ID Y997_RICBR Reviewed; 614 AA. AC Q1RHT6; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Putative ankyrin repeat protein RBE_0997; GN OrderedLocusNames=RBE_0997; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group. OX NCBI_TaxID=336407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RML369-C; RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in RT gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:733-744(2006). 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; CP000087; ABE05078.1; -; Genomic_DNA. DR RefSeq; WP_011477658.1; NC_007940.1. DR AlphaFoldDB; Q1RHT6; -. DR SMR; Q1RHT6; -. DR KEGG; rbe:RBE_0997; -. DR eggNOG; COG0666; Bacteria. DR eggNOG; COG2071; Bacteria. DR HOGENOM; CLU_444717_0_0_5; -. DR OrthoDB; 9813383at2; -. DR Proteomes; UP000001951; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR011697; Peptidase_C26. DR PANTHER; PTHR24189; MYOTROPHIN; 1. DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 3. DR Pfam; PF07722; Peptidase_C26; 1. DR SMART; SM00248; ANK; 9. DR SUPFAM; SSF48403; Ankyrin repeat; 2. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 5. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1. PE 4: Predicted; KW ANK repeat; Glutamine amidotransferase; Reference proteome; Repeat. FT CHAIN 1..614 FT /note="Putative ankyrin repeat protein RBE_0997" FT /id="PRO_0000280921" FT REPEAT 3..32 FT /note="ANK 1" FT REPEAT 36..65 FT /note="ANK 2" FT REPEAT 69..98 FT /note="ANK 3" FT REPEAT 102..131 FT /note="ANK 4" FT REPEAT 135..164 FT /note="ANK 5" FT REPEAT 168..197 FT /note="ANK 6" FT REPEAT 201..231 FT /note="ANK 7" FT REPEAT 239..268 FT /note="ANK 8" FT REPEAT 272..301 FT /note="ANK 9" FT DOMAIN 348..580 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 444 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605, FT ECO:0000255|PROSITE-ProRule:PRU10055" FT ACT_SITE 547 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 549 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" SQ SEQUENCE 614 AA; 69008 MW; DE4BA38CA195140C CRC64; MNKDEELLIE AIENDDLKEV QKLLQEGVDP NILDEDDKPC ILSAIRNKNL DIVSVLLENG ANPNAVDADG EPIISAAIRT KRLDIINILL ENRADPNLQP PRKNTILLKA IQSNNLDIVN AFLNKGANLN ALDISGYPIF LKAIKSENLE IINALLEKGA NPNLVDKDGS PLLFTAINTK NLDIIDALIK MGANVEAKNK DGNTVLNVLL ERRGNVNIIS LLIENSQDKE KIFNLKNNNG ETFLHLAAQQ GNSKIFDKYL DYYPTVNITD KAGYTPLYWS KLLGHTEISN KLIERAEELK ETVYTKVTRT KFFENLPSIP KIAVSYNSKV RGETSEATRN KLKYQYCNVE DIDYRKIVPE SANAEKKINE EIVNEAKRKA KEFLADKDAL VIPGNNSSVD PKIAEHFGGQ VNLEKNKFDF ARSLAEMAML EVAIEKGMPI MGICGGHQII NAYLKGKIDE VSKHKHDSII IEPDSELASI IKRNSPTKDI LNQEFWGMHN DKVQEIGGKN RLIDNKDLLK VTATNEHREI EATESQFGAP IRTFQFHPEM SKTTYSNAEI IRDKKIFASF VQSAETFMNK KSLGADIKFK VPVKKSFTEM VLNRKEQQNN QRGI //