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Database: UniProt
Entry: A0A2R6NGZ2_9APHY
LinkDB: A0A2R6NGZ2_9APHY
Original site: A0A2R6NGZ2_9APHY 
ID   A0A2R6NGZ2_9APHY        Unreviewed;       979 AA.
AC   A0A2R6NGZ2;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=PHLCEN_2v12510 {ECO:0000313|EMBL:PSR71657.1};
OS   Hermanssonia centrifuga.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Meruliaceae; Hermanssonia.
OX   NCBI_TaxID=98765 {ECO:0000313|EMBL:PSR71657.1, ECO:0000313|Proteomes:UP000186601};
RN   [1] {ECO:0000313|EMBL:PSR71657.1, ECO:0000313|Proteomes:UP000186601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC195 {ECO:0000313|EMBL:PSR71657.1,
RC   ECO:0000313|Proteomes:UP000186601};
RA   Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA   Riley R.;
RT   "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT   centrifuga.";
RL   Submitted (FEB-2018) 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:PSR71657.1}.
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DR   EMBL; MLYV02001259; PSR71657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R6NGZ2; -.
DR   STRING; 98765.A0A2R6NGZ2; -.
DR   Proteomes; UP000186601; 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   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:UP000186601}.
FT   DOMAIN          407..489
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   979 AA;  109785 MW;  62DBF2CF4CE3BE6D CRC64;
     MIYDKDGTPL QGITGGYGGD RRVDFIIPHS AVKKGKYEFV IESSCNGMFG VPWDGDTISP
     PDMNRYFGLS SADLCVPNQE AWGLLLDFTT LREISESLPG NTSLQNKALT VANEIMNVFD
     NNDLTSIGRA RKTAQGVFGE GWEKKQEKIY QEGVKQPKVW GIGYCHIDTA WLWPYSVTQQ
     KVARSWSTQV DLMERYPEHR FTCSQAQQFK WLEELYPRLF DRVKEKVKEG KFHLVGGAWV
     ENDANMPSGE ALARQFLYGQ RYFESRFGKR CDTAWLPDSF GLTGALPQLI RLADMKYFFT
     QKLSCNVFPH STFNWIGIDG SQVLCHMTPN LESSDVSLLV FGNGDGGGGP LSKMLENLRR
     IRAAGNESRE LPPVDMGHSV EDFFDTVLKD TIGGTKLPNW NGELYLEFHR GTYTSHGSIK
     KGNRKSEILL RDVEHIATLA SLYRYHKHDY VYPKSKIDVC WEKVLLNQFH DVLPGSAIGM
     VYDDAEKLYA EVRKDGEYLL EEAFGALFPK SLPLTSATVK APGNIVAFNT TPFPRRDVVQ
     VPLSPQMRSK VVQGSKDGLT GFALFDCSKG ENLAHPTGFF ADCMPVSVFT NNSDHFVLRN
     SSVQLTVSKG RITSLIDVQL ERELITKGNT GGLVIFDDRP NYWDAWDVEI HHLETAHQLE
     FTDISVVADG PLRASIRSVI KYGKSNITVT ISLDAIAATV KSNSRSLFIF DAIVDWHERH
     EFLKFELPLD IHNDNATYET QFGHVQRPTH KNTTWDMAKF EVCGHKFADL SEFGYGVAIL
     SESKYGYSCR GNVLRISLLR AATAPDADQD QGMHTFSWAV MPHQGSFLES DVPVAAYLFN
     SPLHVRSIPQ ENVQYPLLQA RAPFVVEGAP NIILETVKRG EDDDHKSGPT TVVLRLYEAF
     GGHVKANLRV ASHIPVSKAC ITNLLEDETK QLRLFSGHED TTSLKLDFHG FEVKTVKLWI
     GPPSTAGVGR YAYHTSRCS
//
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