ID A0A3P1WMK2_9ACTN Unreviewed; 1199 AA.
AC A0A3P1WMK2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Alpha-L-fucosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EII42_04925 {ECO:0000313|EMBL:RRD47027.1};
OS Tessaracoccus sp. OH4464_COT-324.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD47027.1, ECO:0000313|Proteomes:UP000274803};
RN [1] {ECO:0000313|EMBL:RRD47027.1, ECO:0000313|Proteomes:UP000274803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD47027.1,
RC ECO:0000313|Proteomes:UP000274803};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RRD47027.1}.
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DR EMBL; RQYZ01000005; RRD47027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1WMK2; -.
DR OrthoDB; 5526311at2; -.
DR Proteomes; UP000274803; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF37; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000274803};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1199
FT /note="Alpha-L-fucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018127677"
FT REGION 1092..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1165
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 130035 MW; 8D7BA19E614526FA CRC64;
MLFKKWARRA AALLAVTVAS TSLPLAQASP TDDLDVWFSG SLVGTSQYTT QGEEAMRGRL
HAVAGGEQQV ADGVKLAGGN QGLRFSPTGV GLGPGETSFA LETQFTPERF SQMDTVLSVA
GNMFVRVQDE QLHYGWSSQT SSGWNNHVAS AELPATGKPH ALSLIYRRTP EQAKLEVFLD
GEALPEVKAD VGYTSSADVA NQVGFGNEVH PAGQSRGMAG TIHRVRFNRI EADARKPLEL
QPSSGATTQL YLDFSGKLTD GTYTPAATET AAGAVTGAGR LADGMIALGA AGEGISFLGD
PNSLAGEDLD AGFVAEVNFT PEPNQTNLGT LLSVGGNFFV RYEGDQLVYG YSGRDSRWHN
YKAGTGAPEP GKPHVLSVAY EPSGTNAKVV VWLDGVALDT LTGQHLSRQA GNTRGVVRLG
NEANSGAGDR VFKGKLDTAR FGLLDGEFKP SAFELQQLKP SEECTTAPEV EPANYVAVER
GHCPETIVAR ASAVRPTEEQ VSWQELELTG FLHFGINTFY DQEWGHGNED PQRFRPTGEV
DVEAWVRQLR DSGFKMGILT LKHHDGFMLW PTRYSDYSVK STPWKEGKGD ILREFTDAAR
KYGLKVGVYI SPADSNAERK GIFGNGSAKR TRTIPTLVPG DDRVGKELPQ FTYEATDYGQ
FFLNTMYEVL TEYGDIDEVW FDGAGGNASG TEAFDYEAYY DLVHQLQPGA LVAVGGRDVR
WIGNEAGLAR IDEWGPVPIR QHSPTGKIDL VGGRLPGKHF QEELSFSDDR LVKLVTSGGV
DSLHWWPGEA DMKLTDGWFA HPNDVPKTPA RLLNHHWDRT VGRNSLLLLN VPPTTTGSFA
PSSVSAIQGF EELRRRAYGV DLALGREALV MRPSTDRKAN RVETTLTDGN TRTGVELRVG
ESVVIDLGSE QQVERISVSE DTLRFGQQVK SWRVEAKVAD TWQEVGRAGT IGVKRILVLR
NPVTTQHLRL TVDEARADRF ALANFTAHQM LAQAPDKPEE IWIDCGAPKA GPGTQDAPLN
SLEQLRNLEL ASGARIHLAS GTVCAASTAP IWAYGTNDKP GVVDIVGGDQ APTVGGRPAA
EWFAPLSERG FDIRLDGSTP QPEPGESPKP GESPKPGESP KPGESPKPVN RRSRVNRRSR
VNRRSRVSHR SRVNRRSRGS SRRVSRLVRS RALLASCTPA PDCPRRGADS GDGQTEPVM
//