ID   ASD1_NEUCR              Reviewed;         540 AA.
AC   P78710; Q7RVB7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Putative rhamnogalacturonase;
DE            EC=4.2.2.23;
DE   AltName: Full=Ascus development protein 1;
DE            Short=Asd-I;
DE   AltName: Full=Rhamnogalacturonan lyase;
DE            Short=RGase;
DE   Flags: Precursor;
GN   Name=asd-1; ORFNames=NCU05598;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9178004; DOI=10.1093/genetics/146.2.531;
RA   Nelson M.A., Merino S.T., Metzenberg R.L.;
RT   "A putative rhamnogalacturonase required for sexual development of
RT   Neurospora crassa.";
RL   Genetics 146:531-540(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Could be a pectinolytic enzyme that hydrolyzes the alpha-L-
CC       rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage
CC       by beta-elimination, thereby generating oligosaccharides terminating at
CC       the non-reducing end with a hex-4-enopyranosyluronic acid residue.
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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed preferentially during the sexual cycle
CC       and essential for normal sexual development.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC       {ECO:0000305}.
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DR   EMBL; U70861; AAB39649.1; -; Genomic_DNA.
DR   EMBL; CM002241; EAA31324.3; -; Genomic_DNA.
DR   RefSeq; XP_960560.3; XM_955467.3.
DR   AlphaFoldDB; P78710; -.
DR   SMR; P78710; -.
DR   STRING; 5141.EFNCRP00000005597; -.
DR   CAZy; PL4; Polysaccharide Lyase Family 4.
DR   EnsemblFungi; EAA31324; EAA31324; NCU05598.
DR   GeneID; 3876675; -.
DR   KEGG; ncr:NCU05598; -.
DR   VEuPathDB; FungiDB:NCU05598; -.
DR   HOGENOM; CLU_037882_1_1_1; -.
DR   InParanoid; P78710; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IBA:GO_Central.
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:0045490; P:pectin catabolic process; IBA:GO_Central.
DR   CDD; cd10316; RGL4_M; 1.
DR   Gene3D; 2.70.98.10; -; 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; PTHR36574; 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; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..540
FT                   /note="Putative rhamnogalacturonase"
FT                   /id="PRO_0000024913"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..203
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  58011 MW;  B4638AA1B93A28A0 CRC64;
     MGFLTLFHMA FLAVSLFVSG ALAAFGYTTS GNNFVIDAGS ANPLIFSVSK SSCDINSIRY
     RGTELQYSKQ GSHIGSGLGK ATVSVSQING SKSKFIKVTC VTSTLTQYMI VKEADSTIYM
     ATYITAEPAI GELRFIARLL SDKLPYEYPY GEVSTTKGSS STVEGSDVFV VNGQTRSKFY
     SSTRFIDEDS HCVYGGSDLT HVCIITPQQE SSSGGPFFRD IDSNNAGEST NLYNYMNSGH
     VQTEDRRMGL HGPYLMTFSR SGIPKLKTVD ISWFGELGVT GYVPDSQRGT VIGRATGIPS
     GFEGVVHWYN AAAQYWVRTA PNGDFTSPKM KPGTYTMVLY QTEFKVATST VTVSAGKTTT
     ASIASTFNTS HTTLFKIGEY DGQPTGFRNA DKFLRMHPSD SRMSSWGPLT YTVGSSSLND
     FPMAVFKSVN NPVTIKFNLG SAPSQATTLR IATTLSFAGA RPQVVVNGWS APAPAAPAKI
     DSRGVTRGAY RGYGEVYDVA VPAGKLISGT NTITISALSG SSGATFLSPN FIFDAVELFY