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Database: UniProt
Entry: A0A2P4ZGC9_9HYPO
LinkDB: A0A2P4ZGC9_9HYPO
Original site: A0A2P4ZGC9_9HYPO 
ID   A0A2P4ZGC9_9HYPO        Unreviewed;      1178 AA.
AC   A0A2P4ZGC9;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:PON23349.1};
GN   ORFNames=TGAM01_v207876 {ECO:0000313|EMBL:PON23349.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:PON23349.1, ECO:0000313|Proteomes:UP000054821};
RN   [1] {ECO:0000313|EMBL:PON23349.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON23349.1,
RC   ECO:0000313|Proteomes:UP000054821};
RX   PubMed=26893428;
RA   Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT   "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT   Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL   Genome Announc. 4:e01747-15(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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:PON23349.1}.
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DR   EMBL; JPDN02000030; PON23349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P4ZGC9; -.
DR   STRING; 398673.A0A2P4ZGC9; -.
DR   OrthoDB; 1435080at2759; -.
DR   Proteomes; UP000054821; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 1.20.1050.60; alpha-1,2-mannosidase; 1.
DR   Gene3D; 1.20.1610.10; alpha-1,2-mannosidases domains; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   Gene3D; 3.30.2080.10; GH92 mannosidase domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR005887; GH92_a_mannosidase_put.
DR   InterPro; IPR041371; GH92_N.
DR   InterPro; IPR012939; Glyco_hydro_92.
DR   NCBIfam; TIGR01180; aman2_put; 1.
DR   PANTHER; PTHR12143:SF27; ALPHA-1,2-MANNOSIDASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G10520); 1.
DR   PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   Pfam; PF07971; Glyco_hydro_92; 1.
DR   Pfam; PF17678; Glyco_hydro_92N; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PON23349.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054821}.
FT   DOMAIN          412..683
FT                   /note="Glycosyl hydrolase family 92 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17678"
FT   DOMAIN          693..1160
FT                   /note="Glycosyl hydrolase family 92"
FT                   /evidence="ECO:0000259|Pfam:PF07971"
FT   REGION          628..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  129344 MW;  637CCC770B1CB222 CRC64;
     MAPQQNHDKF GYPKLLNKSN DAAATVNVPI KPLHDPQTNC TEQMMIWQWD EATGWEAPEI
     RPYGPLPIMP SASVLQYATE CFEGIKIYRG YDDRLRVFRL QLNCERMLKS SLRVGLPSFD
     IAHLESIIMQ YGALQAEKWL PSGQTGQTLY LRPTHIGTTA ALGVQRPRQS LIYIIATLLP
     GFSTKGNGMR LLTSPADTAR AWPGGFGNRK LGGNYGPTLP AHDAALQAGF DQILWLFGPE
     GFVTEAGASN FFVVWKTKQG DIELVTAGLD NGTILEGVTR YSVLDLVRSN RNQQSVWQYE
     GKSLPPLTAV ERDFSINEIQ DAVEEGRLIE AFAAGTAYFI APAEIIHHRG KDIHIPLPSA
     ESASIFKFPS DSVATAAQSR IVTMFGWMTL GVFAQTLSAF AVPTQDEDLS VYVNPFIGTA
     GPDGTGANSG DTFPGVSLPF GVVKLGPDTT EMNPSTNAFA GYTPDGNVTA FTCFHECGIG
     GASKYGVVGH MPLTTLAGIN VLDNTTYQQP RVSMDRAAVG YYRSDLANGV TVELTASNHA
     GFFQYTYPEN TDRIILLDVS HNLPSLAEFI KSQSYSNGQI EVTNGGRRVR GWGVWRGGWG
     GTGINWGVGK FSSAHQNWQY FSGPWNAPDN PPSPSTPVTW GNASTNPHGV QGGPDGDDSG
     DRVGAVFKFP AKTTVVKSKT GVSFISVEKA CAFQKEIPSW TLNDTVKATK KVWNDDVFSK
     ISIQEPSKNE TRLTLFYSAL YRMHQMPSDR TGENPIWNST EPYYDDYYTL WDTFRCLNSF
     YLLVQPQRGV GMIRSLIDIW RHVGFMPDGR SGNHNGKVQG GSNADNVLAD AYVKGFTDGI
     DWNDGYRAVW TDAEVVPPPN NDPEDSTCTD NQGRCGLPDW INLGYVSTTF SSSISRTVEY
     SLNDFSVSQI AKGIAPNNYQ KYLNRSGNWK NLWNPAINQY NTSGFLGPRN ANGTMITIAP
     QDESYTTEGL PWEYTWTVPF DMQSLIEKMG GADATEKRLD IMFVPDLRTT DLGVGVGSGT
     TLFNPGNEPS FGTPFLYNYL PGRQYKAVNQ SRVNIDENYF TGSNGLPGNS DAGAMDSWML
     WQMLGLYPVV TQPVYLILAP WFEDISVSVG GSYTLRIKAQ GLSNTSFFVQ SLKVNGKPWS
     KSWLEHSDIA KGGLLEFVLG PEPKSWDTGD VPPSPGHQ
//
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