ID   A3LYK1_PICST            Unreviewed;       408 AA.
AC   A3LYK1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Hyphally regulated cell wall protein {ECO:0000313|EMBL:ABN67653.2};
DE            EC=3.2.1.18 {ECO:0000313|EMBL:ABN67653.2};
DE   Flags: Fragment;
GN   Name=HYR6.4 {ECO:0000313|EMBL:ABN67653.2};
GN   ORFNames=PICST_61722 {ECO:0000313|EMBL:ABN67653.2};
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:ABN67653.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN67653.2, 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}.
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DR   EMBL; CP000500; ABN67653.2; -; Genomic_DNA.
DR   RefSeq; XP_001385682.2; XM_001385645.1.
DR   AlphaFoldDB; A3LYK1; -.
DR   STRING; 322104.A3LYK1; -.
DR   GeneID; 4840201; -.
DR   KEGG; pic:PICST_61722; -.
DR   HOGENOM; CLU_006199_3_1_1; -.
DR   InParanoid; A3LYK1; -.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR   Pfam; PF11765; Hyphal_reg_CWP; 1.
PE   4: Predicted;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Glycosidase {ECO:0000313|EMBL:ABN67653.2};
KW   Hydrolase {ECO:0000313|EMBL:ABN67653.2};
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..408
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002655107"
FT   DOMAIN          11..340
FT                   /note="Hyphally-regulated cell wall protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11765"
FT   NON_TER         408
FT                   /evidence="ECO:0000313|EMBL:ABN67653.2"
SQ   SEQUENCE   408 AA;  42135 MW;  12CD4FCB35436C3D CRC64;
     MLFLKLLVRT LACVAAVLAI DITSPRIDRG VVNLSIGDIT IESGAYWSIV DNAVSVLAGD
     LDVKDDAGFY ITSTQSLIGL SVTLASGLGS ITNDGIIAFN SVVSLVAPNY NLIGLSFTNN
     GEMYLGTNGS VVGAPPINLV APSWTNTGLL VIYSQTRSAD GIVNLGGTGL VIQNNGQICL
     TNELYQASTQ IRGTGCITAN VDSTVFLANG LLGVDQSQTF YLADSRSSIR ANAVAVPQTF
     TIAGFGNGNI IGLDIPLATV FPLSSWSYTS STGILTLRGL GLLSQNFNIG PGYNSNLFSI
     TTDSSLGLAS VPLGGLTYSG PVPNAIPSNC QPCKNLPSAP GTSASVTSTS FTSTKSDGSI
     CTDVDQILIS TDAQGSWFTS TSLVSEVCST IPNSQTTETS TWTGTTTK
//