GenomeNet

Database: UniProt
Entry: G9MJQ6_HYPVG
LinkDB: G9MJQ6_HYPVG
Original site: G9MJQ6_HYPVG 
ID   G9MJQ6_HYPVG            Unreviewed;       293 AA.
AC   G9MJQ6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Carbohydrate esterase family 4 protein {ECO:0000313|EMBL:EHK25719.1};
GN   ORFNames=TRIVIDRAFT_189461 {ECO:0000313|EMBL:EHK25719.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK25719.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK25719.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
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:EHK25719.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABDF02000003; EHK25719.1; -; Genomic_DNA.
DR   RefSeq; XP_013959920.1; XM_014104445.1.
DR   AlphaFoldDB; G9MJQ6; -.
DR   STRING; 413071.G9MJQ6; -.
DR   EnsemblFungi; EHK25719; EHK25719; TRIVIDRAFT_189461.
DR   GeneID; 25789406; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_189461; -.
DR   eggNOG; ENOG502QRIP; Eukaryota.
DR   HOGENOM; CLU_021264_11_0_1; -.
DR   InParanoid; G9MJQ6; -.
DR   OMA; WSHADLC; -.
DR   OrthoDB; 1343935at2759; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10951; CE4_ClCDA_like; 1.
DR   CDD; cd00035; ChtBD1; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR46471:SF4; CHITIN DEACETYLASE; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00261}; Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT   DOMAIN          1..45
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          78..275
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        15..29
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   293 AA;  32138 MW;  5789D7BA7A44611A CRC64;
     MSCGSGVGSC PSGQCCSESG FCGTTEDYCQ APQCQIAYSN GSCDANQMPA GQSTKSIPRN
     TNGKAPYNVY ITNCTHPGNV ALTFDDGPYN YTTQLLNILD SFNVKATFFI VGNNLGKGPI
     DVESNGWAKI LRRMYRSGHQ LGSHTWGHAD LSAASSEIRE QQIIYNEMAF RNIFGFFPTY
     LRPPYGTCSR DSGCLGYVTS LGYHVVNWNI DTKDYLNDSP QLIGNSKAIF YNALASANPK
     HDGFISLSHD THEQTVISLT AYMIKTLRSK GFRPVTVGEC LGDPRSNWYT NAR
//
DBGET integrated database retrieval system