ID E9SF85_RUMAL Unreviewed; 518 AA.
AC E9SF85;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Ricin-type beta-trefoil lectin domain protein {ECO:0000313|EMBL:EGC02078.1};
GN ORFNames=CUS_5297 {ECO:0000313|EMBL:EGC02078.1};
OS Ruminococcus albus 8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC02078.1, ECO:0000313|Proteomes:UP000004259};
RN [1] {ECO:0000313|EMBL:EGC02078.1, ECO:0000313|Proteomes:UP000004259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:EGC02078.1,
RC ECO:0000313|Proteomes:UP000004259};
RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC {ECO:0000256|ARBA:ARBA00038263}.
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:EGC02078.1}.
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DR EMBL; ADKM02000112; EGC02078.1; -; Genomic_DNA.
DR RefSeq; WP_002851631.1; NZ_JAJFOM010000001.1.
DR AlphaFoldDB; E9SF85; -.
DR STRING; 246199.CUS_5297; -.
DR eggNOG; COG3266; Bacteria.
DR eggNOG; COG3693; Bacteria.
DR OrthoDB; 8660908at2; -.
DR Proteomes; UP000004259; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Lectin {ECO:0000313|EMBL:EGC02078.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..518
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003243621"
FT DOMAIN 42..181
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 185..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 53775 MW; 8804FCC900A9C652 CRC64;
MSRFSIAKKL TSAAAAVGIA VSALTTAVPL NAFAASNYIS DGWYYIKNVN SQKYLDVSGK
KDADGSNVIQ YKGNGGNNQK WYVTNLGNNV ITIRSGLKGG RMLDVENGAN TDGANIRLWS
ANGADAQKFK VVKSSSGVYC LKTENSGESK AVDVYGWSTE DSANINQWTY NGLACQQFKF
ESTSAGASKS SGSSSSSSSS SSSSSSSSSS SSSSSGSSLE VKNGGTSLSS ALSKAKKGDT
VVINGTVKSG AVKVPAGVNI SGKNSAVIDF SSTSGSNGRG LTFEGNGSTV QNVCIKNASD
NGLYITGSNN TFKNVEACYN KDAGFQVCNG GSNNKFYSCH SHHNADAKGE NADGFANKLH
SGAGNYYENC IADYNSDDGW DCYAAHGAVT LVNCQANYNG YCDGIYGDGN GFKMGGVDNK
TDGEKAHLDP LNHVLKGCTA KGNYASGFDR NNQNGVVTME NCTGDSNKKY NFNWPASGTP
SALGYKVTFG VAKIISCTSK NGKNNIGGAK LSGNCSGF
//
