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Database: UniProt
Entry: A0A0F7ZVJ2_9HYPO
LinkDB: A0A0F7ZVJ2_9HYPO
Original site: A0A0F7ZVJ2_9HYPO 
ID   A0A0F7ZVJ2_9HYPO        Unreviewed;      1077 AA.
AC   A0A0F7ZVJ2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=HIM_04044 {ECO:0000313|EMBL:KJZ76708.1};
OS   Hirsutella minnesotensis 3608.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX   NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ76708.1, ECO:0000313|Proteomes:UP000054481};
RN   [1] {ECO:0000313|EMBL:KJZ76708.1, ECO:0000313|Proteomes:UP000054481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3608 {ECO:0000313|EMBL:KJZ76708.1,
RC   ECO:0000313|Proteomes:UP000054481};
RX   PubMed=25359922; DOI=10.1093/gbe/evu241;
RA   Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA   Bushley K.E., Xiang M., Liu X.;
RT   "Comparative genomics and transcriptomics analyses reveal divergent
RT   lifestyle features of nematode endoparasitic fungus Hirsutella
RT   minnesotensis.";
RL   Genome Biol. Evol. 6:3077-3093(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; KQ030510; KJZ76708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7ZVJ2; -.
DR   OrthoDB; 2786490at2759; -.
DR   Proteomes; UP000054481; 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:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054481}.
FT   DOMAIN          552..631
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1077 AA;  121729 MW;  63DEE77A4D9D7569 CRC64;
     MGGGHDLKDR STYPLFAQRP VGVPKTSILK SRIEPFYKSG QYDKVNLLAN LFKGRFSGKP
     HVKLEVWSAP GQERPTFKEA VSHDFKETST GASFGPSWST HWFRVHLTVP KDIVDEELVV
     FEWDAGNEGL VWTEDGMPLQ GLTGGGERVE WIIPKSFRDN KEHIIYIEMA CNGMFGNAPN
     GKTSIAPPDP NRYYTLGKAT IAAVNVQARM LYFDMWELGD AARELPENSA EQNHALAVAM
     KIIDTFQVNN QDSILKCRKL AQEIIGPDVD SHKVYQVGKD PVVFGIGHCH IDTCWLWPWA
     ETKRKVCRSW SSQCDLMDRY PEAHFACSQA QQFKWLKQYY PGAFERVKNK VREGQFHPIG
     GSWVEHDTNM PSGESLVRQF FYGQRFFEAE FGNRCRTFWL PDTFGYSSQI PQLCRLAGMD
     RFMTQKLSWN NINSFPHTTF MWVSPDGSQV ICHMPPSETY TSDADFGDLR RSIAQHKTMR
     VDKSSLLVFG KGDGGGGPTW QHFEKLRRCA GISNTTGSIP KVKLGLTVDD FFDRLAPKAD
     EFPTWSGELY FELHRGTYTT QANNKHFNRK AEVMLRDVEQ LATFASLKSS SYKYPSEDID
     TMWQAVLLCQ FHDCLPGSSI EMCYDDSDKL YAEVFKTGEK LLKDLYQNLN VFNAQPSQLK
     ESVVLNTLPW HRKEIVEISE TEAGIACGEG HLLPLRTFKI QDEKPAVTVE ETTHGFVLEN
     DDLRVIVEGG CITSLYDRVN NREVIEKGGK ANKFVIFDDI PLFWEAWDVE VYHLETKRDL
     KYGHTKIFES KPHKATLVTD IQISGQSSLK SYISLSASIK GQASQVNCSA EVDWHENSKF
     LKVEFPVEVV NNEASYETAY SITKRPTHYN TSWDMAKFEV CCHKFADLSE HNYGVSILND
     SKYGFATAGK TMRLSLLRAP KAPDANADMG KHSIRWAIFP HKGSLSAATV KAAYAFNNPL
     KLLSASDAAE TLAAAPIKLI NQDESESLIV DAVKRGHDDE DVSRHEGLRV NKGQSVIVRI
     FESLGGRSRG TIQTTLNVKR VTRVNILEDE LDEVKFADGK FAVELRPFEV ATFKLQL
//
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