ID   RHGC_ASPFN              Reviewed;         447 AA.
AC   B8NGP8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable rhamnogalacturonase C;
DE            Short=RGase C;
DE            Short=RHG C;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=rhgC; ORFNames=AFLA_136750;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC       pectine lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-
CC       alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions
CC       of pectins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED50912.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; EQ963478; EED50912.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002379688.1; XM_002379647.1.
DR   AlphaFoldDB; B8NGP8; -.
DR   SMR; B8NGP8; -.
DR   EnsemblFungi; EED50912; EED50912; AFLA_136750.
DR   eggNOG; ENOG502QU5S; Eukaryota.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..447
FT                   /note="Probable rhamnogalacturonase C"
FT                   /id="PRO_0000394953"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        338..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        366..375
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   447 AA;  48195 MW;  CF58B6D65E06917B CRC64;
     MQVKLFYTLA LWAPILVSAQ LSGSVGPLVD FKTKAKNKTC DITDYGAVAD GKTDVGPAIL
     DAWGNCSTGG LIYVPPGTYS LATDLELKHG ESTAFQLDGV LARGHEGSYQ LILVRNCHDC
     EFFSGNSQGA VQGYGYEYLQ DGNYGERLFR FQDVSDFSVH GFAAIDSPAY YLVFDTVSNG
     EIYNLLVRGI ADLGMTDAFD IWGQNVWIHD IEVTNGDECV TVKSPASDFL IENIYCNLSG
     GTAIGSLGTG TNISNIHYRN LYMNQADACY LKTHNGDGIV KNIVWENVIV HGGPYPLAVN
     EAWGKDVGST GVQVQNLTFR NWYGENTANS RPAIRIECDE DVPCYDITLD NVNLWTEDGD
     YVEWSCANAY GSGACLQEAK DTGDLATYTT AVTVTATPSY SATHMPGDFT TNPPSTAPFT
     IPPMPTSFYP GATPISTLLS LSGAGGL