ID A3LYK2_PICST Unreviewed; 409 AA. AC A3LYK2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 2. DT 13-SEP-2023, entry version 61. DE SubName: Full=Hyphally regulated cell wall protein {ECO:0000313|EMBL:ABN67654.2}; DE EC=3.2.1.18 {ECO:0000313|EMBL:ABN67654.2}; DE Flags: Fragment; GN Name=HYR6.2 {ECO:0000313|EMBL:ABN67654.2}; GN ORFNames=PICST_3402 {ECO:0000313|EMBL:ABN67654.2}; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL OS Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces. OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN67654.2, ECO:0000313|Proteomes:UP000002258}; RN [1] {ECO:0000313|EMBL:ABN67654.2, ECO:0000313|Proteomes:UP000002258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545 RC {ECO:0000313|Proteomes:UP000002258}; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting RT yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. 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; CP000500; ABN67654.2; -; Genomic_DNA. DR RefSeq; XP_001385683.2; XM_001385646.1. DR AlphaFoldDB; A3LYK2; -. DR GeneID; 4840202; -. DR KEGG; pic:PICST_3402; -. DR HOGENOM; CLU_006199_3_1_1; -. DR InParanoid; A3LYK2; -. DR OMA; ANGSHKI; -. DR OrthoDB; 1997971at2759; -. DR Proteomes; UP000002258; Chromosome 6. DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt. DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR008440; Agglutinin-like_ALS_rpt. DR InterPro; IPR021031; Hyphal-reg_cell_wall_N. DR Pfam; PF05792; Candida_ALS; 2. DR Pfam; PF11765; Hyphal_reg_CWP; 1. PE 4: Predicted; KW Cell wall {ECO:0000256|ARBA:ARBA00022512}; KW Glycosidase {ECO:0000313|EMBL:ABN67654.2}; KW Hydrolase {ECO:0000313|EMBL:ABN67654.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002258}; KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..409 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002655700" FT DOMAIN 11..337 FT /note="Hyphally-regulated cell wall protein N-terminal" FT /evidence="ECO:0000259|Pfam:PF11765" FT NON_TER 409 FT /evidence="ECO:0000313|EMBL:ABN67654.2" SQ SEQUENCE 409 AA; 44143 MW; E8F78BFEBBCEC888 CRC64; MLLFRSLVRV FLFATVALAF TVQKPKVDRG SINLSIGDIT IQSGSFWSIF DNTVSIFKGD LWVQKNAGFF ITSTNKLIGL KVELASGFGS IRNDGLIVFN SLVSITPSFY KLIGKSFLNS GEIFLVSSGY GVPTAALLAP IWKNTGSLTF FQNKRNNGVV SLGAPGLKIE NWGQICLFNE LYKQTTHIFG DGCITADQDS SIFFSNCLLD IDSRQTVYLA DSRSSVRAVA LAKPKTFKVA GFGNGNKIGL DLPLISPFSK SVIYNAKTGI LSLRVKGFWG QDFNIGLGYN SNKFKITTDN SLGLLSVPWG AVYYDGPVPN KQIPSNCQPC KPYPSPPTTT TTKTNAQTTK TSTWTGTFTT TVTETDTPGG TDTVIVEVPS TPNSQTTLTS TWTGTFTTTV TETDTPGGT //