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Database: UniProt
Entry: A0A1V9YSN8_9STRA
LinkDB: A0A1V9YSN8_9STRA
Original site: A0A1V9YSN8_9STRA 
ID   A0A1V9YSN8_9STRA        Unreviewed;       560 AA.
AC   A0A1V9YSN8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cell 5A endo-1,4-betaglucanase {ECO:0000313|EMBL:OQR88775.1};
GN   ORFNames=ACHHYP_06639 {ECO:0000313|EMBL:OQR88775.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR88775.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR88775.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR88775.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:OQR88775.1}.
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DR   EMBL; JNBR01001096; OQR88775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9YSN8; -.
DR   STRING; 1202772.A0A1V9YSN8; -.
DR   OrthoDB; 47190at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        80..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..509
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  61166 MW;  D8FB2DB4D70ED397 CRC64;
     MATSPRGPSP RLRIDVDEDA GGRRGSSSPS TYKRYESGAV DDDDGTFEDS EATEGSNVQQ
     LDGYKQTSRR GRLWAWRRRI LVILVVAGCI AIVVIFILKL TVKNSSSNTS DGSSESSKAV
     PRGIIRDGLP DGPVDLAVGT NPTAYPPQRC KLPNYVSQDG KIYITGSNGF KQPIGIKGIN
     WSGMETGNAI PYGLWTNTQN GTTVYEIASF LARNNFNSVR LPLCIESILK NRVPNTALLN
     TYSNRAINAK SYLTMISSLV KALAYRGISI LLDLHVLSVS DPGPKWTSAT IGQASYLAAV
     DALTKTFCND DHWNIIGLDL KNAPSQMTWG DKTDTDWAVA AALIGNRMLG GCPNWLAFVE
     GVNAQHTMTL PNGVFASYYD WWGAGLQEVA NYPLALETAN KIVYAPHYYS PSVYPQKYLL
     ANGTRVGDLI GAYTELDNAT LKEVVFATAD NMFGYLAKAE QAAIVLGEFG GLYTQDKHAN
     YTVRRVIESC IAMVQQPGFA GGYVWSLNPE SGYNYNPSDH VGLWQEGLIG PDWVSVNKPY
     LNALRELDNV PHLARWPCLS
//
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