ID   G1WY48_ARTOA            Unreviewed;       978 AA.
AC   G1WY48;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=AOL_s00004g208 {ECO:0000313|EMBL:EGX54175.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX54175.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX54175.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX54175.1}.
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DR   EMBL; ADOT01000005; EGX54175.1; -; Genomic_DNA.
DR   RefSeq; XP_011117160.1; XM_011118858.1.
DR   AlphaFoldDB; G1WY48; -.
DR   STRING; 756982.G1WY48; -.
DR   GeneID; 22888059; -.
DR   eggNOG; ENOG502QXBB; Eukaryota.
DR   HOGENOM; CLU_002926_0_0_1; -.
DR   InParanoid; G1WY48; -.
DR   OMA; EFRIRAY; -.
DR   OrthoDB; 5488371at2759; -.
DR   Proteomes; UP000008784; 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; 2.60.420.10; 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   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   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:UP000008784}.
FT   DOMAIN          201..352
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          435..467
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          483..867
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          888..957
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   978 AA;  109818 MW;  E272457F64CB641B CRC64;
     MAPSIEITNL RLPHTSNLLG IDDPTPIISW SYSIPSAQTA PSWQQITYIL SLRSWSLASG
     SDSAKTYVVV GPQGYCSGNI LWPKVFPRVE SSHVYELSVR AIFTGGKTNA HGEFGSPGGD
     KLAPEGESAE QLAAKFTVGL SDASIASGVL KFEGGIVGGL NGWYKKAPSI TPITTPWSAQ
     GWEKPEPVPA YRNTYTLKSK PQFARVYATG FGVYKISING KAVSAESTMN PGWTEYAVRM
     TYQTYDITEH LQAGDNVVTV WVADGWYRGR LGLPHKRWSA RRGIYGKETG FMALFETFGS
     ENQSFWTGSS SETGWKCIQR SPILETEIYD GEHHDARISI ETAGEDEWKD VKQIPEVFVS
     ELRRPVINEK TVNWRILKWD IESWSTETAT KALQAQTAPL IRHTQTFPLK ETIRTPKGKI
     IWDFAQNITG KIKIKGGNGV EEWEPEFTFH GFRYVQVDGL PEGVEIEAVA KVYGSDCDKG
     LLKFNTTHQD LNRFVENIQW STRGNFYSVP TDCPQRDERL GWSGDINLFG PTAVYIFDCY
     TFLKQWLQGL ADGLYIGGFN RPPIVSPNAF ELPGSHRPMA IWEDCLVALP WNLYKQYRDP
     SLLEALYPSI RQYYTKGIPR NEDGLWVDSF QYGDWLDPTT PPERPELAQT NQIFIADTWL
     CNISQIILNI ATVLGKMEDI ELFKSSKEKV ISAWQKKYLV PIDASISESE EPQQLIRWEP
     NAEDPNPPNP VPDSQTAYSC ALTFGLLPES YIEPAIRRLH HLVKNKANFH ISTGLAGTPE
     IFYALCYPRN LPSTTSQEHL ESVSLAYKLL LKNYDTPSFL YPIKMGATSI WERWDCITKE
     GFANVVSMTS MNHYALGAPG KWIFENIGGI KLEHDDLPVS GVVNADAKEG WKFIFDPIPS
     VEFGVLSNQM EYESPKGRVE CKWSYSTQDK ELSVEVAVPA NCEGEIRIIG KTVQKVGAGK
     YSVKKKLDEV DWKTLEAF
//