ID A0A2H3IFQ6_9EURO Unreviewed; 638 AA.
AC A0A2H3IFQ6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=PENO1_105710 {ECO:0000313|EMBL:PCG89254.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG89254.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG89254.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG89254.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCG89254.1}.
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DR EMBL; NPFK01000635; PCG89254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IFQ6; -.
DR STRING; 290292.A0A2H3IFQ6; -.
DR OrthoDB; 67137at2759; -.
DR Proteomes; UP000218381; 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; 2.60.420.10; 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 PANTHER; PTHR34987:SF4; ALPHA-L-RHAMNOSIDASE C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR34987; C, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02880)-RELATED; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..638
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013796548"
FT DOMAIN 219..413
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 541..614
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 638 AA; 68357 MW; 8D03C81A970947CE CRC64;
MYSPFVCCLG ASLLLAHQYQ SFGSVSNPQN LCDSTDSTTT FDGNASVTYD FHNDIAGIVT
LEVESALSVG AQLGITFAES SLWISNRSSD ATADSGLDAT LWFNVDTAGG KYTSVAAQGR
GGFRYLTLVS NSTASITLKS VSVNYTAAPT QDLQGYTGFF HCDDELINQI WYAGAYTVQL
ATIDPKYGNA LALLVTWPPA APSMYDDWYS NYTITNGTTA LTDGGKRDRL VWAGDLSISL
ETAIVSTYDL HSVRNSLGAL FALQTADGRF PYASRPFPDQ ESFTYHLHTL INAANYYRYS
ADHAWLVSYW TQLEKGISWA LGSVDDTSLA NVSPSASSDW LRSGMGGHNI EANAMLYFVL
QQGIHLAAVV QDSASLAHWN STAEHLKVAA NALLWDETSG LYRDNETATL YPQDGNSWAV
KANLTQSGSQ RARISSGLRS RWGPFGAPAP EAGSSTISPF IGGFELQAHY LAGEGSTALD
LIRRQWGFML KDPRMTGSSF IEGFSTDGSL HYAPYINDAR VSHAHGWSTG PTSALIFYAA
GIQVIEGGGA TWIIAPQPGN LTSVDAGYTT LLGSFSVTFR CSERGGVYQS FAFTTPKKTS
GTVRIPGATG VLVSSSGCRV PLVNGTASGL EGGTWILR
//
