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Database: UniProt
Entry: A0A395N1W6_9HYPO
LinkDB: A0A395N1W6_9HYPO
Original site: A0A395N1W6_9HYPO 
ID   A0A395N1W6_9HYPO        Unreviewed;      1426 AA.
AC   A0A395N1W6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN   ORFNames=FIE12Z_1597 {ECO:0000313|EMBL:RFN54108.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN54108.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN54108.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN54108.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN54108.1}.
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DR   EMBL; PXXK01000030; RFN54108.1; -; Genomic_DNA.
DR   STRING; 2594813.A0A395N1W6; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000265631; 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   Reference proteome {ECO:0000313|Proteomes:UP000265631};
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..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1310
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;  158321 MW;  C56D64C0BF13A591 CRC64;
     MAGPLRRGRL WAGVIFIWIF CFWYWSSSDS TFSLFGNSDP LAGKGASAWT RRLPKYPIPQ
     EKLAVLPEIK GDVKVPKIQA TAPVESAAAK ELRLSRLAAV 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
     GCIWAYKATQ TGLGPEVFSF ISCGSVDVKE TGDCTWSEER WLKAIEEQHA PDFKAPPMKG
     PEWKQPTVQD VVKKHNLPKG MIDVSDPRYI LRPEAIESIF IMYRTTGDAQ WMEKAWSMFE
     TIEKVTRTEI AASAIDDVTK AEPTKMDSME SFWLAETLKY FYLIFSEFDV ISLDQDLLFL
     FLRIVKQFIR NVRAAKTIAD ERAVIQKESA AIRASFREES HDPNVRRNNV AKLLYLFTLG
     ERTHFGQIEC LKLLASPRFA DKRLGHLATS LLLDENQEVL TLVTNSLKND LGHSNQYVVG
     LALCTLGNIA SIEMSRDLFP EIETLVATAN PYIRRKAALC AMRICRKVPD LQEHFIEKAT
     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 IEKIRRILQY HQTSLDIEIQ QRVVEYGNLF SFDQVRRGVL EKMPIPQIKE
     ESRVLGSAPT KKKASNRKSR VIKPTEQDLL DIMDAPAATP AAPSTTNTDL LADILGGTSS
     PPPSAASPPP QSNMSSIMDM FGSAPGSSTA SPAPPSSNFD LMSSGAAAPQ PQAPQAPAGI
     PCYNSNDLNV TFQIQRNAEG MIQATAKFIN TSGSATLSNV SLQAAVPKSQ KLQLLSISSS
     DLGPGAEASQ MMRVSGCKGP LRLRLRIGYT HPTAGQVMDQ VNWTES
//
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