ID A0A0E9NS54_SAICN Unreviewed; 803 AA.
AC A0A0E9NS54;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycoside hydrolase family 5 domain-containing protein {ECO:0000259|Pfam:PF00150};
GN ORFNames=G7K_6556-t1 {ECO:0000313|EMBL:GAO52481.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO52481.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO52481.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO52481.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO52481.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO52481.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO52481.1}.
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DR EMBL; BACD03000071; GAO52481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NS54; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF34; GLUCAN 1,3-BETA-GLUCOSIDASE 3; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..803
FT /note="Glycoside hydrolase family 5 domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002430570"
FT DOMAIN 500..740
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 803 AA; 86235 MW; D47836B0FD3A04A9 CRC64;
MMRLFTLFLF LFTLASSITL AAAEDFQWSD NEVVSPAPRT SHLHHRSLTK RACSNLLIDN
FSSQSQLDNR KNDLGYKTSA DGTASISISS SSSSKLVITP SSSSSYFYSN TKCQSISGYS
AVQFSIAGPS GASVKVAVRY FDSATSCAPY GTSGYKTAYY TVTGLSSTAK RVTIPFSSLG
ITPAGSVISS VYLENFSVTG RSYSLWQLAL TCSSTSTSTG KTATCTSSSS GSYGLIDDFS
ATKSTNDLNY ATGDDSTCKS VTVLASSNKI QIVPASTSSS YWYSDVGCQA LTKFSGVQLS
VAGPSGASVQ VVVSYYPSSS SCSTGTGVQT ATYTVSGLSS TAKRISIPFS TLGIDSNSAV
LASIRLKNFS SKGTFYLWKL AFTCPSSSAS TTSVANLGGS TAAAVAQTTT SSAATSYTTY
TASNVNVLRD AQLDGSIRAV GVNLGGILQY ENWLSSGSPV QALLNELDDG SYYAEKGELV
IMRAFPNNRS AMVTAFQQHR AVLTEADFKL MAQYGINSVR VPINWGIMPV NSGGGDPDEW
ADFATGSLSV LDKIVNTWAP KYGITVLLSM HGHKGTHGVA EHASPGAANP VVYWDQYTEN
QQNSVNVAVY LAKRYLSSPA FLGIGMMNEP VNVAESVVRQ YFLDAYAAVR AVSNCLLVFA
PMLWQQYPSN GWQNFLSPND GYYNVREEWH PYFCFPPDWS SANNSAQILS YTANELQNDW
NGAPGVGKMA TEWSLATPNA MSSSDLTQFA KNQMKAYDYG GGFYFWTWKF WADNNNDNYI
NGWSLKSLLT HGVITKAMMQ AAW
//