ID K9V0L8_9CYAN Unreviewed; 979 AA.
AC K9V0L8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=Cal6303_1913 {ECO:0000313|EMBL:AFZ00947.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ00947.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ00947.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ00947.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; CP003610; AFZ00947.1; -; Genomic_DNA.
DR RefSeq; WP_015197593.1; NC_019751.1.
DR AlphaFoldDB; K9V0L8; -.
DR STRING; 1170562.Cal6303_1913; -.
DR KEGG; calt:Cal6303_1913; -.
DR PATRIC; fig|1170562.3.peg.2090; -.
DR eggNOG; COG1372; Bacteria.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_2_0_3; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000010477; Chromosome.
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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 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; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02397; dnaX_nterm; 1.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_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; 2.
DR Pfam; PF12169; DNA_pol3_gamma3; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00023000};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 337..359
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 599..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 105935 MW; 9DBCD2D5F79E6A41 CRC64;
MSYEPLHHKY RPKSFAELVG QEAIATTLTN AINTAKIAPA YLFTGPRGTG KTSSARILAK
SLNCLKSPIP TASPCGVCDV CQGISKGYAV DIIEIDAASN TGVDNIREII DRAQFAPIQC
RYKVYVIDEC LTGDSLVLTS EGFVRIDDAK IVGKKALSYN DFTGDWEYKK VVRWFNQGHR
QTLAIKTTNG EIRCTGNHLI RTDAGWIQAK DVKEGMRILS PANAVAEPSF TNMVSMGASG
NLSEDTSSNV IPTDKKHTTS KKFWNKLNNF VPFVLADAKK SLISQNFCSK KAKLTTTSTW
ELILPENGSQ NSNSSLFPQW NTNLEKVESV HLAGVERVYD IEVEDNHNFV ANGLLVHNCH
MLSTQAFNAL LKTLEEPPKH VVFVLATTDP QRVLPTIISR CQRFDFRRIP LDAMIDHLGD
ISDKEGIEIT DEALTLVAQL SQGGLRDAES LLDQLSLLPT MVTPERVWDL VGLVSERDLF
ILLDAIASDN AETLIDCTRK ILDRGREPLI VLQNLAGFYR DLLIAKTAPK RHDLVACTQE
TWDDLVYFAK SLHISTILAG QQILRSAEVQ LKNTTQPRLW LEVTLLGLLP SAQQPLTTVS
APTGFSPPSN APAASPPSNI PVASPPSNIP AASPPSNVPV ASPPSNVPVA SPPSNVPVAS
QPVTDDEQQD LNQTWQQVLN FVEQIPSRSL LRQMCHIIQI NDTSVRLGVI QTWMKRVQGE
LPILNAAFKA AFNREITIEL ELVGSQNPSK ASRNNPKSAS TRPANPPSQN PPASTNGNGT
TQNPPPSTSD NGEIQNPPPS TNGNGATQNP PTSANGSNGY EYINGNGNGT SQTSPPSNGN
GTNSISSAST NGNNGNGYTN GNGNGISQIP PASNNSSSSS NGYGNGYTNG NGKTQTPADF
SKPTNIPKSE PSVVAKSSEI LIPSTPTEKH PEADRVIDAA KRLAEFFYGE VVKYSENMEE
SIDSSVSSEY TDDFEVDND
//
