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
//