HEXA_ARTBC
ID HEXA_ARTBC Reviewed; 353 AA.
AC D4AQ52;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Uncharacterized secreted glycosyl hydrolase ARB_06359 {ECO:0000305};
DE EC=3.2.1.- {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_06359;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; ABSU01000005; EFE34596.1; -; Genomic_DNA.
DR RefSeq; XP_003015236.1; XM_003015190.1.
DR AlphaFoldDB; D4AQ52; -.
DR SMR; D4AQ52; -.
DR STRING; 663331.D4AQ52; -.
DR PRIDE; D4AQ52; -.
DR EnsemblFungi; EFE34596; EFE34596; ARB_06359.
DR GeneID; 9520960; -.
DR KEGG; abe:ARB_06359; -.
DR eggNOG; ENOG502SJNP; Eukaryota.
DR HOGENOM; CLU_008392_0_1_1; -.
DR OMA; WQMAAEM; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.300; -; 1.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..353
FT /note="Uncharacterized secreted glycosyl hydrolase
FT ARB_06359"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434661"
FT REGION 94..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 353 AA; 37598 MW; 1E12DCF12B71B332 CRC64;
MKFVLFAQLA AVAAPAIAID LAVQAGQHVM YSYPGLTPPE SLYKLTSEGK VGGLIIFKEN
VNSNLPAIMD KFQALYKASP AYNGHPMIIT TDQEGGNVRR VPGGPSQSAR QIGDSSTPMQ
AASQAGRDAA AALKAQKING NLAPVLDIYR EEGNFIDEFG RSFGNNTEIV TSCGSAFAIS
QSRSGVLSTV KHFPGLGAAK KGENTDLVPI KIDLSLDEIR TFDEVPYRTA IRNGVDLIMT
SWAVYPSLDA KYPAGLSRKW TTDELRTRLG YKGVIITDAI EAGSLKSFGN DGQRGVLAAK
AGVDILLASG RNATQGEAIV NEIVAALKKG TLSMTEFQES SKRIQALQSR LSA