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Database: UniProt
Entry: W3X132_PESFW
LinkDB: W3X132_PESFW
Original site: W3X132_PESFW 
ID   W3X132_PESFW            Unreviewed;       823 AA.
AC   W3X132;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=PFICI_07362 {ECO:0000313|EMBL:ETS79833.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS79833.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001445};
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DR   EMBL; KI912113; ETS79833.1; -; Genomic_DNA.
DR   RefSeq; XP_007834134.1; XM_007835943.1.
DR   AlphaFoldDB; W3X132; -.
DR   GeneID; 19272375; -.
DR   KEGG; pfy:PFICI_07362; -.
DR   eggNOG; ENOG502QVGI; Eukaryota.
DR   HOGENOM; CLU_007933_1_0_1; -.
DR   InParanoid; W3X132; -.
DR   OMA; WEISHEG; -.
DR   OrthoDB; 67137at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   PANTHER; PTHR34987:SF4; BAC_RHAMNOSID_C DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR34987; C, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02880)-RELATED; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF17390; Bac_rhamnosid_C; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT   DOMAIN          385..599
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          743..813
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   823 AA;  88865 MW;  EA70136985E08D5E CRC64;
     MFSIVAALQS SMPAFSSVRL ALSSEPSIAS LNFSTFELSS SVPVATIDYG IEGAGYPFLD
     VESVTGKVQV EIKYSEQLAG LYENFSDGPL VYASGLTNTY RVETLEISLP GRIEALQLQG
     GQRWQSIRLL TDESITFRDV GFIPSVLDID RSKAPGSFRS SNEHLDEIWR LGARAAALSC
     LEEGSQKDLW EISHEGVFVR GMKPALTSQG AFLENYTLRF KANIQKGGFA WSIAQPLASP
     AKGIQLYLTG STRNDSAFVS VNSTLLPPNS IVLGYGFSIV NITTLASYYL DSFNLPFEVE
     EDTWNDVKTI LTKTGYLAVS VNGQQVFNKS LDDYYVGGQT IPTRGSFGFG GWQDQASLFK
     DVEVHDTTNG SLLYENDLTD DSVLSEYGVQ SNTASVCLDG PKRDRLVWLG DFYHTVRVLG
     ASTGQFRAAK GTLQWFLDWQ IKEGLIPYAS PIGYSPQTAR DAYAYGGGGQ LKGYPVWAII
     LPDYQILGLL SFCEYVRISG DVDFANATWP QWQLLASWIL NQTSTATGLP TLVGGFLGPG
     NGSSAISCAT VQAFKSLANV ADAVLDNQSA KTYQTAAETM ARNINDRLWN AALGVYAVSE
     SNTVDYSIAG TAFCILGGVA NATQASSSIA ALDRLKVDFG YLDSTLVNAS NPDTTISPNT
     NGFLLEAFAS QNASGSTQSL LDSLWMRMIT NNKTYTGASW EYISMSGDPG LGLFTSLGHP
     WGGAPTYVLP EYVTGVRTAV GADGFGYKRW TFSPQLGLDM GLEEASSETM TVSGEPIRVS
     WKLSGRTLSV VVDAPNGTTG TFQINGTTRS LVGSFTHKFD VEL
//
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