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Database: UniProt
Entry: A0A094D8T4_9PEZI
LinkDB: A0A094D8T4_9PEZI
Original site: A0A094D8T4_9PEZI 
ID   A0A094D8T4_9PEZI        Unreviewed;      2077 AA.
AC   A0A094D8T4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN   ORFNames=V497_06670 {ECO:0000313|EMBL:KFY55855.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY55855.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY55855.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
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:KFY55855.1}.
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DR   EMBL; JPJZ01001133; KFY55855.1; -; Genomic_DNA.
DR   STRING; 1420910.A0A094D8T4; -.
DR   HOGENOM; CLU_001285_1_0_1; -.
DR   OrthoDB; 8838at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProt.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd16448; RING-H2; 1.
DR   Gene3D; 1.50.10.10; -; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR036026; Seven-hairpin_glycosidases.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR11742:SF6; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE IA-RELATED; 1.
DR   PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SMART; SM00299; CLH; 1.
DR   SUPFAM; SSF48225; Seven-hairpin glycosidases; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601382-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU361193};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361193};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268}.
FT   REPEAT          912..1072
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1327..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1900..1963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1838..1867
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..55
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1340..1369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1903..1928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1501
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        1676
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        1795
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        1997
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   DISULFID        1752..1781
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-3"
SQ   SEQUENCE   2077 AA;  230051 MW;  E4EC5612EF443B7E CRC64;
     MAADSGERGE INEDIPPDSQ SHDPDTMDEN DENETETNGS DEDEDEDEDD EEEEDEPKLK
     NARMTGYMTQ LYRNGDATSC FLVAGDKMYI GTHNGNIHVL SLPSFQSLRV YHAHSASISS
     ISISPFPPPT SDPRSEAVNR AVSQAINESQ KAASVASATS SPAAQRAPRQ QVIPNIPSNA
     IYIATSSIDG NVCIASLIDI KDVQLRNFAR PVQAVALSPD YKNDRTYISG GTAGNLVVTV
     GGRSGTNATS TTTGTAAATA SGWLGTIGLG GNSGKDTVLH SGEGIISTIK WSLSGKYVVW
     VNEKGIKIMR SNIGLESADL DSAWKRIAHV DRPQESGWEE MAAVWKARAE WIDESSLGTD
     DDSTSTGATS PIVTKLRQQA TTNKDPIEKL VVGWGSTIWI LHVHPGGVGV GKHAGERTVG
     RAEIIKILRM DCIISGLSLY TPTLLLVLAY INPDDENADE APSPKGHKSK LSNASTGSEP
     RGGIQRRQNA VPPELRLIEL STSEEIDTDG LIVSRFERLS AADYHLCVLP AAKESATTRT
     SRTTLETLAG MGSGMWNATI NATTLLSSAQ SIRSVGSGDS ASQTGSLSSR NKSVNRPQQA
     AHPNIAAPGI KIFIHSPYDC ILATKRDLSD HLSWLLEWHK YEDAWNLLDE HPEIISSSAE
     KLAEIGPGTP ERHDAGDFYD DASSVKETAA RLIDSSVEKE KRRIGELWIQ QLITDGDWIA
     AGQVCGKVLG SSSRWEHWVW IFAGANKFGE IANYIPTTQL QPPLPPTIYE VVLGHYIATD
     RLRLKELLDV WPPELFGIRT VSTALENQLK YREVREDSVE DGETGRDWRI VKECLGKLYL
     ADGRPKDALK CYMQLQDADT AMALIKDYHL IDAVADDIPG LVLIRVSKEQ MKSAPRKELE
     ETTADVITLL VDEAQRGLVR PESVITQLQD KDMPLYLFFY IRALWNGDSQ DEKSAEARER
     MLVESRAHVE QFADVAVQAF ASYDRALLME FLKSSTSYTF EKAIHVCDER DYIPELVYLY
     SKTGQTKRAL FLIIDRLADV SQAIGFAKEQ ADKDLWEDLL DYSMDKPRFI RGLLEEVGTA
     IDPITLVRRI PEGLEIDGLR DGLSRMIKEY EIQHSISSGV ARVLRGEVAT AQNTLRSGQR
     KGVKFDVVVK SEDHIDVAAN DVAPVAADND DKADDNAAAV RARKPILPGH CVGCGEPFTE
     GEQETLVGFA CGHVFHLSHL LAYTHPSRPS TPPSMDLDED GQFVQNHSIG AKVTHASHYW
     HWHWAVPCRQ GPHPTRPSAR PDSPSRPTRT EGTMLRFRKY RVFLIFAAIL VITLYNFWEP
     GPGSSFGNSH ASGDGKSAQN GDRDGAKKKK KPVDIQGIAH PEDSDDSKTI HWRKPTEYYP
     VAAEDLIHLP SGTPKKMPRI QFEFPVESAE AKKIRVERRD KVKAEFLHAW KGYKKHAWGH
     DEVGPVNGGS RDPFCGWAAT MVDSLDTLWI MGLKDEFEEA LKSVKKIDFT TSPKSSIPVF
     ETTIRYLGGL LAAYDISEEK YPILLTKATE LGEILMSIFD TPNRMPVLHY GWQPHSANER
     HRAAGNSNFA ELGTLCLEFT RLAQLTGEDK YYDAVARITN ALVEWQEAGT VEIKGIFPDS
     VDASGCNSTF VPEDEEPAEN ATEKALGARD AEAFCRPQGL TKGPSRESYS MGGGQDSTYE
     YFSKMWLLLG GLDTTYRTLY LNTMHAIRTH LLYRPLIPGG RDVLFTSKMQ INPYLAGDSN
     RETIYEVTHL SCFIGGMVGM GAKLFGLDSD LPIAERLSDG CVWAYESTRS GVMPEDARAV
     PCENPLDCEW SEERYYKYLD PRWALRPGEI EKYDAEKVRQ EEERVAKARI EKAREEEEKK
     EKVLLDEAYG VTRRSEGGAT KYSLDGTAVE SSEHDVEAID ANNPSPVNIN HKRPFSNSTS
     TATTSDDDAL PTLPPYVAPT KTENVPINPH ARGLPKDRSD PYRPLTHEEY ISDFMGRNTL
     PLGFAKVESD KYILRPEAIE SVFYMHRITG SPTWPEKGWK MFTSIIAATR TEIGHSAVIG
     VNREPAKTHK QDSMESFWLA ETLKYFYLLY SEPELTA
//
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