ID   A0A0P7AY40_9HYPO        Unreviewed;      1107 AA.
AC   A0A0P7AY40;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Glycoside hydrolase family 3 N-terminal domain-containing protein {ECO:0000259|Pfam:PF00933};
GN   ORFNames=AK830_g8173 {ECO:0000313|EMBL:KPM38387.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM38387.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM38387.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM38387.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:KPM38387.1}.
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DR   EMBL; LKCW01000135; KPM38387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7AY40; -.
DR   STRING; 78410.A0A0P7AY40; -.
DR   OrthoDB; 2732849at2759; -.
DR   Proteomes; UP000050424; 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   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   PANTHER; PTHR30480:SF8; PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04060)-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424}.
FT   DOMAIN          196..524
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1107 AA;  120309 MW;  A63D5E864F99FE81 CRC64;
     MPDTPMAWHS SIRPTSKRPS FHNHQQSPAS SLTTSIPQCH QTRQWTAVAV AVAVAVAVAA
     AACVCPMAPC NVNPAAVHHT SNTKLRPPRP TRPLSAGGQP IAAPRAPRAG VYASAKFPTL
     RSMAAPHGSD SSSSSSPPPD KASHRYLKPK SRSDRHLNSS SAGPRYHVTR RRRRHRPTAM
     ASSGSVDDLD PLWQNLDWAI GQILIMGWDG TEVTPQIRSL IEDHHLGSII LTAKNLKSAQ
     QTAKLVQELQ AIAQQAGHPQ PLLIALDQEN GGVNSLFDED YVCQFPSAMG VAATGRAELA
     YEVTKATATE ISACGVNLML GPVLDVLNNA RYQPLGVRAS GDDPQEVSQY GLAALRGIRD
     AGMASCGKHF PSYGNLDFLG SNLDVPIITQ TLEELSLSAL VPFRNAIASG KLDAMFIGGC
     GISSPSMNVS HACLSDQVVD ELLRNDLGFN GVAISECLEM EALSHELGVQ NGVVMAVEAG
     CDLVLLCRAY DVQLEAIKGL KLGYESGIIS KERIFTSLRR VLRLKATCTS WTKALNPPGI
     SLLSQLHPKH LMLSLQAYDD SITVIRDKEK LLPLTSSMHP GEELLLLTPL VKPLPASSLT
     KKLLDSKDSQ RSVWTNHDMW SHRDRERGAI MSGEGVFREF GKSLARSRNQ KLLHTSYTAN
     GVRPVHENLI NRASCIIIVT ADANRNLYQA GFTKHVDMMC SMLRSRGQKK QLIVVAVSSP
     YDFAMDKSIG TYLCTFDFTE NALHALARAL VGDITPLGTL PGTLRKSKKV LKSRQHWLVE
     EYHPERDSSG LDELLLAVHR ASAPDLQFLQ TTTAATFQLD NQHISEAHFV VRNSSTQALY
     GFVATYYLHG VGILGAIFVD PGKRDVSIGR SLHRRAMKSL TQRRGIKKLQ IGTALPGVFP
     GIPVDVEVNT TKDWFTNSGW DTQFPRRVTD MVIHDLASWA APEGLLQSIQ RVNISFDLIH
     GLDNAESVLS HVRAHTNPEI LELYRSALSE TKSCGIVRAK DGTGSLLGTV IICRQHSHLA
     TYVPALVSHA EDIGGILAPV VSAMPFATLV LQGLALMGVR QNKNHRATKT VLGWVVDDGT
     EPLAAMGFET LQAFDEITNS PDSFASQ
//