ID K0YCY2_9CORY Unreviewed; 808 AA.
AC K0YCY2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE Flags: Fragment;
GN ORFNames=HMPREF9719_01658 {ECO:0000313|EMBL:EJZ81387.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:EJZ81387.1, ECO:0000313|Proteomes:UP000006078};
RN [1] {ECO:0000313|EMBL:EJZ81387.1, ECO:0000313|Proteomes:UP000006078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ81387.1,
RC ECO:0000313|Proteomes:UP000006078};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Turicella otitidis ATCC 51513.";
RL Submitted (AUG-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}.
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:EJZ81387.1}.
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DR EMBL; AHAE01000078; EJZ81387.1; -; Genomic_DNA.
DR RefSeq; WP_004601548.1; NZ_JH815195.1.
DR AlphaFoldDB; K0YCY2; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_3_4_11; -.
DR Proteomes; UP000006078; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000006078};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 34..177
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 371..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 808
FT /evidence="ECO:0000313|EMBL:EJZ81387.1"
SQ SEQUENCE 808 AA; 84651 MW; 0CF92C7D692FF5BD CRC64;
MSLYRKYRPA SFSEVVGQEQ VTRPLSAALD AGRINHAYLF SGPRGCGKTS SARILARSLN
CVHGPTSTPC GECESCRSLA PGGPGNLDVT ELDAASHNGV DDMRELRDRA YYAPAESRYR
VFIVDEAHMI SNAGANALLK IVEEPPEHLI FIFATTEPEK VIGTIRSRTH HYPFRLLTPQ
AMRGLLKRTV EREGVAVDDE VYPLVIRAGG GSPRDSLSIL DQLLAGAGED GLSYDEALPL
LGVTDLSLLD RTVDALAGRD KAALFETVDD VIESGIEPRR FVGDLLDRLR DLMILQAVPE
AIDMGLVDAP ADRAEVLREE AARFTGAQAA ALADQVNSRI ADMRGATSPR LLLEVLLAHL
ALLVEGAGPA PEIQSPDAPQ GAGAAPAAEG EQASSGRYER PSKRAARQAR EAKERARRAA
RGETQPAEQE QQPQGQGERQ AGEQRPEAQP PAEDARPASG SAAPASEATG EEPRPGEARV
DAPHEAAADP AGDNAAGERP AGRPQRAEDQ AASAEASGNA VDEYAADEPA PEAPRADVAE
ARRESAPEDS SGGASDAAPE PTARTSEGED RRAEAPSPEP DEPEDEDPEE EAAAGSDAAA
AASAARPAEA PSGEDAEQRR DEGPAEAADS TEPAEDEPAD EAGRQEGPSD EELAASIREN
WGELREAIRK KNGVAGVMVT EARVLDVRDG TVLLGHNTGA LAARLNAENN NSTVVDVLSE
HAGVPLKAHC QVGTARPGGE GAAPKAGGGD KPRSSGRAEA PRRRERERPA VDDADRGAQP
AEAGNGADRP GGNAGGGAAE DRPARPEA
//
