ID Q9HEP1_CANAX Unreviewed; 379 AA. AC Q9HEP1; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 68. DE SubName: Full=Mannoprotein MP65 {ECO:0000313|EMBL:CAC19886.1}; GN Name=mp65 {ECO:0000313|EMBL:CAC19886.1}; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5476 {ECO:0000313|EMBL:CAC19886.1}; RN [1] {ECO:0000313|EMBL:CAC19886.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 20955 {ECO:0000313|EMBL:CAC19886.1}; RA La Valle R., Silvia S.; RT "Cloning of MP65 mannoprotein coding gene."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. CC {ECO:0000256|ARBA:ARBA00008773, ECO:0000256|RuleBase:RU004335}. 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; AJ010064; CAC19886.1; -; mRNA. DR AlphaFoldDB; Q9HEP1; -. DR CAZy; GH17; Glycoside Hydrolase Family 17. DR VEuPathDB; FungiDB:C2_10030C_A; -. DR VEuPathDB; FungiDB:CAWG_01129; -. DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt. 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; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR000490; Glyco_hydro_17. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR16631:SF14; FAMILY 17 GLUCOSIDASE SCW10-RELATED; 1. DR PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1. DR Pfam; PF00332; Glyco_hydro_17; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1. PE 2: Evidence at transcript level; KW Cell wall {ECO:0000256|ARBA:ARBA00022512}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004336}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004336}; KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..379 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004327157" FT REGION 67..124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 67..118 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 379 AA; 39247 MW; 8CBC4B3B7EBEC3E4 CRC64; MLFKSFVTFT VLANALAAPL AHQHHQHKEE KRAVHVVTTT NVVVVTIGNG DQTTTFAAPS VAADSSVSVS VNTEPPQNHP TTTQDVASAS TYPSSTDGSA ASSSAAASSS SQAGSEPSGG VGSGGAKGIT YSPYSDNGGC KSSSQIASEI AQLSGFNVIR LYGVDCDQVA AVLIAKTSSQ KIFAGIFDVS SITSGIESLA EAVKSICGSW DDIYTVSIGN ELVNAGSATP SQIKAYVEEG RKALKAAGYT GPVVSVDTFI AVINNPDLCD YSDYMAVNAH AFFDGHVAAE NSGAWVLQQI QRVWTACGGK KNVLITETGW PSRGDSNGVA VPSKSNQQAA ISSIKSSCGA SAILFTAFND LWKADGPYNA EKYWGIYSN //