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Database: UniProt
Entry: A0A2N0ZYM8_9GAMM
LinkDB: A0A2N0ZYM8_9GAMM
Original site: A0A2N0ZYM8_9GAMM 
ID   A0A2N0ZYM8_9GAMM        Unreviewed;       814 AA.
AC   A0A2N0ZYM8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=CXF74_18095 {ECO:0000313|EMBL:PKG37597.1};
OS   Psychromonas sp. Urea-02u-13.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=2058326 {ECO:0000313|EMBL:PKG37597.1, ECO:0000313|Proteomes:UP000233836};
RN   [1] {ECO:0000313|EMBL:PKG37597.1, ECO:0000313|Proteomes:UP000233836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Urea-02u-13 {ECO:0000313|EMBL:PKG37597.1,
RC   ECO:0000313|Proteomes:UP000233836};
RA   Collins E., Ducluzeau A.-L.;
RT   "Pharmacopeia of the Arctic Ocean.";
RL   Submitted (DEC-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};
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|ARBA:ARBA00006360}.
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:PKG37597.1}.
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DR   EMBL; PJBZ01000097; PKG37597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0ZYM8; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000233836; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis 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:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR021029; DNA_pol_III_tau_dom-5.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038249; PolIII_tau_V_sf.
DR   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   Pfam; PF12170; DNA_pol3_tau_5; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          37..179
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   814 AA;  89909 MW;  090EDD9DF19ECF3E CRC64;
     MSYQVLARKW RPHNFSQVVG QQHVLTALSN GLTQNRVHHA YLFSGTRGVG KTTIARILAK
     SLNCEQGVTA TPCGKCENCV AIDQGRFVDL LEIDAASRTK VDDTRELLDN VQYKPAVGRY
     KVYLIDEVHM LSKHSFNALL KTLEEPPEYV KFLLATTDPQ KLPITVLSRC LQFHLKAILP
     DQIEAQLAHI LKHEDATFEY TALNVIAKAA DGSMRDALSL TDQALAFGAG NIEYQSVLKM
     LGTLDNSHLH YLLHFIASGN VAKVFQKIEE FVVLGADFAK LHQELAGLCH QIALQQLQRP
     QANSEKSAIQ LLSERLSPEE VQLYYQIALE GYKDYRFAPN GKVALEMTVM RLLAFKPANY
     IELDEKALVN NTLVNTTVQS EGNIDLPSFN PAPESIQPAA LIETTPVVEQ VSVIGNDSSP
     SLPETRLPEP APVTVVETLT AQEMPVPTPV IETSPVQDVS SQPMPNQQAP SQQAVIETPP
     VQEAPANSPA VEVAAPITEA VPVPVKSEPV LESSNSRNML RSHRLKRNET KKSQATTDHV
     ISTPVVAALP KVDNIIPDVA AKKTDLPITP VIQTDNVTSA PNRQNFSPEL PPIEQYQESE
     QADNRFDSQF DSPYDQFENN SYDPYSPPEE MQSVNTQVAA LPSVSNNVQA PVIDNSALNT
     GIVTKHASFS DQHFEAVEID KAKYVEDKLT DSWSLAIQTM QVRGLVKLLA KNSVMKKVDD
     QIVLTLKAEH QHLLNNSGLC EELQMQLKSF YGAQYNMYIE VGNVEGQLTA FESEMALYEQ
     YLNNAKHAIV DDENIKALVA NCGAKVYENS VIPL
//
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