ID K0YPR8_9ACTO Unreviewed; 1238 AA.
AC K0YPR8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9241_01341 {ECO:0000313|EMBL:EJZ85797.1};
OS Schaalia turicensis ACS-279-V-Col4.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=883077 {ECO:0000313|EMBL:EJZ85797.1, ECO:0000313|Proteomes:UP000003994};
RN [1] {ECO:0000313|EMBL:EJZ85797.1, ECO:0000313|Proteomes:UP000003994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-279-V-Col4 {ECO:0000313|EMBL:EJZ85797.1,
RC ECO:0000313|Proteomes:UP000003994};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces turicensis ACS-279-V-COL4.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC carbohydrate moieties of glycoproteins.
CC {ECO:0000256|ARBA:ARBA00004071}.
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:EJZ85797.1}.
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DR EMBL; AGWQ01000007; EJZ85797.1; -; Genomic_DNA.
DR AlphaFoldDB; K0YPR8; -.
DR STRING; 883077.HMPREF9241_01341; -.
DR PATRIC; fig|883077.3.peg.1355; -.
DR eggNOG; COG1409; Bacteria.
DR eggNOG; COG1470; Bacteria.
DR eggNOG; COG3210; Bacteria.
DR eggNOG; COG3391; Bacteria.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_007212_0_0_11; -.
DR Proteomes; UP000003994; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
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 Gene3D; 2.60.40.2700; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR006585; FTP1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SMART; SM00607; FTP; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000003994};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1238
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003845354"
FT DOMAIN 590..693
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 686..857
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 963..1061
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 630..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 134425 MW; 16E41C954F432A92 CRC64;
MLRRRIVSSL ATAALLIGGG ALSPAFASVQ TSQENVGDIL GAPAAVEKST NERIAAWQKL
QFGLFMHWGV YSMFEGSYKG QRQRIGYPEQ IKAWMNIPRE EYLKEAKKMT ADKWDAAKIC
QTAKNAGMKY VMVTSKHHDG FAMWDTKTTD YNVVKQTAFG KDPMKQLADE CGKIDMKLAF
YFSIIDWEKH EPEPYSNLNP ITEEHLQYNL DQITELLTNY GPIAEFWFDM GRPTAEQSQK
MADKVHELQP NTTVVNSRVW NNKGDFNVGG DNAVHSSFSI GPWESIRSIF PQCWSYCSDS
RANRAAGTAN RVISETISNL VGVVANGGNF AFNVGPMGDG SFPEYDEYVL KELGTWHTDH
PHAIDGASAT WIPAPSNALL TVNGSDLYIF PNQWKSGESI TVPGLANKVT SVTVDGKGTP
VQFARNGLDL TVTMSGESPD KYRPVIKVAL DGEARYVPTQ TVNLDHGSGT IPTRDIVERT
VGASRDAAIL DAYIVDRSGE KYGDVEFDLT QSSGFQDDVE YNVSFNGVTH LFKGIDLKTR
PISGYTMNPN EVSRLRIQLA NPSYYTDALN VKVESIKVAA YKDHAASVAP TFTSQPSDAQ
VVEGESVTFT AGASGRPAPT YQWYRIDADD EDEDEDGAED EDGAEDEDEA ILIEGATNSS
YTFVTTKDDN EADFFVVATN EAGTATSEIA TLTVVDPSLN LALKKPARQS SDSAWNGPAS
RAVDGNTDGK WDNGSVSATA TQNDPWWEVD LEKTVPVGQV NIYNRSADDQ CNGNQSCAER
LKGFYVIASK DKLDDKLSSE EIEKKGEAGE LKYFKVEEKA DFPTSLNFDG YQARYIRVML
PGNWKELNLA EVEVYGQNTA PTAVISAVAD PEEGFSVSGD QLNAVPGSIL TFTAKTSGFP
APKLQWQTSA DGQTWNDVEG QTQQGYSFEI DAKHHGLKVR VAATNSVETA YSEPLTINIV
EKPALTPLSA SLNDSVLEPA DDGAWQKVTV NEGETVVLST TASGMPVPTI AWQSREVSGA
EDSWTPIEGA TTDKLSLKAS KDVQSHLYRA VATNSQGEAV TAPLRVVLHQ QTPTPNPGGD
EPGQADVPTL ELGAAQVKVG DTLSIRVKGL KKGERIKLTV HSEPVVIPES DIKYDDEQGT
AQADWKVPAG FEVGEHTVKV VSKSGESIIK FEVLPADAVP VPDQSNADKP VGDSQPVKKA
SVKKLSSTGA DAVLLAELSA LFLATGVAGF AARRRVRD
//