ID A0A0D1EC23_USTMA Unreviewed; 352 AA.
AC A0A0D1EC23;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=GH16 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=UMAG_00330 {ECO:0000313|EMBL:KIS71900.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS71900.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS71900.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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}.
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DR EMBL; CM003140; KIS71900.1; -; Genomic_DNA.
DR RefSeq; XP_011386231.1; XM_011387929.1.
DR AlphaFoldDB; A0A0D1EC23; -.
DR STRING; 237631.A0A0D1EC23; -.
DR EnsemblFungi; KIS71900; KIS71900; UMAG_00330.
DR GeneID; 23561664; -.
DR KEGG; uma:UMAG_00330; -.
DR VEuPathDB; FungiDB:UMAG_00330; -.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR InParanoid; A0A0D1EC23; -.
DR OMA; DWHTYTI; -.
DR OrthoDB; 337487at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006037; P:cell wall chitin metabolic process; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR PANTHER; PTHR10963:SF22; GLYCOSIDASE CRH2-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..352
FT /note="GH16 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002229822"
FT DOMAIN 27..73
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 67..303
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 328..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 42..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 352 AA; 38729 MW; 31560D99BF0B794D CRC64;
MASSRFTSLL FALAAALTIF TLVVSAQETC SATSKCGEAA PCCSAYGFCG SSNAYCLGQC
DPTSSFSPSS CKPMPKCKSQ TISFENNAKP WVAASSYRGD PNQAPFTLDE GVAEPSKSGT
KLILTKSGTA KRGTLLSSTR YWYYGSASAV MKHGSWAGVV HTFIGMSPTK DEIDWEFTTG
SDQDVQTNWY WFGEPEGYTH GFTVPDGTLN DISRPRFSVR DWHTYTIDWS PNRLRWSIDG
TVVRTLYRKN TYNSHDKLYH YPSSPMRLQL SIWGAGDGTF QQGTVDWAGG LIDWSQAHNA
RFVNMVKSVT ISCNDPEDVK NNRPNYAFSA KQTNPQNGQP KVLATSRSSI IS
//
