ID A0A225B9T4_9EURO Unreviewed; 1529 AA.
AC A0A225B9T4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=UA08_00643 {ECO:0000313|EMBL:OKL63705.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL63705.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL63705.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL63705.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) 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:OKL63705.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFMY01000001; OKL63705.1; -; Genomic_DNA.
DR RefSeq; XP_020123826.1; XM_020260472.1.
DR STRING; 1441469.A0A225B9T4; -.
DR GeneID; 31000398; -.
DR OrthoDB; 1331861at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000214365; 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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProt.
DR Gene3D; 1.50.10.10; -; 3.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR InterPro; IPR018556; SPIN90/Ldb17_LRD.
DR PANTHER; PTHR11742:SF104; ENDOPLASMIC RETICULUM MANNOSIDASE MNL2-RELATED; 1.
DR PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR Pfam; PF09431; SPIN90_LRD; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE 3: Inferred from homology;
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:UP000214365}.
FT DOMAIN 1093..1235
FT /note="SPIN90/Ldb17 leucine-rich"
FT /evidence="ECO:0000259|Pfam:PF09431"
FT REGION 36..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 527
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 650
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 816
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT DISULFID 607..636
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-3"
SQ SEQUENCE 1529 AA; 171387 MW; 906A015CE1377BC5 CRC64;
MPRSRRYRSF VVFSIIFGLA FVHFLRSREW SDDWPGTKDL QAPPTAINHD SPVSPPEPAT
EIKFKSGPAG ERPSAPEELP LKNKELPKDR ETGKQKELVD DETWSTETTY SPTDYSDALD
PPSVEESSLK IFGDKPQSEV TEQSGTKKQS DRVGTSNQLP TNTIKQHWEK LPEHFPVNEY
DLIKLPTGRP TSLPKLQSTF KDESNTEKLL RTQRLAAIRE EFEHAWDGYT EYALGHDEIR
PVTGQYRDPF AGWGATLVDA LDTLWIMDLK DEFAAAVEEV RKIDFTTSIR RDIPLFETVI
RYLGGLLGAY DISGQKYSVL LDKAVELAEI LMGAFDTPNR MPVTYYNWAP AAVAQPHRAG
TRVVLAELGS LSMEFTRLAQ LTMEHKYYDA IARITDELEK MQNNTRLPGM WPLVVDASGC
APLSSSSLEH PTRTEKSGVV INKSSGLGIA KSSPTMVLEK HLPIPKDMEK RDPGLESDAE
PADYETGTKA TTPLTSIPAS KQDCTKQGLA SPPRTAFDRF GLGGQSDSTY EYLPKEHMLL
GGLSDQYRSL YEISMEPVRD NLIYRPMLPD EERDIRFVAT VQVSDNLKDG TGEKNTKYTY
EGTHLTCFAG GMFAVGAKLF GLEGDMNIAA KLTDGCVWAY ESTNTGIMPE GFEILPCDDP
LACPWNATRY MDTMDPHEKS RIIQAEKSYE RQLLRAKEAY YGISHETQPS QEKKPNIVSP
VRNSVVEESD TIAKRDINPR GLDDYDEHAH LSTSNSKVVQ EEASKLLPDV DDPNFVAPPK
PTVLSHEDYV AARLQEERIP LGYTKIQSRK YILRPEAIES VFIMYRLTGD NIWREKGWKM
FEAIARHCRT ELADSAISDV TSKAPELLDE MESFWLAETL KYFYLLFSDP SVVSLDEYVL
IGPAGTRRDE CAIKWSGFVV VMQDMDLEEV SYDLEDEKQF WAELEEIVSK QCDSHALIDN
ALRTYLDFGA KFKGEFLVSE YDISCCSYKL FSSSLFAQHA DYIRRQIIYS LLQNDGTFQL
MNEEGCFPKL LELIRSPGIN LDNGAGLHRL LMDLLYEMSR IQKIKIEDLF CVDDDFVKYL
FEIIEGVSDD AHDPYHYPVI RVLLVLNEQF MVSAHDPASG LSSSPLTNKV MKVLSVHGNI
YKTFGENIIL LLNREGETSL QLLTLKLLYL IFTTPSTYEY FYTNDLRVLV DILIRNLLDL
PGEAIALRHT YLRVLYPLLA HTQLKNPPHY KCDEIRKTLS ILVHSQIEGS DSVCERIMHF
AEADETTKRL VSRCSQVEWL RDAGPQLHGT AELQLSEEVM AISISSGMPP ATLSESPISQ
DSDATTSPTR PESEPPSAFS SGDEKSTETL GVHLGSATSS KLSMLEVARQ SEIPGIVTPS
LKNKASQQPI VSVGKVRPRP QPPNPRRTYP KPHGKGDHDD GRGRPADRTE TAPISTDSPG
PVGTILQAPE TSISRSTSRP RPAVPPPRRS QHPSSTTKSS TKPEPPKTRR WRHGPKPSTE
PPLDEGVDET ASSPSPQRSS GDSYTINDT
//
