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Database: UniProt
Entry: A0A0S8JHI8_9BACE
LinkDB: A0A0S8JHI8_9BACE
Original site: A0A0S8JHI8_9BACE 
ID   A0A0S8JHI8_9BACE        Unreviewed;       922 AA.
AC   A0A0S8JHI8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=AMS26_23425 {ECO:0000313|EMBL:KPL09008.1};
OS   Bacteroides sp. SM23_62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL09008.1, ECO:0000313|Proteomes:UP000050819};
RN   [1] {ECO:0000313|EMBL:KPL09008.1, ECO:0000313|Proteomes:UP000050819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62 {ECO:0000313|EMBL:KPL09008.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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};
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:KPL09008.1}.
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DR   EMBL; LJUP01000369; KPL09008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8JHI8; -.
DR   PATRIC; fig|1703352.3.peg.3793; -.
DR   Proteomes; UP000050819; 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; 2.60.120.260; 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; 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; 2.
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..922
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006648981"
FT   DOMAIN          192..230
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          247..374
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          384..472
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          477..809
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          817..888
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
FT   REGION          144..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  104203 MW;  B3510F164A92EB24 CRC64;
     MIFKNTLTIL FSLLFLNAVA ELSPTDLRCE YLEDPLAVDI RQPRLSWINL AEKGARGHYQ
     VAWQIRVATA EEKLPDADLW NSGKVESDPS TQVRYTGKPL ISRQDCWWQV RVWDRDGQVS
     AWSKPARWSM GLLDPGDWKA GWIGPPWQGE EALPRPSAPK RDEPPDKEPS LIPGKIPPPA
     PMLRKEFTVT GEIASARAYV TGLGFLEFYV NGQKVSQDVL VPNVTLYGER EDLGPIGAMI
     RDHFREYRVL YLAYEVNDLL TQGENVIGTM LGNGFYNPAS YWCQGYGSPR FLGQLHLVYT
     DGTEQVIVSD ESWTAAKSPI LMDMVYDGEH YDARLEQTGW CTPDFDDSGW ENAVSRKAPE
     GKLKAHMSPV DRVMEKLPPR TIEKLGEGRY RVDFGEEISG WVRLQDVTGE AGHRIDIKYL
     CESPVGDNSY TLKGHGPESY AARFTWFVFR EVEISNWPGE MRPEQLMAEA VYSNVETTGH
     FECSNLLFNR IHKIWNRSQK DNMHGGIASD CPHRERSPYT GDGQVACVTV MHNFDSRAFY
     TKWIRDIFGA QNPENGYVPN GAPWQPGCGG GVAWGAAMVI MPWEFYIHYG DVDMLKENYE
     GMKGYVKYML TWTGEDGIMH SQAPERENPN RWMNLGDWCA PGELPPPEMV HTFYLWRCAD
     LTAKTARVLD KETEASAYEQ LAGKTKKAFQ RRFYDQVNGT YGPAGGNIFA LKMGVPVEQY
     ERVINSLRSD ILKNDGHLDT GIFGTQFFFE VLSEHGLHEL AYGAMNKMSE PGYGWWIEKG
     ATTTWERWDG QGSRNHPMFG GGITWLYRHL AGMNPDPQSP GYRHIIFKPQ PAAELTSASY
     SNKTPYGEAS IGWKKKGRKF SMNIRVPAGC SASVYVPAIS ADKVKESNQK PGHWPEVIFQ
     QESDGYAVYQ VGSGNYDFSS RF
//
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