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
//