ID A0A177C5P7_9PLEO Unreviewed; 573 AA.
AC A0A177C5P7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=CC84DRAFT_1152216 {ECO:0000313|EMBL:OAG02047.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG02047.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG02047.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG02047.1,
RC ECO:0000313|Proteomes:UP000077069};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418}.
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DR EMBL; KV441556; OAG02047.1; -; Genomic_DNA.
DR RefSeq; XP_018032412.1; XM_018176792.1.
DR AlphaFoldDB; A0A177C5P7; -.
DR GeneID; 28760278; -.
DR InParanoid; A0A177C5P7; -.
DR OrthoDB; 2715696at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 PANTHER; PTHR32018:SF1; RHAMNOGALACTURONAN ENDOLYASE; 1.
DR PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OAG02047.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..573
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008057748"
FT DOMAIN 314..395
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 410..570
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 573 AA; 63710 MW; C688E352F377D982 CRC64;
MGLFQLAGVA ALALCASAAP AEPRAPKPKS FLKDLGNSTW VIGNGIWNMT QGRQYGVKLW
YKGKDRVGPT ATGHYVSYNG AASDLNWTSA AIADSGKDWI NIKFTAKEGD FHWVIHDDLA
GAYQYFVNHA LPTLGEFRTL WRLDNVSFPN GHTNVKDGQL PPLSEYAAAT NVQDETWQKA
DGTFLTKYDW SAFVRDQTYY GVYGDEVGSW YINPGKDYYN GDHLKQELMV HRESKTGDAV
QLNMIHGTHY LARSSDNFTD GKTWGPWLWY LNDGNKADAD NRWKKEDKSW PYEWFKDAAY
QSRGSVSGKL VLSDGRPASG AAVFLGDSNS ALSAADQGKD YYYTAYADKQ GRFTIENVRT
GTYGLYAWGN GGNIADVKTS FVQNDVVVSK RKKTDLKSLK WTVTDKSKSI FQIGDFDRTS
RGFALSGPTP FEHGRIAKTP GNLTYTVGKS HSSDWYFGQS NLGVWSINFN LKSIPESATG
AKLYTSLAGF SSGTKSNILV NNEKIGNISS NAVLLVSSQD TYRGATQAGE WRNLQWDVKK
ELLKVGENKL DIAVTESTKW RGWLWDSVAL EWV
//
