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Database: UniProt
Entry: B2GH54_KOCRD
LinkDB: B2GH54_KOCRD
Original site: B2GH54_KOCRD 
ID   B2GH54_KOCRD            Unreviewed;       588 AA.
AC   B2GH54;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Putative DNA polymerase {ECO:0000313|EMBL:BAG28806.1};
DE            EC=2.7.7.7 {ECO:0000313|EMBL:BAG28806.1};
GN   OrderedLocusNames=KRH_04590 {ECO:0000313|EMBL:BAG28806.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG28806.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG28806.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
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DR   EMBL; AP009152; BAG28806.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2GH54; -.
DR   STRING; 378753.KRH_04590; -.
DR   KEGG; krh:KRH_04590; -.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_035229_0_0_11; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd06444; DNA_pol_A; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:BAG28806.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW   Transferase {ECO:0000313|EMBL:BAG28806.1}.
FT   DOMAIN          342..547
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   588 AA;  63077 MW;  2D2CDC86804261FD CRC64;
     MNPMHIVVAA AEPGTWVLQV VSANGERAGQ ELTVADAELP GVVAQREEAA ARAGVQPPVW
     TWQDTSVPAA LLCAAGVWVT RCRDLGLCAT ILATASTAPG SGAPDDAGEP RPLAYRPVLE
     PADPRHVPGP RPLAPASNQG SLFAVAEEHG PGVTELIAEL AAQTSACATA RNPQRLERLL
     SLESQGALVA ADMRHRGIPW NPAVHQQILE DMLGTRPAGE ERPARMQELA QEVRTALAAP
     ALNPDSPVEL LKALRNAGVD VDTTRAFKLQ EWTLVNGQPQ EQRVATVTPV LEYKKLSRVF
     SATGWHWLDT WVHEGRFHPE YVVGGVVTGR WAARGGGALQ IPKYIRDAVR ADPGHALVVA
     DAAQLEPRVL AILARDDALA EASRGRDLYT AIAEQGQARG SELTERSHAK LALLGAMYGA
     TSGAGGRFMP QLTRMFPRAV GYVEHAARVG ELGHQVCTYL GRWSPAPGPE WFEVQRATDT
     QAGERRAAQA SRSHGRFSRN FVVQGSAAEW ALAWLGHIRQ GLHGADVDAE LVFFLHDEVM
     VHCAEQHADR VQQIVEHAAG QAVHTVFGTV PVEVPVATTV VTSYADAK
//
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