GenomeNet

Database: UniProt
Entry: A0A088QDY9_9CORY
LinkDB: A0A088QDY9_9CORY
Original site: A0A088QDY9_9CORY 
ID   A0A088QDY9_9CORY        Unreviewed;       510 AA.
AC   A0A088QDY9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=AAA domain family protein {ECO:0000313|EMBL:AIN81480.1};
GN   ORFNames=DR71_1998 {ECO:0000313|EMBL:AIN81480.1};
OS   Corynebacterium sp. ATCC 6931.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN81480.1, ECO:0000313|Proteomes:UP000029247};
RN   [1] {ECO:0000313|EMBL:AIN81480.1, ECO:0000313|Proteomes:UP000029247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP008913; AIN81480.1; -; Genomic_DNA.
DR   RefSeq; WP_038628667.1; NZ_CP008913.1.
DR   AlphaFoldDB; A0A088QDY9; -.
DR   STRING; 1487956.DR71_1998; -.
DR   GeneID; 64051049; -.
DR   KEGG; coa:DR71_1998; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_0_11; -.
DR   Proteomes; UP000029247; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR004482; Mg_chelat-rel.
DR   InterPro; IPR025158; Mg_chelat-rel_C.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR   PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR   PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13335; Mg_chelatase_C; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029247}.
FT   DOMAIN          212..389
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   510 AA;  53998 MW;  07DB3F74EB086E07 CRC64;
     MTVGTALAVS LSGIEGTIVQ VEADVGRGLP GMYIGGLGDA AVGEAKHRVR TAVANSQLLW
     PKTKVVVSLS PAHIRKHGTS FDLAIVCAIL IATNDDMEAR GRLRQTVLIG ELGLDGSIRP
     VLGVLPQVLA AREAGARWVI VPAANAAEAA LVDGIAVCTA ADLTQLWGWV LTGSGLRTAL
     NDDPSEQTFS VDLADVDGQS EARFALEVAA AGGHNLFMQG SPGTGKSMLA ERLPTILPPL
     QKWQQLEVTA LHSVAGALDN RDTLVQHPPF VAPHHSATVA ALVGGGAVPK PGALSLAHHG
     VLFLDEITLM RPAVLDALRM PLENGVVVHL RTHHRMTFPA RAQLVMATNP CRCGAAYASE
     CTCSSAERAK HGRALSGPLR DRMDLNVTLS PAGANLGIRN KADNEPSAAV RERVQAARDR
     ACRRWQGLGL ADEVAVTNAS VPRSLLRRHA GLDEEAMALL DFQLRKGEIT QRGVDKVIAV
     AWTLADLEGI DAFTFEHVQR ACKLHDREGG
//
DBGET integrated database retrieval system