ID A0A1V6RU61_9EURO Unreviewed; 795 AA.
AC A0A1V6RU61;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=PENVUL_c025G05822 {ECO:0000313|EMBL:OQE05307.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE05307.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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};
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:OQE05307.1}.
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DR EMBL; MDYP01000025; OQE05307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RU61; -.
DR STRING; 29845.A0A1V6RU61; -.
DR OrthoDB; 1751175at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR34987:SF2; B, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G05040)-RELATED; 1.
DR PANTHER; PTHR34987; C, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02880)-RELATED; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT DOMAIN 375..605
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
SQ SEQUENCE 795 AA; 89657 MW; 70FF0B65839A7FF5 CRC64;
MASAEEQKTI NELQANWIWV PNWTDSSNTN TAGQIVHFTR NVNLLSRATK SVLHFSADTR
YKLYVNGKHI AVGPTRSSPL IWYYDTLDIA PYLKEGHNEI RFVVIRYFAA LRSAMPFVRT
ALPGLTVIGN IETGDEVVNL ASSENWMASV DESIQFPMGL ADDVFLHISE RIAPATPGAA
VTPFAYKMRT LNGDIPPWNL RPRSIPMPES TLAIVKTIRA CNSLVDISDW TAFFANNNSL
ALPASSTHTL EVQADVHSTA FVRWAFKATK KASYIRLKVT HSEGYELEPR SYPFFRSKGD
RMDASVGHIV GPYDEVKLDI PGTETAIYEP FWFRTFRLMR IEITVGPEPI ELVSFDATQV
NYPMAVKASW KEPGDAHSER IWDVSIRTMR NCMFDGYSDC PFYEQLQYSG DSRSVGLFHY
LLSGDDRLMR QAITNFAASV TPQGLTQSRF PSHVPQIIAG FSLYWILQVC DHHLYFGDTR
FARGFIPRID GILDFFDAHI DELGLVSGLP EVVWQYVDWV TTWGATDNHP DKGVPTSGRK
SNRHTYFSML YAWVLQKVAG LVRDVGRPGH AAEYEARAES LLGAIQAHCY DGKFFTDSTA
DVADELSYSQ HCQVFAVICG AARAEDSARI LAESFTNDRF SKCSYMMRFY AFRALALAGE
DLYESFWERM WVPWRGMLAN NLSTWEEDDV RQRSDCHAWG SVPIYEYCTE LAGVQPVAAG
SSKISFRPRL RLTGALEAKV ALGKDNLATI SWKLSGNENI VELRLEKAVE VVSQLPRGKE
EEHGVVDYLR FAFKD
//
