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Database: UniProt
Entry: R1G2R9_9PSEU
LinkDB: R1G2R9_9PSEU
Original site: R1G2R9_9PSEU 
ID   R1G2R9_9PSEU            Unreviewed;      1041 AA.
AC   R1G2R9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=H480_24812 {ECO:0000313|EMBL:EOD65798.1};
OS   Amycolatopsis vancoresmycina DSM 44592.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD65798.1, ECO:0000313|Proteomes:UP000014139};
RN   [1] {ECO:0000313|EMBL:EOD65798.1, ECO:0000313|Proteomes:UP000014139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD65798.1,
RC   ECO:0000313|Proteomes:UP000014139};
RA   Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT   "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EOD65798.1}.
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DR   EMBL; AOUO01000371; EOD65798.1; -; Genomic_DNA.
DR   AlphaFoldDB; R1G2R9; -.
DR   PATRIC; fig|1292037.4.peg.4689; -.
DR   eggNOG; COG3408; Bacteria.
DR   eggNOG; COG4692; Bacteria.
DR   Proteomes; UP000014139; 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; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307:SF6; ALPHA-L-RHAMNOSIDASE; 1.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 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; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1041
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039022116"
FT   DOMAIN          340..506
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          517..617
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          622..954
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          958..1028
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
FT   REGION          762..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  110267 MW;  C1A264AE756B3184 CRC64;
     MVTALFALVA TSFAAAPGSA AGPEQALRAV DLRADNVVNP LAARSTPTLG WKLRSERPGE
     RQSAYRIRVA SSPRLLAEHR ADVWDSGRIA SADSVAVPYR GPATPAGQRN YWTVEVWGTR
     GAPAAEAGPA WWETGAGWAG AQWITPDTGD AYAWQDFALD VDFTVKAAAA AVVFRAAGPD
     DFLMWQVNAA ETPGKVLLRP HAKSHGSFSL LGETDLSPVI TPQTANARHH LRIEARGSTV
     VTAIDGTTVD SRPVDAVRAG TIGFRTSVSQ GTPEAAAYDN LTVHGLDGTQ LFSDDFSATP
     DSRFPGAAID GGQLEPQGDP LLLAQSPDAP LLRHEFVLGK PVASARAYVY GLGFYELHLN
     GGKVGDQVLS PGSTPYDRRA LYDSFDVTSQ VHKGHNAAAL WLGNGYGPRF SRYGFRWTGP
     KQGILALAVT FADGTRQTVT TDGSWRWSDG PVTANDLYAG ESYDARLERA GWDRPGFDDA
     AWHPVRTAAA PAAEFTGSAA PPIRVVRTLR PVAVQQPRPG VYVYDFGENF AGWARLRVAG
     PAGTTVRMRT AEELTGDGTL DTTTNRNAAS TDSFTLGAAR GVQVYEPRFT YHGFRYLELT
     GYPGTPDLGS VAGRVVHADV AATGHVETSD PLLNAIWANN RRAVLNNSMS LPTDNPVRDE
     RTPPGMDVQA YHDAAVLDFG MDGFYGKYLL DLPPGTALPS DDGNAQLPDM GGGSVDLAWS
     LYEQYGDLSR LAAAYPAMKS FVDTNAAALP GRIWPDDRGF GDWCPPDRSP NAGSGQGNPS
     AGACSSERSL VNTALSYRQA EAAGKAAQAL GKPGDAARFA DLATSISAAF NAHFLVGATY
     GDGRQTTSIL PLAFGIVPPD KVAAVGAKLV DTILNQDAGH LDTGIFGTRY LPEALAKAGR
     IDVALTVLRQ RTYPGFGYEI GRGATTPWEQ WTYESGMETH DHAMFAGLNA AFYTQFAGIT
     PASPGYASIA VAPQVPAGLG HVAASIDTVR GPVASEWTQT GCRFDLTVTV PANATATVTL
     PTGRRISIGS GTSKFTVRHC A
//
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