ID A0A143HPX9_9GAMM Unreviewed; 916 AA.
AC A0A143HPX9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3224_15370 {ECO:0000313|EMBL:AMX03783.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX03783.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a defensive agent. Recognizes blood group fucosylated
CC oligosaccharides including A, B, H and Lewis B-type antigens. Does not
CC recognize Lewis A antigen and has low affinity for monovalent haptens.
CC {ECO:0000256|ARBA:ARBA00002219}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the fucolectin family.
CC {ECO:0000256|ARBA:ARBA00010147}.
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DR EMBL; CP014864; AMX03783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143HPX9; -.
DR STRING; 252514.A3224_15370; -.
DR KEGG; mthd:A3224_15370; -.
DR Proteomes; UP000076077; Chromosome.
DR GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR GO; GO:0001868; P:regulation of complement activation, lectin pathway; IEA:UniProt.
DR CDD; cd04080; CBM6_cellulase-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR006585; FTP1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006626; PbH1.
DR PANTHER; PTHR45713:SF6; F5_8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45713; FTP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00607; FTP; 1.
DR SMART; SM00710; PbH1; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50022; FA58C_3; 2.
PE 3: Inferred from homology;
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Reference proteome {ECO:0000313|Proteomes:UP000076077}.
FT DOMAIN 1..138
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 141..290
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 301..436
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 314..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 98320 MW; B97C67B3F36C7D2E CRC64;
MLSSLYGVSA FAIDPVSVTA SSNDGNIPEN TLDNNLETRW SAIGDGQWIE YDLGKNYIVK
DVQIAFYKGD QRTATIEIQV SSDGNTWESL FYGDQPSKTL DLQIFDVDDT EARYVRIVGY
GNTSNNWNSF TEVAISASEV ASGEIVNLAL GKSTSQSSTD YSGISSRAVD GDVRGNWSSN
TITHTENEIQ PWWQVDLGSV STISTINLYN RTDSCCSSRL SNFYVLVSDK PFSSNDLNVL
LAQDDVASYY YGSTAGSPTS IDINRSGRYV RVQLAGSNPL SLAEVEVYGV EATGSLFIVP
GKIEAEDFGS YADADSENRG GAYRPDEGVD IQETTDSGGG YNVGWMDAGE WLEYPIYVSN
TGEYSAQLRL ASPSDTGQIS IEVDGVVVAQ HGVASTGGWQ NWNTEEVYLG NISAGTHTLR
INVESAAFNL NWLNIIDNDS SIREGATYVG GGGTVAGALP ISCETPAGFT LVDSLPEMIE
AMGKNNVKVA LKPGTYVIDE SDTSLFTSQS LPGGKAASTL LPVDGHNSHY DFRCAYIKFD
TDLWRQFGKN EVIQLRTVGN YNTISNLSIE DIGDTSPSGG ALGVMMDGRD NVIEGLIITS
RGSQPYGLGD AYGKGAGPVL SHQKHSSVLI RGLRNTFRNS TVFNYSYGHS VFMQGSEDTL
IDGIYVQGEL RSTEDMLAAN NPRFAAADAR AASVDFMTVW GYKLPTGYWM SLQEAGIRAY
NGGNTIIDGV EYERGADTVT VLNSVIRNTR TGVTLVHATG SKYVENTTVI GCEQGYSIGS
GNIVNSYADA DVGPVITFAY SSDNGTKADI TVLPTDGSKN GWGALAFIGG KNHDITLRSS
QTDIPSNLQV VLSGDKHSIR HLEDSLQNQD QLTLTSSVVN NLTNFPVLIN NLASGVNGQS
NGPVSGNTSD NNIQQN
//