ID   A0A1X2GIZ1_9FUNG        Unreviewed;      1046 AA.
AC   A0A1X2GIZ1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=DM01DRAFT_1286538 {ECO:0000313|EMBL:ORX54951.1};
OS   Hesseltinella vesiculosa.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX   NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX54951.1, ECO:0000313|Proteomes:UP000242146};
RN   [1] {ECO:0000313|EMBL:ORX54951.1, ECO:0000313|Proteomes:UP000242146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX54951.1,
RC   ECO:0000313|Proteomes:UP000242146};
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:ORX54951.1}.
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DR   EMBL; MCGT01000012; ORX54951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2GIZ1; -.
DR   STRING; 101127.A0A1X2GIZ1; -.
DR   OrthoDB; 2786490at2759; -.
DR   Proteomes; UP000242146; 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; cd10789; GH38N_AMII_ER_cytosolic; 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:UP000242146}.
FT   DOMAIN          506..589
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1046 AA;  118110 MW;  BE6E9B5CC4F33466 CRC64;
     MVLHESIDAA PKVPDNITRS RISNFLATSG QFHAMGIHHG LWTHRHSGHP HVCLAVHSVP
     DMKEAIVQPF EAIEQLERSF GPSWSTHWFK VDICIPDDMA DKPVTFLWNM ENEGLIWSSD
     GEPLQGLTGG DGQERHAYIL TNKANKGDTF SFYIEAACNG MFGVGANDAM VPDPNRTFRI
     KVADLVVPNE PVQRLYHDLS VINGIAYDTV NGSARARKAI WVLNQVINCF SLESKDIDSC
     LALTRAFLSQ TNGTGQHQVT AVGNCHIDTA WLWPYDETKR KVARSWASQL NLLERYPSYV
     FTGSQVQQYE WLKELYPTLF DKIKEQEKQG RWEIIGGSWV EHGDGESLCR QMLLGQRFYE
     QHFGKRTNLP QVLKQSGCDY FFTQKLSWNN INKFPLTTFW WTGIDNSSIL THLTPADTYN
     AEVRPSELQK CVNNHHDLEA SNQSLLVFGH GDGGGGPTPE HLERLVRLTD VDGVPVCKPG
     RVDDFFAQVA STSEKLQSYK GELYLEFHRG TYTTQALVKR GNRQCEVLIR DAEFLATAAR
     LLAKDRPTSY SYPTEDIQRL WKLICLNQFH DCLPGSSIGL AFVDVHAFHR EVIYESLTLR
     RKAQDYILFN EEAQVLGHKH KNGLAVFNTL PWPRTDVIAL PQKNTCWLGQ QTNDDNEYIV
     VDHVPGFSVS GITSNSLKKS KEDAKAYQRS DGQFVLENGN LQAVFNGSGQ LVELHDKHTT
     ERGNLVKNGC KGNMLQLYED VPTYWDAWDV EIYHLQKFKV LEGGNGVKIT ASGPLRAELQ
     FRQAISDASW LEQTISLTSV GSIIEFDTNV EWHESHQFLK TEFNWNLISD FATYDIQHGV
     LRRPNHYNTT NDSAKFEVCG HKFADLSDAT YGVALINNCK YGYATHGTSQ RLSLLRSPKG
     PDENADMGQH QFKYAIYPHR GDYTSSDVVR KALEFNVPLS VRQTTHLPKS QMIVPPLFTL
     DPPDRVILDT IKLAEDDNGS GNTVVLRLYE AYGGQCTVHI HSSLEISNVQ ISNVLEDDLE
     VVPGFAKHKF ILTLTPFQIM TLKLTL
//