927 MW; 907D21D3D98A8127 CRC64;
MTESPIKNNQ SVLIKFFLLD PETKQDSIEY KSFFNQSYKG QTNTFYSQIQ KDFQEGVLVE
IETFVDFNAK NQEYYFNFTP KNGTPKYQIL DNVPLMYQRQ DDYPDKKRIE FHLHTKMSNL
DAVTSVKDYL DIAEKWGHEA LAFTDHNGVY AFPEIEKHLR GKKIKPILGA EFDFIAEKPL
YITNQEQYPQ FPDFILKNHK YVVFDLETTG FSKIRDKIIE ISAVRIENGK ITEEMFDELV
DPQTKLNPRI EEITQITNQD LEGKPTIDAI LPQFLDFAKG YTLIAHNASF DMDFLLENVK
RLGLSYEPQP VIDTMPLSQK YFKQFLKFFS LKRLAKVFKA KPTLEGHSHR ALYDSETTAL
VYIEMMKKLE EREVLTFYDL KGTADTLFER SYHVNVLAKN QTGYQDLFYL ISDALTQDFY
KKPRLLKSKL NQHREGLLVG SGCFDSNVFE TALNNSEQDL AEAIAFYDYI EVQPLNTYKH
VIYDLGGDDP EINALSIVQN TLLKIINEAR KQGKIIIATG DVHYLHQYEK IYREIYINAK
LIGGGLHKLS KFSSENLPDN HLLTTQEMLD AFSFIEDELL RKDLVINNPH LLNQQIDKIQ
ISPQQLFSLQ DDTFAQNLKV PSIKQEMKVL ITTRIEALYG QIVHPLIQER IDKELKSILG
DDNQKDANQN ITPIYYLSYL LVKKSMEDGY SVGSRGSIGS SIIANVLEIT EVNPLRPHYR
CPKCQYTVMK MTEEEKQKPL YQKYLKKDDP NDYDILEHTY SGYDLPDKKC FQCNVNFSKN
GQDIPFETFL GFEGNKTPDI DLNFAGDYQS KAHDYIKELL GEEHVFRAGT IQTVAKRNAY
GYVKGFVKDK GFDEEIRVSE ISRRSTMIEG VKRSTGQHPG GIVVVPKGHK IYEITPVQYP
ADDTESKWKT THFDYHSFEN NLFKMDILGH DDPMLIKFFM DYVKKNPSLF PFDRYQDIPL
DDIKVYELFA NKEKNKTSIA VPEFGTNFVI AMLKDIYDKE KKTFNFSTLV KVSGLSHGTN
VWTQNAKDIL AGKGDFQEDI KKKISFDEVI ACRDEIMNTL IEKGVDALQA FDIMEFVRKG
KPHTHPQEWE KLISPVEATI PQWYLKSLTK IKYLFPKAHA AAYVLMAMRI AWFKVNHPLL
FYSGYFSKRA DQFDYNVMLK TAPEIEKELR QADKNPDDGQ ITMKKTVKNE LTAKEQSRIN
TLKNAYEMVQ LGYQFLPIDL NKSEANEFVI ENDKALRMPF VAIDGLGQVA ADNIVMNRKE
KLFTQDDFVK RVKINKTILK KFKDEMIIER LPEE
//
