ID C6HDD5_AJECH Unreviewed; 903 AA.
AC C6HDD5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN ORFNames=HCDG_04216 {ECO:0000313|EMBL:EER41569.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER41569.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
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DR EMBL; GG692423; EER41569.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HDD5; -.
DR STRING; 544712.C6HDD5; -.
DR VEuPathDB; FungiDB:HCDG_04216; -.
DR HOGENOM; CLU_004624_4_0_1; -.
DR OMA; WWYWTWK; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 528..775
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 102749 MW; A7071417C588CED1 CRC64;
MPHHSRERER GEYRSRDRDR RQYHYEQANT HDRHEYTSHT YDDYGNDIQD SDDGDDDAVF
NDRRRSRHSR RNSSSHPQAR PSPARRTQLN PSHRPQQPQQ RTRRQGRSYD SDDDDGDDSE
SAVIVVDSRP NVSRPAHKKD RERDREGRRR RDSMADEESP RKGRLRDRRR KGLNDDDEEH
DVRGGFGTDR ERDKRRKEKE KYLPRESGVW NKQSKHASTD SANSATQLLS VDALAKLNAA
QMKAEAVEKA KTAKDEKALL EKERKRRKRE EAREKERRIP VQKGAKSKGW AGRRLVSGAF
LEEGRSPELK TRGGGGRGVW KDEKGRKGAA GGGGDDDKGG GWFASWSKKK KLCVSAGVLA
LLLIIIIPVA AVLSKNKKAD QGASDDSGDG PSDPASQGPP PRTELGNFDP NTLPESAKKT
YFDPRTWYDT ADMNVTYTDE TVGGLPIMGL NSTWDDSAQA NKNVPPLNKK FPYGKQPIRG
VNVGGWLSLE PFITPSFFSN YNFRDNVVDE YTLSKKLAPN AAQYIEKHYA TFINEQSFRE
IRDAGLDHVR IPYSYWLVKT YDDDPYVERI GWRYLLRAIE YCRKYGLRVN LDLHGVQGSQ
NGWNHSGRQG SIGWLEGNDG TKNGDRSLET HKQLATFFAQ ERYKNVVTIY GLANEPMMLK
LDIEAVINWN TKAISIIRES GLKDAKIAFG DGFLNLEKWK TIMQDVDDNL LLDTHQYTVF
NTGQVGLPHR KKLDFVCEAW VNLITKSNTK GTGWGPTICG EWSQADTDCA KYLNNVNVGS
RWLGTMDNPQ AKDQVLQAHC PTQWPQGDPA ANGPPCSCDQ ANADPSHYSD SYKKYLQMYA
EAQMYAFEKG YGWFYWTWQT ESAAQWSYKK GLDAGILPKK AYEPEFKCEN DKLGSFGDLE
EYY
//
