ID A0A1Y1W6B5_9FUNG Unreviewed; 1050 AA.
AC A0A1Y1W6B5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=DL89DRAFT_275108 {ECO:0000313|EMBL:ORX69069.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX69069.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX69069.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX69069.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORX69069.1}.
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DR EMBL; MCFD01000008; ORX69069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1W6B5; -.
DR STRING; 61395.A0A1Y1W6B5; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000193922; 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; 2.60.40.2220; -; 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; 2.
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:UP000193922}.
FT DOMAIN 508..588
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1050 AA; 118769 MW; 3F58616139958670 CRC64;
MFIPKSSNFV VHSAVVYGHK HRSITNSRVN NFLDDGQWKD VNIQAVLYDL RVSGSPHINL
EVWSAPGQDR PTFEHAVKQK FRPTHQGESF GPSWTTHWFH VTVQIPKEFA GKPVQFLFDS
NSEAMIWSAD GEPLQGITGG GGDERHVDYL LTRKATDNEG IREFYVEMAA NDLFGNGDYH
QHPQDRAIYY NLSTVELVAP NLDAWALYHD LEVIVEMAGR LPQDSARSWQ ALKAANAMVN
VFDHRNIDTI APAREIAEQF FSVNGAHTRH QVYAIGNCHI DTAWLWPFAE TKRKSARSWA
TQLQLMDQYP EYKFAASQAQ QFEWLKQNYP GLFARIQDKA KSGQFIPIGA TWVEMDCNLP
SGESLARQFL LGQQFYQEHF DETCKVFWLP DTFGYSSQLP QIYFFTQKLS WNNINRFPNT
TFRHCRPGEL IDSEHNHKDI VYTNESMLLY GNGDGGGGPL KAMLERLRRM ADTDGLPRVK
NAHPNEFYEH VEKTATELVS WKGELYFELH RGTYTSQSNN KRNNRQAEFL MRDVELLNTV
AKASSFGLYD YPMEAIRKLW KQVCLNQFHD VLPGSAIGMV YRDSDKIYNE IFTIGDALRK
RATDFLYGDV VAKAPEDMSA VLLVNTAAWM RTDIIAVPEL PLSLLSKAGA NVQIRRKDGA
PLVLATNVCG NRAQLLDPAQ TTEFHSSPVK VYQEGDDFVL ENTMVKVTIG HNGRVKSFID
IREDRELVPE GAQGNVFELY DDVPLYWDAW DIEIYNLEKY QSLPGTDITM VDKGPLVASL
IVRVPIGDTS VLVQTITLTA ISPRLEFDCH IGWHENRKCL KVSFTWDIHS DVATYETQFG
VVQRPTHRNT SWDMAKFEVC GHKFADLSEY GYGVALLNDC KYGYSTLENT MTLTLLRSPK
APDENCDMGP HVFRYAVFPH KGTFAESTVV KEAYNFNVPL LHLPANADRF SMKGGMAGAA
HPYFSLSNAP NVVLDTVKAA EDGSSSFVVR MYEAYGGHAK ALLTTALPAM KAEIVNILEG
HVSDLEWLPH SKSTAIKFKP FEIVTVKFSI
//
