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Database: UniProt
Entry: A0A161VMU0_9PEZI
LinkDB: A0A161VMU0_9PEZI
Original site: A0A161VMU0_9PEZI 
ID   A0A161VMU0_9PEZI        Unreviewed;       408 AA.
AC   A0A161VMU0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KZL72315.1};
GN   ORFNames=CT0861_10035 {ECO:0000313|EMBL:KZL72315.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL72315.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL72315.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL72315.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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:KZL72315.1}.
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DR   EMBL; LFIV01000060; KZL72315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161VMU0; -.
DR   STRING; 708197.A0A161VMU0; -.
DR   OrthoDB; 2733845at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR018828; RRG7.
DR   PANTHER; PTHR28133; REQUIRED FOR RESPIRATORY GROWTH PROTEIN 7, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR28133:SF1; REQUIRED FOR RESPIRATORY GROWTH PROTEIN 7, MITOCHONDRIAL; 1.
DR   Pfam; PF10356; RRG7; 2.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE   4: Predicted;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Transferase {ECO:0000313|EMBL:KZL72315.1}.
FT   DOMAIN          242..287
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DISULFID        261..275
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   408 AA;  43456 MW;  9D8A510A8A94031C CRC64;
     MRQSRKERPE LLYPDPPTTH HHNLASFVAY AERTGLDVAS TVYVGTHYEY TVSATLSQYG
     IQAVRVGGAS DKGIDLLGTW DTPSQNEPLK VILQCKGGAQ RAGPSLVREL EGSFIGAPVG
     WRGDGVVAFL VSEKTASKGV REALEMADFW FAEIDFFFAL SPGLERDCSN IQPNTEYCTV
     GFEPLRDPEG RCGPQFGNAS CAYGSLPCCN SQTWKCSETY EDCAPGTCYE GFCPGDAVWS
     TGGTCDTGHG NRQCAGKWGD CCNQDGWCGT GPDFCGKDVC QMGNCTAPIV PVLSSSVPVS
     FPPVTESFAQ LTTATSLSLS STAGSNAQGI SDHFKGLRSY SCDFNLCPAG VFVCTSPAAE
     PAAIPELTDR HGCPGDNVAG GKDHAYYVDL CEFTCSHGYC PAGTCQYC
//
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