ID A0A150UUJ4_9PEZI Unreviewed; 690 AA.
AC A0A150UUJ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=M433DRAFT_75159 {ECO:0000313|EMBL:KYG41785.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG41785.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG41785.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG41785.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG41785.1}.
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DR EMBL; JPDO01000589; KYG41785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UUJ4; -.
DR STRING; 766039.A0A150UUJ4; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF5; ALPHA-RHAMNOSIDASE; 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, ECO:0000313|EMBL:KYG41785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..690
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571272"
FT DOMAIN 248..474
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 594..649
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 690 AA; 74903 MW; 8DA348647B1890A4 CRC64;
MAKLYHALLV ASALLSLSIA ETCWQGVPCT GPTEAAFPGE WESNIFAPSS RTVSPSQVID
LGTAQVLSSY PGASSIKGNA SALVFDFGKE VGGIATIEYT TSGGPGQLGL AFTEAKNWIG
LASDSSNGQF SRGYGDQACD DGAIYDYFTT DGKHTYTMPL MRLRGGFRYM TLFLLTNNTA
GSINIDSVSL AISFSPTWSN LHAYQGYFHS NDDLLNKIWY SGAYTLQTDL VATNEGRQFP
FLTSEWANNA TLANGTIVIV DGAKRDREIW PGDMGIAVPS SFYSLGPDLE AVKNALQAMY
DYQNSDGSFP EAGPPLLQQD SDTYHCWTMI GTYNYVFYTN DTAFLNENFE GYVRAMDYIY
DLVLEPLGLL NVTGTRDWGR ESPAGYCSEA NMILYRTLTT GAELASWAGY DALASEYSSR
ASTLQKNIMT YLYDYTYGAF NNNVTSEMHP QDANSMSLAF GVVPANSSEG KTISERLTDN
WTPIGPDCPE LPNNVSPFIS GFEVQGHFTV GNTQLGLDLI RTSWGWYLNN PNGSQSTVIE
GYLTNGSFGY RNYRGYNWDS SYPSHSHGWS SGPTSALTNF VLGLSITGRV GSTWKFAPQF
GDLTSVQGGF TTSLGKYQAS WNIIDGGRKY TAEVTAPEGT VGEVILPPLP GGGECSWSWN
GQNRGTFGDN AQIRMSGITG GKHNVVVTNT
//