ID H6BQE2_EXODN Unreviewed; 771 AA.
AC H6BQE2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Extracellular cell wall glucanase Crf1/allergen Asp F9 {ECO:0000313|EMBL:EHY54535.1};
GN ORFNames=HMPREF1120_02703 {ECO:0000313|EMBL:EHY54535.1};
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:EHY54535.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY54535.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY54535.1};
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 -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC {ECO:0000256|ARBA:ARBA00009805}.
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; JH226131; EHY54535.1; -; Genomic_DNA.
DR RefSeq; XP_009154996.1; XM_009156748.1.
DR AlphaFoldDB; H6BQE2; -.
DR STRING; 858893.H6BQE2; -.
DR GeneID; 20307342; -.
DR VEuPathDB; FungiDB:HMPREF1120_02703; -.
DR eggNOG; KOG3475; Eukaryota.
DR HOGENOM; CLU_353743_0_0_1; -.
DR InParanoid; H6BQE2; -.
DR OMA; RYDAPYI; -.
DR OrthoDB; 2680063at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd02183; GH16_fungal_CRH1_transglycosylase; 1.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 2.20.25.30; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR001569; Ribosomal_eL37.
DR InterPro; IPR011331; Ribosomal_eL37/eL43.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR10963:SF27; GLYCOSIDASE CRH1-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01907; Ribosomal_L37e; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022730};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..771
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003603224"
FT DOMAIN 21..240
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT DOMAIN 287..331
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 427..471
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 362..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 78799 MW; 8259743DC418C424 CRC64;
MMAIHTYLRT ALLLGAAVVG LASADACNPL NGPCPAIPGL ATSTYSIDFT QQTTTPSDWI
LADAATVNYG APNGANFTFA KRYDAPYIWS RFYVLFGRIE VVLKAAPGAG IITGAVMMSD
DLDEIDWEWS GNNFAGSNGK VQTNFFGKGI TGYYDRGSTP AVNNPQDQFH TYALDWSPDA
LTWSIDGQNV RTLKNSHATS GEYQFPQTPS RLHLGVWCAG DPGNNGATVA WGGGPTNFSQ
APFSAYVKSV KITTSSPCST WQYPNPFDGT YKSVVCTNQT ITNTLPCTYA VAQGDDGYKI
ATTLGVTLAA LKAANPNVNW DTLLVGQSLN VPGGNCTTSS SGSAVPSATS ASSDMAAATS
SANSAAVPTN SNSATLTSDA TSSPSSISSS ESASASIMMS GSALTAVASS TMAGSSLSSS
SQSAPATVYT VVAGDTGYGI PKKLGCSFDE IFGVNPGLDW DNLLVGQTLN LPSGCTRSLT
SSTLLPSSGA PTNPAQPSPS SQSASLTTET TTPPSDTPTS DNLAAASGTL PSAPAAASSS
APSITSGSTI TSTCTVVASQ SSVDSAATST QEDSSLSSNS DAAAASSQPP TTKNASSQSS
NSDTAAASSQ APATGSVPST SVSMTSSNTP LSPSSPVPTA AVPSVATSSG QASVVSIPVS
HTSASTTDKV NPVTPASAAK LSEQCLQLLG HNKTHTLCRR CGRRSLHIQK HTCANCGYPA
AKTRKYEWSE KAKRRKTTGT GRMRSLSTVN RKFKNGFQTG TPKGARGPLK A
//
