ID Q7SGD7_NEUCR Unreviewed; 677 AA.
AC Q7SGD7;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 3.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:EAA35942.3};
GN ORFNames=NCU00985 {ECO:0000313|EMBL:EAA35942.3};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA35942.3, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA35942.3, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CM002236; EAA35942.3; -; Genomic_DNA.
DR RefSeq; XP_965178.3; XM_960085.3.
DR AlphaFoldDB; Q7SGD7; -.
DR STRING; 367110.Q7SGD7; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; 5141-EFNCRP00000000684; -.
DR EnsemblFungi; EAA35942; EAA35942; NCU00985.
DR GeneID; 3881286; -.
DR KEGG; ncr:NCU00985; -.
DR VEuPathDB; FungiDB:NCU00985; -.
DR HOGENOM; CLU_009935_3_1_1; -.
DR InParanoid; Q7SGD7; -.
DR OrthoDB; 19834at2759; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAA35942.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..677
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004291293"
FT DOMAIN 158..271
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 285..364
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 405..530
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 75432 MW; 6EDDF0E0DE5E5F2C CRC64;
MAPRSLLSLS LSLLTLFTPL SHASAIRQGA ANPPKIPSGP NGSGESPPQP YAPQPALLTT
EWTASVGADP SNHWPQHPRP QLKRDDKWWQ SLNGIWRYQN LHFASSARMN VDISTLAPDV
EVEGGYDGGE GGGGMPTEEK ETLIPSCIES GFSGIQEMNV TGMVFKRTLE FPKKWMNETG
RRVLIHFEAV DYEAVVYVND KKLGHNVGGY FRFTVDATNA LKTGKKNELQ VIVRDPTDEP
GFYTPHGKQT RTPSHIFYTP CTGIWQSVWM ESVPGDNYIG DLDVSADMEG NVTMTVYSSS
KTTTAVKVSI LENGTEVATH DASSDQEFSF QVPDPKLWSP DSPTLYNISV TMGDDQITSY
TGFRTISKGV VNGIQRPLLN GKFVFQFGPL DQGYWPDGIY LPPTEEAMLY DLDLIKSLGM
NMVRKHIKVE PQLYYYACDK LGLLVIQDMP SMRPAASLAT DFPTPAQQAE FERQLSVMVN
QFKHHPSITT WVIYNEGWGQ IRDNGNYPEF HITDAIRALD PTRLIDSVTG WFDHGAGDFH
DNHHYASPEC GTPFYSSPNT PYDPNRIGFQ GEFGGVGHVP DSKNLWPDPK AIATIPETYE
ISPDLDSYNY RTHELLGELR TQVERYACSG AVYTQTTDVE GEVNGLVTYD RRVVRVNVTQ
WQSDIQALYD AAEKRAS
//