ID A0A1H1FBN1_9EURY Unreviewed; 577 AA.
AC A0A1H1FBN1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:SDQ98513.1};
GN ORFNames=DWB78_16275 {ECO:0000313|EMBL:RDI70172.1}, SAMN05216278_3130
GN {ECO:0000313|EMBL:SDQ98513.1};
OS Halopelagius longus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1236180 {ECO:0000313|EMBL:SDQ98513.1, ECO:0000313|Proteomes:UP000199289};
RN [1] {ECO:0000313|EMBL:SDQ98513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|EMBL:SDQ98513.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000199289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|Proteomes:UP000199289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDI70172.1, ECO:0000313|Proteomes:UP000255421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC12-B1 {ECO:0000313|EMBL:RDI70172.1,
RC ECO:0000313|Proteomes:UP000255421};
RA Zhang X.;
RT "Genome sequence of extremly halophilic archaeon Halopelagius longus strain
RT BC12-B1.";
RL Submitted (JUL-2018) 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}.
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DR EMBL; QQST01000002; RDI70172.1; -; Genomic_DNA.
DR EMBL; FNKQ01000004; SDQ98513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1FBN1; -.
DR OrthoDB; 184874at2157; -.
DR Proteomes; UP000199289; Unassembled WGS sequence.
DR Proteomes; UP000255421; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR031919; Fucosidase_C.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
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; PF16757; Fucosidase_C; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 465..564
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 64062 MW; 9F10014E1BB766D6 CRC64;
MADEREVSHS NDGDAQQTTD LVTGLSRRGI LASGGALTLG SLLGVDAAGA TSGKEKEDGR
ESAPETMTGF EEAVAETTER GRHVVEEGPY EPTWASLGDV DPTPEWFRDG KFGIFCHWGP
YSVPAYGHEW YPRQMYNDGH WIHDHHVDTY ERPDAYPYQK FVPEFTAENF DADEWADLFE
RAGACFAGPA AEHHDGWSLW DSKVTPWNAG DRGPKRDLVG ELSSAIRDKG LRFLTTFHHS
YNLRGEEGYF STAYENYPSV MEEYPDRVMY GNLPEELRHE TWFAKLVEAV GQYDPDLVWF
DWGLHWMPEA YRKRFLAFHY NRAAAEDRDV VVTNKDDSLP LDASVEDFEM GRPKTAQEQA
WTAELPVAET GGWGYVEGRT FYSAEFILHT LIDIVSKNGQ LLLSIGPRPD GTIEEAERER
LLSVGEWLET NGDAIYGTRP WEAFGEGPTR LEEGGDFVSD IVYTADDVRY TCDPDTNSVY
AIVMGWPGAG TLTLAGTAVE NASGASSTQS EDEDSSGKPK EGEVTLLGYG RVSHSVDDDG
HLTIDVPGLS TGERPSNIAV TFELSGFDLS PTDAAHR
//
