ID A0A2U2ZKM3_9ACTN Unreviewed; 660 AA.
AC A0A2U2ZKM3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:PWI12852.1};
GN ORFNames=DI272_00800 {ECO:0000313|EMBL:PWI12852.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI12852.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI12852.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI12852.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-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}.
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:PWI12852.1}.
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DR EMBL; QFRX01000001; PWI12852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZKM3; -.
DR OrthoDB; 5526311at2; -.
DR Proteomes; UP000245455; 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 CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
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; IPR000933; Glyco_hydro_29.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
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; PF14200; RicinB_lectin_2; 2.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000245455};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..660
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039537935"
FT DOMAIN 523..658
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 660 AA; 71415 MW; BE09F7FFAEA468FC CRC64;
MTSSSLPLSR RRLLAAVGAS AAVGLLRFAP EAAATDGPGS YTASWASVDQ HPPAPAWFQD
AKFGIYYHWG AFSVPAFGNE WYPRNMYVGG SAENNHHKAT YGDPSVWPYH NFIDGARDKA
GNFVQFAPKP VSQGGKWDPD AWARLFKAAG ARFAGPVAEH HDGFSMWNSR SNPWNSVQHG
PKLDLVGLHA QAIRGQGLKF MASLHHAYHF NGFYDHVPNQ SDPTLRILYG QQGSAAENKL
WYDKLVEVID GYQPDLVWQD FDLHLVQESY RLQFLAHYYN QAVAWNKDVV ATYKDGLNNK
GEVFDFERGG PADLLTPYWL TDDSISSSSW CYTVGIGYYS TQAMLHSLID RVSKGGNMLL
NIAPMADGTI PSAQQSILLA MGDWLGRFGE AVYATRSWTS YGEGPTKMGG GSFSGPVAGK
PQDVRFTRSR DNKVLYATAL GWQGGTMTVT TLNSNRINLS SLTGAQLLGN TAGTYIDLPA
PIQDAGGLHL TMPSSNAPFS ALAYTVKLTF SGEIPVLGAP GGSTTWVRIA NVTSGLVLDS
GGNVAAGSNL KQWNYDGSTN LQWQLIDLGN GYYRIMNRTN GMAADSWGNA ANGAPARQEA
WNGGNNQQWS LNSLGDNRFQ IVNRGTGTAL DGSGSTTAGS TTVLWTPNSS TNNAWTITAV
//
