ID   B8MLN8_TALSN            Unreviewed;       876 AA.
AC   B8MLN8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=TSTA_101410 {ECO:0000313|EMBL:EED13901.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED13901.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; EQ962658; EED13901.1; -; Genomic_DNA.
DR   RefSeq; XP_002486139.1; XM_002486094.1.
DR   AlphaFoldDB; B8MLN8; -.
DR   STRING; 441959.B8MLN8; -.
DR   GeneID; 8101829; -.
DR   VEuPathDB; FungiDB:TSTA_101410; -.
DR   eggNOG; KOG4342; Eukaryota.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   InParanoid; B8MLN8; -.
DR   OMA; DVFGFSW; -.
DR   OrthoDB; 2786490at2759; -.
DR   PhylomeDB; B8MLN8; -.
DR   Proteomes; UP000001745; 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:UP000001745}.
FT   DOMAIN          392..471
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   876 AA;  99022 MW;  10BAA1571689B2C4 CRC64;
     MACNGMFGNG PGRPIFKNNA GGDSIQPPDP KKYFQLSKAE IVVVNWEARM LYMDIVAIHD
     SALELPDDSW QQHKALNIAM KIINTFRPGN KDSITKCRTI AADFLGPDVG SYEIYHNATE
     VDIFAIGHCH IDTCWLWPWA ETKRKVVRSW LNQCDLMDRY PELKFACSQA QQFKWLKEEY
     PIAWKRVKEK VKEGQFHPIG GCWVEHYTNM PSGESLVRQF LYGQRFFESN FGYRSKTLWL
     PDTFGFAAQL PQLSRQAGMN RFLTQKICFN NINEFHHTTF NWIALDGSQV ISHMPPVRTY
     TAEGTVADVK RSIAKHLSLD QDHTALMAFG KGDGGGGPTW QHMERLRRCR RIADEVGILP
     RVHVGKSVDD FFDGLEKKAG SLVTWFGELY FELHRGTYTT QANTKRNNRR AEFLLRDIEL
     LATVASISDR SYKYPKREID GMWEAVLLCQ FHDCLPGTSI RMCYDDSDKV YENVFATGTA
     LLNAVYRSLD IVEVAEKGDL KKQNMIALNT LPWPRMEIVE LSDTETAVAS GEGIILALEQ
     FTGAEVEARV TIKETSKGVY KMQNSQLSVT VQNGCIISLY DRIADREIIP EGSKANHVVT
     EIKIDEISSI KSIISLTAAL EGQQSVVECS AEVDWHETMR FLKVEFPVNI RNTEASYEAQ
     YGVIKRPTHY NTSWDMAKFE VCCHKFADLS EHGYGVSILN DSKYGFSTVG NVMRLSLLRS
     PKAPDDTADM GRHQIRWAIM PHRGGLSAET VRAAYAFNSP LKFLSCSRLK DCTLTQSPIR
     LTGDQSLILD TIKRGEIDED VSRGDLPSHK GRSVIIRIYE SLGGRARGRV ETSWPVSKVC
     KTNLLEDDEE AVVCENGNFK VDLGAFQVAT YRICLA
//