ID A0A2G5DU40_AQUCA Unreviewed; 1232 AA.
AC A0A2G5DU40;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=AQUCO_01400021v1 {ECO:0000313|EMBL:PIA47018.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA47018.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA47018.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-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}.
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DR EMBL; KZ305031; PIA47018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5DU40; -.
DR STRING; 218851.A0A2G5DU40; -.
DR InParanoid; A0A2G5DU40; -.
DR OrthoDB; 3675885at2759; -.
DR Proteomes; UP000230069; 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:InterPro.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 466..616
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 29..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 742..772
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 31..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 136723 MW; 6337D2F02F8E3808 CRC64;
MSDFRDMSDE LHWKKELTAL RKAARILRDP ETTSSLRSPL SSRTAAGGST LNYLGGTRGP
STARCQTGRY SELDSSSSSL KCTNTQKQVF LYNWRQPPSK SSDSGAKVDE CRNFGNGEPM
PGTSGDSSSD TNKVGSKSDT CHDEHVILSS EANFKTSTQK TVKKSKKNSA VSRRTVKRSA
NSKLLDYPSI SIEQSDDTEY CNSEDLRIST HDMMRKSGYT SKPASPLLSK RENRSYSSKL
IPKVHREDSS FSCTPASTSS YNRYRKKNHS TAESCGNTTA SFNEDEADHL DLSRRQGCGI
PCYWSKRTPK HRGCGVCYSP SLSDTLRRKG SRIFCGSQIL NEKRQSSRSN KRKLVKKSSQ
GLPLLTNSCD GRGGSSIDSG ESDDELSTNF GELDLEALSR LDGRRWSMSC GSQEGLELVA
LTGSDQGTPD HVRSLSQKYK PRFFDEIIGQ NIVVQSLINA TSRERIAPVY LFQGPRGTGK
TSTARIFSAA LNCLATEETK PCGSCRECTN FISGKGKDLR EVDATNKKGI DRVKYLLKSL
SMAPPSYFSH YKVFIVDECH LLPSKTWSEF MKFLEEPPAH IVFIFITTDL DNLPRTVLSR
CQKYLFNKIR DADVVTRLKK LSDTENLDVE SHALHLIALN ADGSLRDAET MLEQLSLLGK
KITASLVNEL VGVVPDEKLL DLLELAMSSN TAETVRKSRE LMDSGVDPMA LMSQLAGLIM
DIIAGTYHLV DSKCSGSFFG GRSLTEAELE RLKQALKLLL EAEKQLRVSS ERSTWFTAAL
LQLGSVPSPD PSHSSSSRKQ SSKTTVEDQS NTSWELYAHK KKLNAQHMLQ KSVSSSASSP
RTVDERCGPS SHPRLLVDSS SLDARPHYSR VVEGGTSVLG ESKVLRCLNP EKLDDIWNKC
IERCHSKTLR QLLHAHGKLV SISEVEGVLL AYIAFEDGDV KSRAERFLSS ITNSLETVMR
HNVEVRLGLI GDSETSINRR RPLLPDSSEL KTQEISGMVD RESNEEFSKL ARGTPKRSDG
SVTVVDGFNQ VTTALPMYSE EEKHGNRKER KQDTPMQRIQ AIIDEQRLES AWLQAAKGST
PRSLSRLKPE KNQILPQDGN SRQNEIASMI LTGVSSRKWE DELNREIKAL KINDTRGQQK
EKTGQRFDHI SMSPSLLHNR GYVGNFDKEN LGYESGTSGG GGVNGVLCWK RSKHSKKGRV
KAGTPVRLQK KKQFSCFGQC GKASKGNKKL KR
//
