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Database: UniProt
Entry: A0A1X7AMF7_9GAMM
LinkDB: A0A1X7AMF7_9GAMM
Original site: A0A1X7AMF7_9GAMM 
ID   A0A1X7AMF7_9GAMM        Unreviewed;       345 AA.
AC   A0A1X7AMF7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA polymerase III subunit delta' {ECO:0000256|ARBA:ARBA00014363};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=holB {ECO:0000313|EMBL:SMA49152.1};
GN   ORFNames=EHSB41UT_03087 {ECO:0000313|EMBL:SMA49152.1};
OS   Parendozoicomonas haliclonae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Parendozoicomonas.
OX   NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA49152.1, ECO:0000313|Proteomes:UP000196573};
RN   [1] {ECO:0000313|EMBL:SMA49152.1, ECO:0000313|Proteomes:UP000196573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA49152.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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};
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DR   EMBL; FWPT01000007; SMA49152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7AMF7; -.
DR   OrthoDB; 9811073at2; -.
DR   Proteomes; UP000196573; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004622; DNA_pol_HolB.
DR   InterPro; IPR015199; DNA_pol_III_delta_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00678; holB; 1.
DR   PANTHER; PTHR11669:SF8; DNA POLYMERASE III SUBUNIT DELTA; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   Pfam; PF09115; DNApol3-delta_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SMA49152.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196573};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SMA49152.1}.
FT   DOMAIN          227..340
FT                   /note="DNA polymerase III delta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09115"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  38938 MW;  23780643107AEB91 CRC64;
     MPSKSGSSKS DTSVPENRLV EPMSWQTDNW QQLSRRLAED QLPHALLLKG QTGVGKRQFA
     LAFAQYVLCQ NKQGEKICGQ CRNCLLNKAG THPDLLLIEP EERGKQIKVA QVRHMIEFTE
     KTPQQGGYRV VVLCPAEGMN TSSANALLKC LEEPGRDTLM LLVSEQVSSL LPTIRSRCQQ
     ILFSRPSTDE ALQWLAHAIP DQERARTLLQ LAAGEPSTAL RYDKEGLLDQ RDAMKSTLAE
     LTRGQKTPAE IAIKWQNYDA VVVLEWLTLW LQEMIRYSAA QDKQFLATED MQKMLAYIAD
     RAGQKTLLET HAWLVKQRSL MLSQVNLNKQ LLLESVLTRW LGLSV
//
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