ID H6BSF6_EXODN Unreviewed; 816 AA.
AC H6BSF6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glucan 1,3-beta-glucosidase {ECO:0000313|EMBL:EHY53362.1};
GN ORFNames=HMPREF1120_01556 {ECO:0000313|EMBL:EHY53362.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53362.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53362.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53362.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; JH226131; EHY53362.1; -; Genomic_DNA.
DR RefSeq; XP_009153823.1; XM_009155575.1.
DR AlphaFoldDB; H6BSF6; -.
DR STRING; 858893.H6BSF6; -.
DR GeneID; 20306195; -.
DR VEuPathDB; FungiDB:HMPREF1120_01556; -.
DR eggNOG; ENOG502QV54; Eukaryota.
DR HOGENOM; CLU_002540_2_1_1; -.
DR InParanoid; H6BSF6; -.
DR OMA; IMSESQG; -.
DR OrthoDB; 3714838at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039279; QRT3-like.
DR PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..816
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003603517"
FT DOMAIN 49..285
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 441..512
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
SQ SEQUENCE 816 AA; 88676 MW; A9D745218FA59545 CRC64;
MWSSCRHLWV VVLYLVHFTA CLSAQSTYWL ANKPNVGKVA FQDPSYPVFR NVKDYGATGG
GVQDDSDAIN RAIAAPGNRC GGGNSTYGSF CQSSTVTPAL VYFPPGTYLV SKPLVMYYFT
QMVGDAVNPP TIKVQSNFTN IVGLAVLDAN IYIPSGSGSE WYANQNNFYR QVRNFIIDMT
TAPLKTAGIH WQVAQATSLQ NVVINMVAKD VVNNQQQGIY MENGSGGFFS DMVITGGAVG
MYLGNQQFTT RKIHLDGCLT AIKMNFDWLW TFTQITITNS DVGIDMTNGG FSNQAIGSLV
LLDSTISATQ GILTPYAPGY SSPQAAGTLI LENVDFTGSQ AAISAAGGTQ ARTVLAGGQF
IPLFAQGNAW TTAGQALNGQ SFNGTTCTYA NSSQTAYSAQ ETTIQRQLAP IPRPSSLVDS
NGQYIYRVKP QYETLQWSSF LSAKAHGLLG DGVTDDTVAM QALFNLAANT GQIVYFDKGA
YIVSSTVTVP PNVKITGELL SIIMATGSFF NSEMNPKPMW KIGNPGDVGT VEISDLIFET
KGPCPGAIMI EWNIKAAGPA LAGIWDAHWR IGGSAGTQLQ QDTCIKTPAT PIASGNAKLT
NCIGAFLLLH VTPQADGYFE NTWGWVADHE LDMGTRDQVY IFNKGGFLIE SNNGPVWMYG
TAAEHSVMYD YQFVNARNVF MGHIQHETAY FQGNPNALLP FTPQDSWHDP TYSDCVQPNC
ARTWGLRFVN SSSIFMYGGG LYNFFENWNT QACLGTESCQ ERMVDIRNST DIYLWALSTK
GSQFMISYEG TDVVPYSVNK ANFCETIALF ELAADQ
//