CRH11_ARTBC
ID CRH11_ARTBC Reviewed; 465 AA.
AC D4ALQ5;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Probable extracellular glycosidase ARB_05253 {ECO:0000305};
DE EC=3.2.-.- {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_05253;
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 -!- FUNCTION: Extracellular glycosidase which plays an important role in
CC fungal pathogenesis. Involved in cell wall assembly and regeneration,
CC and adherence to host cells. {ECO:0000250|UniProtKB:Q5AFA2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. Secreted,
CC cell wall {ECO:0000250|UniProtKB:Q5AFA2}. Membrane {ECO:0000255};
CC Lipid-anchor, GPI-anchor {ECO:0000255}. Note=Covalently-linked GPI-
CC modified cell wall protein (GPI-CWP).
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE36314.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSU01000002; EFE36314.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003016959.1; XM_003016913.1.
DR AlphaFoldDB; D4ALQ5; -.
DR SMR; D4ALQ5; -.
DR STRING; 663331.D4ALQ5; -.
DR EnsemblFungi; EFE36314; EFE36314; ARB_05253.
DR GeneID; 9526680; -.
DR KEGG; abe:ARB_05253; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_027506_2_0_1; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..441
FT /note="Probable extracellular glycosidase ARB_05253"
FT /id="PRO_0000434904"
FT PROPEP 442..465
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434905"
FT DOMAIN 22..223
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 261..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P27051"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27051"
FT LIPID 441
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 465 AA; 47574 MW; 0FB986C25C4CC5B3 CRC64;
MKLSLAAALL GALAVSAQTS TECNPLKQKC PADPALAGSA DFGLTSESPR FHATGGTPTY
GNDGASLTIG KRFDAPKLTS DFYIMFGYVE WEIKAAPGKG IVSSAVLLSD CLDEIDWEFL
GGDPNQVQSN FFGKGDTTTY DRVKFHPAPN NNQEFHKYAV DWTADKTTFY IDGQNVRELT
PDAAKGQYPQ TPMRVLAGSW AGGDPSNNQG TIEWAGGETD FSKVPFTMFV KSIKVTDYST
GKEYVYKDMT GKWESIQAVD GQVNKSGKPG SGPKVESSTL PSSPSTSAHV PVHTVPGGGI
GNPQAPNTGS SPSNTLTNGP SSTMTSLVGL PSSWIVTETG TGGVVTPTSA AESTSHHSDY
TSRSSRSVSS SVSASSGNGG HGMTTSTGSG SAPTGTGSLP GSGSGSAPGY PVPTGTNGGG
SNNPTDGGAS PTSPAMQAPG STGAIHSVSN ALLLSFCAIA AWALV
