ID A0A366SE10_9HYPO Unreviewed; 1426 AA.
AC A0A366SE10;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN ORFNames=FIESC28_00021 {ECO:0000313|EMBL:RBR27158.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR27158.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR27158.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR27158.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC {ECO:0000256|ARBA:ARBA00007658, ECO:0000256|RuleBase:RU361193}.
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:RBR27158.1}.
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DR EMBL; QKXC01000001; RBR27158.1; -; Genomic_DNA.
DR OrthoDB; 25313at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000253153; Unassembled WGS sequence.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016482; P:cytosolic transport; IEA:UniProt.
DR GO; GO:0016197; P:endosomal transport; IEA:UniProt.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProt.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.1230; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR008153; GAE_dom.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1.
DR PANTHER; PTHR22780:SF5; AP-1 COMPLEX SUBUNIT GAMMA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
DR PROSITE; PS50180; GAE; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601382-3};
KW Glycosidase {ECO:0000256|RuleBase:RU361193};
KW Hydrolase {ECO:0000256|RuleBase:RU361193};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1315..1426
FT /note="GAE"
FT /evidence="ECO:0000259|PROSITE:PS50180"
FT REGION 1201..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 317
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 436
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 514
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT DISULFID 393..422
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-3"
SQ SEQUENCE 1426 AA; 158322 MW; 656B2FDA4351C64C CRC64;
MAGPLRRGRL WAGVVFIWIF CFWYWSSSDS AFSLFGNNDP LAGKGANAWT RRLPKYPIPQ
EKLAVLPEIK GDVKVPKIQA NAPVESAAAK ELRLTRLAAV KKSFEHSWSG YSNYAWMHDE
VTPLTGKSKD PFGGWAATLV DALDTLWIMD MKEEFTKAVA AADGIDFTRS HMTTINIFET
TIRYLGGFLS AYELSGKSHP ILLKKAIELG DLLMVAFDTP NHIPITRLEW KKAAYGQSQS
ASRETLVSEL GSMSLELTKL SQITGNMKYY DAVKRLGDQF ESTQLNTRLP GMWPVVVDAY
TPAFHAGSEF TLGGMSDSLY EYLPKWYLLL GGQLEQPRRL YENFIPVAIK HLFKRALTPS
EKPIIISGDY QVTDLPGQQP KYTSVARGQH LTCFAGGMMA MASKIFNRPA DLDIATQLTD
GCIWAYQATQ SGLGPEVFSF ISCGSVDVKE TGDCTWNEER WLKAIEEQHA PDFKAPPMKG
PEWKQPTVQD VVKKHNLPKG MIDVGDPRYI LRPEAIESIF IMYRTTGDAQ WMEKAWTMFE
TIEKVTRTEI AASAIDDVTK AEPTKMDSME SFWLAETLKY FYLIFSEFDV ISLDQDLLFI
FFRIVKQFIR NVRAAKTIAD ERAVIQKESA AIRASFREES HDPNVRRNNV AKLLYLFTLG
ERTHFGQIEC LKLLASPRFA DKRLGHLATS LLLDENQEVL TLVTNSLKND LGHSNQYVVG
LALCTLGNIA SIEMSRDLFP EIETLVATAN PYIRRKAALC AMRICRKVPD LQEHFVDKAT
QLLSDRNHGV LLCGLTLVTS LCEADEEEGG EEGIVEKFRS FVPGLVRTLK GLATSGYAPE
HDVTGITDPF LQVKILHLLR VLAVGDAETS EQINDILAQV ATNTESSKNV GNSILYEAVR
TILDIEADSG LRVLGVNILG KFLTNRDNNI RYVALNTLIK VVAIEPNAVQ RHRNTILECL
RDPDISIRRR ALDLSFTLIN ESNVRVLIRE LLAFLEVADN EFKPTMTSQI GIAADKFSPN
KRWHFDTMLR VLSLAGNYVK EQILSSFVRL VATTPELQTY AVQKLYINLK KDITQESLTQ
AGAWCIGEYA DALLKGGQYE EEELVQEVKE HEVVDLFSLI LNSAYATQVS TEYIVTALMK
LTTRFSDPAQ IEKIRRLLQY HQTSLDIEIQ QRVVEYGNLF SFDQVRRGVL EKMPIPQIKE
ESRVLGSAPT KKKAANRKSR VIKPTEQDLL DIMDAPAATP AASSTTNTDL LADILGGTSS
PPPSATSPPP QSNMSSIMDM FGSAPGSSTA SPAPPSSNFD LMSGGAAAPQ PQAPQAPAGI
PCYDSNDLNV TFQIQRNAEG MIQATAKFVN TSGSATLSNV SLQAAVPKSQ KLQLLSISSS
DLGPGAEASQ MMRVSGCKGP LRLRLRIGYT HPTAGQVMDQ VNWTES
//
