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
//