ID A0A109FE01_9BASI Unreviewed; 1157 AA.
AC A0A109FE01;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=RHOSPDRAFT_35927 {ECO:0000313|EMBL:KWU42572.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU42572.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU42572.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU42572.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; KQ954505; KWU42572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FE01; -.
DR STRING; 1305733.A0A109FE01; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000062823; 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:0000313|EMBL:KWU42572.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT DOMAIN 576..661
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1157 AA; 129920 MW; 706ACF6F4859135A CRC64;
MAATAHSAKM AYPMLNETGP RAQHFRGLTL GRLDSFEGGN YPNIRNVLFE HRIDDKKHIQ
LEYWSCPGRE KVPFKDAVRK PFKPAAKGLR LGPSWTNHWF RVTMNLPAEW ADVERVQLEF
DPSCEAMIFD TEGCPLQGIT GGGGIDRRVE FILPKEKRAS GYKYYIEVSC NAMFGNGLFE
TNAPPDMNRF YTASRPLLHA PSSPYLLESA DLVVPRMEAW RLLWDFRVLK DLARSLPERS
PLGVKCFEVA NAIMNVFRYD DLSTIAASRK LAAEVFGGPE WEKEAHKVYG KDPVADRVTS
YAIGNCHIDT AWLWPFSVTR QKSARSWSTQ LDLMERYPEH RFVASQAQQF KWLEQDYPQL
FKKVKAKVAA GQFLPIGGMW VESDQLLPSG ESLARQFLYG QRYFKSRFGQ YCRVFWLPDS
FGYNSASPQI ARLAGLDFFF TQKLSWSQFN DFPHTTFRWQ GQDQTQIVVH MCPQNTYTAQ
ASVDDVLNTW RNHKSLQSTQ TGLLTYGNGD GGGGPLAPML ENLRRCRAVA NNTKIGGGEI
PKVHMGATVE QFYNDLLKQT DKGEKLPVWV SELYLELHRG TATSHGSIKR HNRKTEVLLH
DLELVATLAS LYSSKYDAKK AYSYPKDEID SLWEDMLLCQ FHDVLPGSAI GMVYDDAEKI
YADVQEKGAA LLDSALNVLV PTSKSLSHPE ALDSLVALDT LGLPRRELVK VPMSVARALD
DAALQRSHDG EAYVLFDTTG GTIVTEPVSI NNTSLSRDGS SARARLAGTD HVLSTDKLHV
VISKEGRITS IVDRELDREL ILPNKNAGFV IFQDTPNNWD AWDVDLFHLE TKTDINASSV
RLLEDGPMRS SVLATYHFGK SVVKATISLD ATAPSTKQDA RSLIKFDVQV DWHERHRFLK
WEIPLAITPT GDVCTYENQF GFIQRPTHRN TTWHRAQFEV CGHRFADVSE FGYGVALLND
SKYGHACENS TLRLSLLRAS TLPDDEQDQG AHHFTFAILP HRGSFAESDV PAVARMFNYP
LHLRRLPSIA LTESELMKSR GDDRHGQGPF SVVGARNVVL DTVKRGEEDD FSARSKHETV
ILRLYEAYGG AAKAKIAATI PEGRKIASAE LVDILERKVD NLTVSDKSVS GSASSTFNID
LPRMRAFQIV TVKLMLA
//
