ID C6VY20_DYAFD Unreviewed; 423 AA.
AC C6VY20;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=AAA ATPase central domain protein {ECO:0000313|EMBL:ACT96921.1};
GN OrderedLocusNames=Dfer_5733 {ECO:0000313|EMBL:ACT96921.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT96921.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT96921.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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DR EMBL; CP001619; ACT96921.1; -; Genomic_DNA.
DR RefSeq; WP_015815161.1; NC_013037.1.
DR AlphaFoldDB; C6VY20; -.
DR STRING; 471854.Dfer_5733; -.
DR KEGG; dfe:Dfer_5733; -.
DR eggNOG; COG2256; Bacteria.
DR HOGENOM; CLU_017985_0_3_10; -.
DR OrthoDB; 9778364at2; -.
DR Proteomes; UP000002011; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002011}.
FT DOMAIN 41..153
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 423 AA; 47257 MW; C8D7F6543FF4CEEE CRC64;
MNTITTPLAE RLRPRTLDDF VGQEKLLGPK GPLRRAILQN AIPSMIFWGP PGVGKTTLAL
LIAETTKRQF YNLSAISSGV KDLREVLARP SGLFPAILFI DEIHRYNKSQ QDALLGAVEK
GQVTLIGATT ENPSFEINSA LLSRCQVYIL EAFGEKELKG LIARALEKDP WLKEKNIKFA
SYDALMRLSG GDGRKLLNLL ELVVLGKGDA KKIEITDEWV TEVAQQNIAR YDKSGEQHYD
IISAFIKSLR GSDPNGAVYW MARMIVAGED PSFIARRMLI MASEDIGNAN PTAMIMANAC
MQAVNVIGYP ECRIILSQTA VYLATSPKSN ASYMAIGEAI EAATRTAHLP VPLHLRNAPT
KLMKQIGYGK DYKYSHSYEG NFAKQDFLPD ELKGTRFFEP GHNSREEEIR KKLQHWWGDW
YGY
//