ID F7VR39_SORMK Unreviewed; 326 AA.
AC F7VR39;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=WGS project CABT00000000 data, contig 2.4 {ECO:0000313|EMBL:CCC07972.1};
GN ORFNames=SMAC_01537 {ECO:0000313|EMBL:CCC07972.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC07972.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC07972.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC07972.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:CCC07972.1}.
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DR EMBL; CABT02000004; CCC07972.1; -; Genomic_DNA.
DR RefSeq; XP_003352702.1; XM_003352654.1.
DR AlphaFoldDB; F7VR39; -.
DR GeneID; 10810326; -.
DR KEGG; smp:SMAC_01537; -.
DR VEuPathDB; FungiDB:SMAC_01537; -.
DR eggNOG; ENOG502S9PF; Eukaryota.
DR HOGENOM; CLU_009397_8_1_1; -.
DR InParanoid; F7VR39; -.
DR OMA; TWYAYAT; -.
DR OrthoDB; 1435052at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08999; GH43_ABN-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..326
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003363630"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 154
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 326 AA; 35402 MW; B623F567DE0AB872 CRC64;
MQLTSLLSVI VALAMAPLVT LASPAETLGN RDFPDPAITF DPRTHEWYAF ATNSNGKNVQ
AAYSPRPLDG PWTYVEHDLL PTPGKWVNPD QHDIWAPDVH YFEATDSFVM YYSGLLADSR
YHCVGIATAE NITGPYEALD EPFACPDSEG GAIDASGYVD PIDGSFFVVY KVDGSSKGPG
GPCGNGDPPG EPTPFRLQRV NESDGITPIG HYTEILDRDP ELDGPLIEAP NLIRTWNGTF
VLFYSSHCYN TPEYDVKYAT ADKIEGPYHR HGELMNTTSF GFDGPGGASS VRGGGIMVFH
ANCDAGRCMY VTEFVVEGDG IVTLLD
//
