ID A0A178B6C4_9PLEO Unreviewed; 530 AA.
AC A0A178B6C4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=Rhamnogalacturonate lyase {ECO:0000256|PIRNR:PIRNR011794};
DE EC=4.2.2.23 {ECO:0000256|PIRNR:PIRNR011794};
GN ORFNames=IQ06DRAFT_212390 {ECO:0000313|EMBL:OAL05785.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL05785.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL05785.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL05785.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23; Evidence={ECO:0000256|ARBA:ARBA00001324,
CC ECO:0000256|PIRNR:PIRNR011794};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR011794}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418, ECO:0000256|PIRNR:PIRNR011794}.
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DR EMBL; KV441706; OAL05785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B6C4; -.
DR STRING; 765868.A0A178B6C4; -.
DR InParanoid; A0A178B6C4; -.
DR OrthoDB; 66666at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10317; RGL4_C; 1.
DR CDD; cd10316; RGL4_M; 1.
DR CDD; cd10320; RGL4_N; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR InterPro; IPR016590; Rhamnogalacturonase_B.
DR InterPro; IPR015364; RhgB_N.
DR PANTHER; PTHR36574; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR PANTHER; PTHR36574:SF1; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF09284; RhgB_N; 1.
DR PIRSF; PIRSF011794; Rhamnogalacturonase_B; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR011794};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR011794};
KW Signal {ECO:0000256|PIRNR:PIRNR011794}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT CHAIN 19..530
FT /note="Rhamnogalacturonate lyase"
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT /id="PRO_5010009598"
FT DOMAIN 20..275
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 281..354
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 366..528
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 530 AA; 56186 MW; 3A22921E833F142D CRC64;
MLSSALLAVA ALSSTALAAF GASQSEDTIT VDAGSSNALV FTVNAKSCDI NSIKYRGEEL
QYPSTGTHIG SGLGSATVKY ETISGQYVKV TCTTSTLTHY MVVRSGDSTI YLATHTTAEP
DIGELRFLAR LNNKVLPDQY PYDLVSTTGG SSSTVEGSDV FIVNGQTRSK FYSSERFIDD
TTVSEALSGA VHACMLMNSY SYEGSSGGPF FRDINTNNNG DYTSLTFYMN SGHVQTEKYR
MGLHGPYALA FTRSGVPEGG DKMDTTFFKD LGITGYVAPS ARGTVTGTAT GIGSSFQKVL
HWYNDAAQYW AYADSAGKFT SPAMKPGTYT QVLYQGEFKV KASSVTVSAG KATSANVAAD
VESKTTIWRI GDWDGQPKGF RNADKQLRMH PTDSRMSSWG PLTYTVGTSS LDSVPMAIVK
DNNPLTIKFT GTDTGAATLR VGTTLAFAGC RPSVVVNSYS PATPAAPTKI DSRGLTRGAY
RGFGEVYNYA IPAGKLVSGS NTITINCASG SSGSGFLAPN VILDAIELFK
//
