ID A0A369GZS2_9HYPO Unreviewed; 1077 AA.
AC A0A369GZS2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=CP532_0582 {ECO:0000313|EMBL:RDA89234.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA89234.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA89234.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA89234.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDA89234.1}.
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DR EMBL; PDHP01000002; RDA89234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GZS2; -.
DR STRING; 2039875.A0A369GZS2; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR CDD; cd10812; GH38N_AMII_ScAms1_like; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748}.
FT DOMAIN 552..631
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1077 AA; 121680 MW; FB991575186E01B3 CRC64;
MGGGGQNKSN SSYPLFAHRP VGVPKTSILK DRIEPFYKSG QYDKVNLLAN LYKARYSGQP
HVKLYVWSAP DQERPTFKDA VSHDFKETNT GASFGPSWST HWFRVHLTVP KDVIDEELVI
LEWDAGNEGL VWSQDGTPLQ GLTGGGERIE WIIPKSFRDA KEHVIYVEMA CNGMFGNAPN
GKTSIAPPDP NRYYTLSRAD IAVVNVPARM LHFDMWELGD AARELPENSA EQSHALAVAM
KIIDTFQVND QESIIECRKL AREIIGPDVD SHRVYDVGKD PVVFGIGHCH IDTCWLWPWA
ETKRKICRSW LSQCDLMDRY PEAHFACSSA QQFKWLKSYY PSAFERVKSK VAAGQFHPIG
GSWVEHDTNM PSGESLVRQF FYGQKFFEKE FGTRCRTFWL PDTFGYSSQL PQLCRLAGMD
RFMTQKLSWN NINTFPHTTF MWVSPDGSQV ICHMPPSETY TSEANFGDLS RSITQHKTLR
VDSSSLLVFG KGDGGGGPTW QHFEKLRRCA GISNTVGGIP KLKLGLTVDD FFDRLAPKAN
DFPTWHGELY FELHRGTYTT QANNKFFNRK AEVMLRDLEQ LATFASIKNE SYAYPREEID
EMWEAVLLCQ FHDCLPGSSI EMCYDDSDKL YAQVFKQGQA LLEGLYHSMG ISDARPSSSK
ESVVLNTLPW HRQEIVEVSD TEAVIASGDG QLLDMRALKP EDDKPAVRLT EKDDVFVLEN
DHLRVVVEGG CITSLYDRVN DREVVEKGGK ANKFVIFDDI PLFWEAWDVE VYHLETERQL
TYGKTKVHES KPHRATLVTE IKISGESSLK AYISLSAAIE GQPSQVDCSA EVDWHENSKF
LKVEFPVEVV STEASYESAY AITKRPTHYN TSWDMAKFEV CCHKFADLSE HNYGVSILND
SKYGFATVGK TMRLSLLRAP KAPDAHADMG HHAIRWAIFP HKGYLSSQTV RAAYAFNNPL
KLLSASSAEA KHSLDAPIKL VNLDESGSLI LDVVKRGHEV EASHYRMLPT KEAPSMILRV
YESLGGRSKG VVRTKLQVKR VAKCNVLEDE QEEVKVADGQ FFIELRPFEV ATFKVQL
//
