ID   CRR1_ASHGO              Reviewed;         450 AA.
AC   Q75A41;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Probable glycosidase CRR1;
DE            EC=3.2.-.-;
DE   AltName: Full=CRH-related protein 1;
DE   Flags: Precursor;
GN   Name=CRR1; OrderedLocusNames=ADR078C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Spore specific glycosidase involved in spore wall assembly
CC       during sporulation. May be involved in copper import (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Spore wall. Note=Spore wall envelope.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE016817; AAS51998.1; -; Genomic_DNA.
DR   RefSeq; NP_984174.1; NM_209527.1.
DR   AlphaFoldDB; Q75A41; -.
DR   SMR; Q75A41; -.
DR   STRING; 33169.AAS51998; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   EnsemblFungi; AAS51998; AAS51998; AGOS_ADR078C.
DR   GeneID; 4620323; -.
DR   KEGG; ago:AGOS_ADR078C; -.
DR   eggNOG; ENOG502QVQI; Eukaryota.
DR   HOGENOM; CLU_039093_0_0_1; -.
DR   InParanoid; Q75A41; -.
DR   OMA; WPCCSPY; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005619; C:ascospore wall; IEA:EnsemblFungi.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006037; P:cell wall chitin metabolic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Reference proteome; Signal; Sporulation.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..450
FT                   /note="Probable glycosidase CRR1"
FT                   /id="PRO_0000228140"
FT   DOMAIN          67..347
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          428..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        225
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        229
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50921 MW;  D678B18378F129B6 CRC64;
     MSKRIIQLIL LSAFARANYV EPFKSNPYIA CSEASHCPKE WPCCSQYGQC GSGPLCISGC
     NPKFSHSPES CVPVPALLPQ LEIVASDDKG VYLEMSGQPA LVTKFQRKSS AQLLEVHHEE
     QQYGVSALEQ DLNSRGLIHF PDYMITSKPK VAREMLEQYD FIHSGFISVD GKSESLILGM
     PKKTTGSLIS SSKVFLYGRA AVTMKTSRGP GVITAIVFMS STQDEIDYEF VGSELHTVQT
     NYYYQGELNH SRMRRHSLPS NSHEEYHIYE VDWDAERIHW MVDGEIVRTL YKRDTWDPVH
     KIYKYPQTPM MLQISLWPAG TPDAPQGTIE WAGGLIDWEN APDIKAHGQL AAQIQRVAIT
     PYNNDFCPEI HESMGQWGAQ NSEEEPFRVA YGYESNNGRF DPKKLKWYTD ARLHLSSWHA
     TGIKPTAAQR QQHHRRSLPH VEAPPITNTM