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Database: UniProt
Entry: A0A094CSN7_9PEZI
LinkDB: A0A094CSN7_9PEZI
Original site: A0A094CSN7_9PEZI 
ID   A0A094CSN7_9PEZI        Unreviewed;       909 AA.
AC   A0A094CSN7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN   ORFNames=V493_04582 {ECO:0000313|EMBL:KFY25567.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY25567.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY25567.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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   -!- 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:KFY25567.1}.
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DR   EMBL; JPJV01001791; KFY25567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CSN7; -.
DR   STRING; 1420906.A0A094CSN7; -.
DR   HOGENOM; CLU_319610_0_0_1; -.
DR   OrthoDB; 2874448at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR005595; TRAP_alpha.
DR   PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR   PANTHER; PTHR11113:SF14; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF03896; TRAP_alpha; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029327};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        805..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          187..402
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          105..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   909 AA;  96444 MW;  FFC81A3FB5312CB4 CRC64;
     MPSSTNARAP RDIITRFTNC RLLRHNSLVQ EDLWVSSLTG KILDGQDVFY TEKRLPDVVV
     DLGNRILSPG MIDVQLNGAF GINFSDVPEE EGSFPKKLQE LLPHLGPSGS ARDSTNGSES
     LGAHIEGPFL SPSKNGIHNT EVLISAPNGF SDLIACYGSD NLNNAKMLTA APEEGVQQAI
     PDIISRGIVY SIGHSEATYE QASAAVAAGA TMITHLFNAM RPLHHRDPGI FGVLGCTDVT
     APQTTLRTSR SASNSSASSS SSSSGSSSGS STDFRPFFGL IVDGLHLHPT TVKIAWSAHP
     DGCILVTDAM HLVGLPDGMY TWGSSGRERI VKTGPRLTLE GSDKLAGSAI SLVECVNNFL
     AWTGASVPLA LKTVTETPAR VLGMEGVKGS LVVGADADLV VMSEVGGELG GYSPATRLPA
     GPMARRLTTN QEIAGSIPAH PSISGPPAGP YVKLITSSSL SRWTLYQKPQ NRKCFAQTIA
     WNSASYAVGS GPGVINIPGA MSSALSQHEL ASTLSSSYTV YLFSRRCRGL SGPYPSSVTK
     AKTPILRPPG PTDDNTLDPP YDAQFCLGIL KTDLIDLFAP NAAHTRDVSP SAQLVVDTLH
     HSRIKPHHLQ LHVSSPISRN IIVMVSYRFS VLALLALRTI GAVAAKASPE DAAKEGTTPA
     TEDAPPFDVS VTATFPSAEI FGPKIINGQG THALLDITNN EGAPITLVMV GGMLSRPETD
     LKPGAHASSL IVKNLTTTKY TVEVPAGAKE SLPFTFTTDM QPADLQLSLM AIFTDNKGNV
     RQVPAFHDTV SVVEAPTSFL DPQIVFLYLV LAAATAGTLY FVYKTWIETL FPQTKRGGKG
     GERARRSVAG TKKAVPTDEQ LSVIGADGPA VTTKDLAQKA YDESWIPNHH INRPSARKVQ
     SSSKKVPTK
//
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