ID K2R1X2_MACPH Unreviewed; 904 AA.
AC K2R1X2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-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=MPH_06544 {ECO:0000313|EMBL:EKG16231.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG16231.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG16231.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG16231.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG16231.1}.
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DR EMBL; AHHD01000283; EKG16231.1; -; Genomic_DNA.
DR AlphaFoldDB; K2R1X2; -.
DR STRING; 1126212.K2R1X2; -.
DR VEuPathDB; FungiDB:MPH_06544; -.
DR eggNOG; ENOG502QXBB; Eukaryota.
DR HOGENOM; CLU_002926_0_0_1; -.
DR InParanoid; K2R1X2; -.
DR OrthoDB; 5488371at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
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; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR016007; Alpha_rhamnosid.
DR InterPro; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR InterPro; IPR013737; Bac_rhamnosid_N.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008902; Rhamnosid_concanavalin.
DR PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR33307:SF6; ALPHA-RHAMNOSIDASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF05592; Bac_rhamnosid; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR Pfam; PF08531; Bac_rhamnosid_N; 1.
DR PIRSF; PIRSF010631; A-rhamnsds; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 157..326
FT /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08531"
FT DOMAIN 336..439
FT /note="Alpha-L-rhamnosidase concanavalin-like"
FT /evidence="ECO:0000259|Pfam:PF05592"
FT DOMAIN 444..796
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 798..869
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 904 AA; 101719 MW; 72CD03255F9FC131 CRC64;
MSVQLIDVRF EHHPDGFGIG TATPRLSWRF SHGKTPAENW QQSGYTVEIS RQEGTQTHSF
HVESSESVLN PWPTKPLTSR ERVSVRVRAF GASERDGHQP DPAPTEWSHW HVVEAGLLQR
SDWTGNFIVS PLEEPKDKPH RPVLFRKSFD SPATKEARAW LYITSLGVYE AHINGRRVGD
LQMTPGWTSY RHRLQYQVFD VTELIQEGKN TIGVEVSEGW YAGRLTWGKG IRNFYGDKLA
TLVQLEIQTK DGVNQRIVSE ESWKTHQSDL IMSELYDGEV YDARQHLQGW TSPTFIEGSN
WKPSCILEFP NILLFAPDVA PVRVTQSVQS REIFRSRSGK TLVDFGQNLV GKVQIKLLHK
PEGHTVKIRH AEVLEHGELG TRPLRNARAE DTVIFSNQPL KDWAPRFTFH GFRYVQLEGW
SLDDDVPPST ENIAALVMHS DLVRTGQFSC SNDLVNRLHE NVVWSMRGNF LSIPTDCPQR
DERLGWTGDI QVFSPTASYL YQSAGFLSNW MQDVAAEQGD MDGIVPLVVP DVLGTTSWPS
VPQAVWDDVA ILVPWVLYQW SGDVEIVRRQ YSSMRVYLDT SIRRGDDGLW DPDLWQLGDW
LDPNAPPREP GLARTDGTLV ADAYLVYVTG IMAKISDAVE RPQETVLYQK QHDDLKAVFA
DKYIAPSGLL VGDSQTALAL ALAFSLHGES NPKQVRTAAD RLARLVRYSK FRVSTGFAGT
PLVLHALSST DHIQLAYRML LEEQCPSWLY PVTMGATTIW ERWDSMLPDG SINPGEMTSF
NHYALGSVAN WLHTVVGGIR PLEPGWKKFL VSPVPGGTLT NAEVKFESPY GLVEAKWKLD
DGHTRFVLRL NVPPNTTALL VLPGQKAEEG VWIGSGSHVR EASFKAPGNW PPKAMYTQFQ
EGLE
//
