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Database: UniProt
Entry: Q7SGD7_NEUCR
LinkDB: Q7SGD7_NEUCR
Original site: Q7SGD7_NEUCR 
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
//
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