ID D4RX05_9FIRM Unreviewed; 443 AA.
AC D4RX05;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=CBS domain protein {ECO:0000313|EMBL:EFF69445.1};
GN ORFNames=BUTYVIB_00356 {ECO:0000313|EMBL:EFF69445.1};
OS Butyrivibrio crossotus DSM 2876.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=511680 {ECO:0000313|EMBL:EFF69445.1, ECO:0000313|Proteomes:UP000006238};
RN [1] {ECO:0000313|EMBL:EFF69445.1, ECO:0000313|Proteomes:UP000006238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2876 {ECO:0000313|EMBL:EFF69445.1,
RC ECO:0000313|Proteomes:UP000006238};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UPF0053 family.
CC {ECO:0000256|ARBA:ARBA00006337}.
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:EFF69445.1}.
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DR EMBL; ABWN01000018; EFF69445.1; -; Genomic_DNA.
DR RefSeq; WP_005601116.1; NZ_GG663519.1.
DR AlphaFoldDB; D4RX05; -.
DR STRING; 45851.BHV86_07530; -.
DR eggNOG; COG1253; Bacteria.
DR HOGENOM; CLU_015237_4_2_9; -.
DR Proteomes; UP000006238; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR002550; CNNM.
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; PF01595; CNNM; 1.
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; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..197
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 285..342
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 443 AA; 49956 MW; 6885B722AD4BDE77 CRC64;
MVYGHFGIGI VLFVFFLTID VILYAFNAAI RTLSPNDIAE SKEGKAKYRE MISKILESPS
RFNDTVNIIV YITNIIAGSY ILGSLARRVI QSVNGDKTWV YIVLAVAMIL VFIIFGVIIP
EKCGRRKPVR TAIRLVKYVR FLMLVLSPVV FVTTMIAKGI LRIFGIKNPD AEENVTEEEI
ITMVNEGQEQ GVLEAGEAEM ITNIFELGDK HAGDIMTHRS NIEAVESTIT LDNFIQNHIE
GKYSRFPVYE GDIDNIVGTI HIRDALIFYR NIPNRKKLLK DIKGLLRKPY MVPETMDIDD
MLKDMQEKKI HMGIVVDEYG QTAGIVSMED IIEEIVGNIL DEYDDEEEVV EYAGDDTYVV
DGLTDIEDIN SLLGIKIESD GFETLNGFLI SKLGRIASEN ETEVIEAYGF SFKILEVTGN
VIRKVEITKI DKKEGIDDEQ LQN
//
