ID A0A167AII5_9PEZI Unreviewed; 702 AA.
AC A0A167AII5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KZL80180.1};
GN ORFNames=CI238_08344 {ECO:0000313|EMBL:KZL80180.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL80180.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL80180.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL80180.1,
RC ECO:0000313|Proteomes:UP000076584};
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 -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000256|ARBA:ARBA00005495}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:KZL80180.1}.
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DR EMBL; LFIW01001977; KZL80180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167AII5; -.
DR SMR; A0A167AII5; -.
DR STRING; 1573173.A0A167AII5; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.90.1590.10; glutathione-dependent formaldehyde- activating enzyme (gfa); 1.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF04828; GFA; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZL80180.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 10..120
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000259|PROSITE:PS51891"
SQ SEQUENCE 702 AA; 78035 MW; 09B2F585EF0728A5 CRC64;
MSDAIAPPLI NGSCLCGAIR YTVAGGHAFT VLCHCNSCRK FTGSSFGANS LVDRKNLTVQ
DPGSKISVYG AQTADSGRSL ARSFCSACGS SLFIANDIDP TQIAVTSGTM DDVQGVEGTD
SDKLWTPKQA TPVEFSLGAA TMTTHEDGAI FLNPVIPGFN PDPTVCVVPA TESSPTRYFL
STSTFEYFPG CAIYTSEDLI NWELIGHALT RKSQIELRTV EPGAGSWAST LRYRPQEKRW
YLANGLFQRY RPTNDERIFP RGFYVWTDNI WDENAWSEPV YFDNPGFDQD LFWDDNGKVY
LSTTVRMGTR TPGLKLKDFA IHISEIDITT GRTITPPRVI RKSPYGIAEG SHIIRKGKYY
YLFTAEGGTE AGHQEWVLRS EAGPYGPWEG QDRALWYNGP DEEVQRTGHC DVFEDGRGRW
WAVMLGVRPV KSGDKYLEPQ MGRETFLVQV DWEDDWPIFN KGRNVTLQTV GREPIQKVAV
ADANGVKWKA DLSKPSLELG WYHKNTPIKP CYSLTERPGH LRLYGNCFDL NSPESPAMLL
RKQSSYSETF RVKMLFNPSR PGYESGVTVW WSQYSYATIG IGAVQPEDGG PAIPTIFRRE
PTGKANELRL THPLLESDGS SVPSLNLNHP VQLSITTKPT EYEMYLSAGE VNTKLSFTSE
ALTVFPPVGG AFCGVMYGVY SFGRSEPVLD PSDFTDVEIL EI
//