ID A0A094F4K7_9PEZI Unreviewed; 1028 AA.
AC A0A094F4K7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY85886.1};
GN ORFNames=V498_07634 {ECO:0000313|EMBL:KFY85886.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY85886.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY85886.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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 -!- FUNCTION: Is probably involved in a pathway contributing to genomic
CC integrity. {ECO:0000256|ARBA:ARBA00037565}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}.
CC -!- SIMILARITY: Belongs to the IRC22 family.
CC {ECO:0000256|ARBA:ARBA00038311}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:KFY85886.1}.
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DR EMBL; JPKA01002166; KFY85886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094F4K7; -.
DR HOGENOM; CLU_000631_10_0_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06593; GH31_xylosidase_YicI; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR005595; TRAP_alpha.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR PANTHER; PTHR43053:SF4; MYOGENESIS-REGULATING GLYCOSIDASE; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR Pfam; PF03896; TRAP_alpha; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1028
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001901892"
FT DOMAIN 343..521
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 568..885
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 902..982
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
SQ SEQUENCE 1028 AA; 112698 MW; 291ECBA9558995C1 CRC64;
MVSYRFSVLA LLALRTIGAV AAKASPEEAA KEGITPAPED APPFDVSVTA SFPSAEIFGP
KIINGQGTHA LLDITNNEGA PITLVMVGGM LSRPETDLKP GAHASSLIVR NLTTTKYTVE
VPAGAKESLP YTFTTDMQPA DLQLSLMAIF TDNKGNLRQV PAFHDTVSVV EAPTSFLDPQ
IVFLYLVLAA ATAGTLYFVY KTWIETLFPQ TKRGGKGGER ARRSLGGVKK AVPTEEQLSV
IGADGPAVTT KDLAQKAYDE SWIPNHHINR PSARKVQSSS KKIPTNTMKF RDGMWLVAEG
TTIEYAEQVY SITEREDKKA LSLLCPTRRI SNRGDVLNRS TLTIDIEAVS DGIISVESTH
WAGAVRKGPN FELFPNGAPE VEATITTASE RTVLSAGALT ATVAGAAQPF RIDFKGANGR
VLTDLRERSV GLAYNPPISN MLQTGDMRNI KHHVFTQTTL GVGESVHGLG ERFGPFNKVG
QAVSLWNADG GTSSDQAYKN VSFWMSSRGY GVFIDTPERV ELEIGSERCC RLQTSVEGQR
LKWFIIDGPT PKDVLRRYAK LTGQASSVPE WSYGLWLSTS FTTDYDEQTV TAFLEGMKKA
AIPVDVFHFD CFWLKAFQWC DFAFDKEKFP DPAGQIKRMK ESGLCKKVSV WTNPYLGQAS
PLFAEAAANG YLLKRKNGDV FQWDLWQAGM AIVDFTNPAA ATWFQGLITS LLDLGIDSIK
TDFGERIPST DVQWHDGSDP GRMHNYYAVL YNEVVYSAMN ARFGPGESVL FARAAAAGSQ
RFPLQWGGDC ESTPEAMAES LRGGLGFGLS GFAFWSVDIG GFEGNPPPWL YKRWVAFGLL
CSHSRLHGSD SVRVPWAIDN DDQSDEGATA VLRTFVQLKD KLGVYIQAEA AKSVRDGLPL
SLRAMCVEFP EDPTSWTLDR QFMLGESVLV APVFEEDGSV EFYLPEGRWT AFVSGEVKEG
PRWIKEVHRF DSVPLYVRER TVLPLRAEGG EVSLKVYGIK AGEVAKVQEI VEGALKEREV
TVAEDMLA
//