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Database: UniProt
Entry: K2DRR1_9BACT
LinkDB: K2DRR1_9BACT
Original site: K2DRR1_9BACT 
ID   K2DRR1_9BACT            Unreviewed;       446 AA.
AC   K2DRR1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=CBS domain-containing protein {ECO:0000259|PROSITE:PS51371};
GN   ORFNames=ACD_17C00088G0003 {ECO:0000313|EMBL:EKE08591.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE08591.1};
RN   [1] {ECO:0000313|EMBL:EKE08591.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKE08591.1}.
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DR   EMBL; AMFJ01006239; EKE08591.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2DRR1; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR044751; Ion_transp-like_CBS.
DR   InterPro; IPR005170; Transptr-assoc_dom.
DR   PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR   PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF03471; CorC_HlyC; 1.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM01091; CorC_HlyC; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Membrane {ECO:0000256|SAM:Phobius};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..283
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          290..347
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   446 AA;  50584 MW;  88D327DADFADE7ED CRC64;
     MIPDTPLLPL LLLLGSFFLT TCSSAVLRLG RYKSKELLKS RGAPWFFFRS LLHKFFPLHD
     WENLYFCITF SKHIYSLAYA ITAFFYAIST ISGLHHLVDE MPSKEDWAPL LTLGLSIIAL
     SVVFDFLARL MGNVWSKAFL RIAAPFASIY LFVLFPLVGF FLKLARLLIY KTQTEEEGGL
     VTDKGKIREM IKESELQHHL DPSDQRLISS FVNFKERVAK EVMVPRVDVF SIENTTSIKV
     AAKLFAEEGY SRIPVYKESL DDIIGVALYK DLLKCFAKPH FDLNAPIETI VSDVIYVPEK
     KKIAQLLQEF RNKHIHMAII VDEYGGTEGI VTIEDILEEL VGEIEDESDI DEGEEYWALP
     HGGWVIDAKM TLIDIENQLG IKIPASPEYE TIGGYVFHYA GTIPSKGWKL SRDEFDLEVL
     SSNERSLKKI KIIPRSGKAA ESESGI
//
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