ID D6GSM1_FILAD Unreviewed; 410 AA.
AC D6GSM1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=CBS domain protein {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=HMPREF0389_00579 {ECO:0000313|EMBL:EFE28662.2};
OS Filifactor alocis (strain ATCC 35896 / CCUG 47790 / D40 B5) (Fusobacterium
OS alocis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Filifactor.
OX NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE28662.2, ECO:0000313|Proteomes:UP000007468};
RN [1] {ECO:0000313|Proteomes:UP000007468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., Izard J.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL Submitted (DEC-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}.
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DR EMBL; CP002390; EFE28662.2; -; Genomic_DNA.
DR RefSeq; WP_014262620.1; NC_016630.1.
DR AlphaFoldDB; D6GSM1; -.
DR STRING; 546269.HMPREF0389_00579; -.
DR KEGG; faa:HMPREF0389_00579; -.
DR PATRIC; fig|546269.5.peg.1054; -.
DR eggNOG; COG1253; Bacteria.
DR HOGENOM; CLU_015237_4_1_9; -.
DR OrthoDB; 9798188at2; -.
DR Proteomes; UP000007468; Chromosome.
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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000007468};
KW 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 55..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..183
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 202..261
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 267..324
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 410 AA; 46967 MW; C4F5785A86DDBA36 CRC64;
MQITILVALL FFSAFFSMSE TALMSMSKIR LRHLVENHVK HAKLTQDLLD HPNQLLGTIL
VGNNLVNIAA SAIATSIAIY FWNNKGVGIA TFLMTLLILI FGEITPKNIA IDYTEEIVLF
IAPIMSVFVK IFSPVVWILT NFTNGLLHLF GLNKQEKKPL ITEEELKTIV EVSSQEGVLE
SDEKEIIDNI FEYSDMRVKD IMIQRMDIVA VDVSATYEEV VEAFGEKQFS RIPVYEDTID
NIVGVLYAKD LFFIPVEKIK QFDIKKYMRE PFYTYEFIKI SDFFRRMQGD RIHIAIVLDE
YGGVAGIITM EDIIESILGD INDEYDPQDE EDIVCIKEGE YLVNGSVRLE DLNEEIGTHF
ESEDFESIGG FILGILGRIP RTGEIINYES IRFVIEKVDK SRIMKIRLFY
//
