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Database: UniProt
Entry: A0A010QGI3_9PEZI
LinkDB: A0A010QGI3_9PEZI
Original site: A0A010QGI3_9PEZI 
ID   A0A010QGI3_9PEZI        Unreviewed;      1827 AA.
AC   A0A010QGI3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=CFIO01_06379 {ECO:0000313|EMBL:EXF79057.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF79057.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF79057.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF79057.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF79057.1}.
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DR   EMBL; JARH01000575; EXF79057.1; -; Genomic_DNA.
DR   RefSeq; XP_007597258.1; XM_007597196.1.
DR   KEGG; cfj:CFIO01_06379; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_237441_0_0_1; -.
DR   OrthoDB; 5488371at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 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; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR010610; EryCIII-like_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   InterPro; IPR002213; UDP_glucos_trans.
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   Pfam; PF06722; EryCIII-like_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXF79057.1}.
FT   DOMAIN          99..260
FT                   /note="Glycosyltransferase family 28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          420..525
FT                   /note="Erythromycin biosynthesis protein CIII-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06722"
FT   DOMAIN          1077..1231
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          1259..1361
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          1367..1718
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          1722..1800
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
FT   REGION          645..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1827 AA;  202216 MW;  FFCB87760C842488 CRC64;
     MAALTRVKSK GLGHIALGDG GRSETATSGN VGNDGRVRVR FHENPQKLAH WLRDFEGAFR
     PHSGDYDEEF EQARLRRRSS VILQNLQQHP PSKSPRLNIA IHIVGSRGDV QPFIPIAQLL
     MKEPYGHRVR ICTHPVFKDF VESNGVEFFS IGGDPEALMA YMVKNPGLLP SRESVKAGDI
     KQRRKEMAEI INGAWRSCIE AGDGMGERTT AATVLNADDL FVADAIIANP PSMAHIHCAE
     KLGIPLHMVF TMPWCPTQAF HHPLASMSYG EADTSAANYL SFIMMELLTW QGLGDLINKF
     RTQTLGLDHI SPLWGCQLLP RLRVPYTFLW SESLIPKPAD WDSHINITSF SFLPLADKYT
     PPADLTAFLE AGPPPIYIGF GSIVVDDPKA LTQLIFKAVG QAGVRAIVSK GWGGVGGGDD
     VPDNIYLIGN CPHDWLFKRV SAVVHHGGAG TSAAGIACGR PTVVVPFFGD QPFWGQMIAR
     AGAGPAPVPF KEMTAETLAA SITFALKPEV QVAVQQMAER IAEEDGAGDT ARDIQERLAL
     DTMRCDICPE RLANWRHRKT GAHLSNFAVG CLVDKGYMKP HDFKLLKHKH WYVDEGAEHP
     LIGLVAAVSG FFTNIGVATS DYSHRLKHPP QAAQNRMHAV DLEAQRPTHE KQPEEESNTT
     REPSAEPSEG PDVQPGPEGK AEDGEDGHLK RVAKAHSMTP KQMNAIAMKM ATKSLQCADP
     AVEIAMMDAN DVDERGRRKS SVATLVKKRN RPTEVARATG RYGIELVKAG LKAPVAVCYN
     VANGFHNYPS YGFIGHEVRR RDQITGLGSG LRTSGKEFVL GTWEAFSGVV VKPYEGAKRE
     GVKGFGKGIY QAGRGFTFNL FAAIFGLPGY TLKGIEKEFS KHRLTALKAE VLLIRLRQGI
     DDFRRSTEAE RNELYDPSLR RRYTAMAGLR VVDVRVDHYR QPYTLGIHVE RPQISWRFSD
     ASSRFNLGGW EVKIQKPDGS HSVISAPSNS PGISSPSAEW PEDIVIQSRQ TYSIEVRAQD
     ENGSDFSSWS EPFSFETGLL VRSDWTGNLI SAPWAEDGKS GPQPEDLFRR VFEAKSKVRS
     ARLYATAQGV YEAEINGRRV GDYFLAPGWT AYDGRLQYQT YDVTEHIAPS ASNCIGMRLA
     EGWFNGRIGF EGGKRSIWGT RTAALAQLEI TYEDGSIDTV VTDDSWTTTR GPIKLAEIYD
     GEKYDATAEI PGWSSSDSPA GEWETVQVLT RLPDTTDLIC GYGEPVKRLE YVKPLELITT
     PSGKSILDFG QNLVGFIRIN NVKGQRGNKI TLLHAEVLEK EELGTRPLRD CKAEDVYTLK
     GGDSGETWEP RFSFHGFRYV QVEGWPSTAL DLKEAIEACV CHTDMEEVGN FSCSDDDLNK
     LYSNVRWSMR GNFLSVPTDC PQRDERLGWT GDLALFAPTA TFIYNCFGIL KNWLADVAHD
     QKVLDGVPPM VSPNVLIGQK NWSKIGANAI WHDVVILAPW ALYEESADLG ILRDQYQSMK
     AWIDVIPRNK TGSTHLWDFG LFQLGDWLDP NAPPDEPMKA VTDPPLVANA FLVRSLDLIT
     KIAALLSQAE DAERYQREAA AARREFQDEY VSSNGRLTSD SQTAYALAIC FDLISEKQAV
     RAGSRLAEVV RRNGFRIGTG FAGTPYICEA LTRTGHSDVA YAMLLNRKCP SWLYPVTMGA
     TTVWERWDSM LPDGTINPGD MTSFNHYAFG AVAKFLVERL AGLQRLEPGW KRSRAEPILG
     AEFTNASAEH VTPYGKVACA WKLADEGGSR LRLKVDVVVP PLTEMEVVLP TKGGRRVEIV
     GSGEWSFETE YERTYEWPVK ELSLFPQ
//
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