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Database: UniProt
Entry: A0A0D2DBY2_9EURO
LinkDB: A0A0D2DBY2_9EURO
Original site: A0A0D2DBY2_9EURO 
ID   A0A0D2DBY2_9EURO        Unreviewed;      1049 AA.
AC   A0A0D2DBY2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Fumarylacetoacetase-like C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV07_00100 {ECO:0000313|EMBL:KIW33234.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW33234.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW33234.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW33234.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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DR   EMBL; KN847040; KIW33234.1; -; Genomic_DNA.
DR   RefSeq; XP_016253450.1; XM_016386522.1.
DR   AlphaFoldDB; A0A0D2DBY2; -.
DR   STRING; 569365.A0A0D2DBY2; -.
DR   GeneID; 27339294; -.
DR   VEuPathDB; FungiDB:PV07_00100; -.
DR   HOGENOM; CLU_009826_0_0_1; -.
DR   OrthoDB; 1430490at2759; -.
DR   Proteomes; UP000054466; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01299; Met_dep_hydrolase_A; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF115; FUMARYLACETOACETATE HYDROLASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF56529; FAH; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT   DOMAIN          107..449
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          545..756
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
FT   DOMAIN          805..1037
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   1049 AA;  113489 MW;  A1C6C8FF0869614D CRC64;
     MAPGLLANGW HDDVALPPES TQTRYPYENL AFDPKLQPKR YEIAGTSPSS KILFLGVNIL
     DSTGKEPYRG DVYIEGERIV AVGSVPRVEH LQAQPDVRVI QGRGRTLMSG LGDSHTHLTW
     NNNALELLGD VSVEEHVLIT VKSALCYLDS GYTMCYGAAS AKDRLDCVVR DAINRGDIPG
     PRYLANGREI ARRDGELAAG ITAFADGPLE MREVIRHHAR IGVDQIKLSM SGESITETRS
     AEECFFADEE TAALQAHRNG LRVCSHARAR DSVIQCVKHG VDVIYHASYT DDVGMNMLTK
     ARHKHVVAPA INWLYTTVHE AEPFGYTFEK AEQVGYKKEL EVAITALKEM NKRGITVLPG
     GDYGFAWCPH GTYARDLEHF VKLLDFTPME SIIAATAGVA KLFMQEGELG KILPGYYADC
     ILVNGDPLQD IAVLQNHDKL DVIMINGRIH KSSPADFVVV QPAAPSPQPK NPHNFVTFED
     DLGRARVGHL DLETSLVHTL AMPSGSPLSN LQQVIELGHD TIVQTGDSFP LSSVKLLAPI
     TDRDIVCVGN NYADHVKEYR ESGYDVQKIQ QKASFPTIFT KRSTSVIAAN EDIYAHPGFT
     GCLDYEGEVG VIIGKPGFGI SEKDAMEHVW GYTIINDVTA REKQRDHGQF LMGKSPDTFC
     PMGPIAVPKD SLPETLHVQT FVNGEKRQDG TTADLITSIP QLIEVISAGL TLQAGDVIAT
     GTPAGVGVGF HPPKFLRPGD LVEVSVTGLG KLSNRVSDKR PNALARQPGS RLPVYNLERT
     WGAAGLTRVG DKMVNVREIG SGSDTVVFVH GLGASSEYYA PLIQEAGLDA SRRLILYDLE
     GHGLTPTAAS SVVSVESYVA DLEHLFSAKD ITRATVVGWS LGGLIAMLFA ERHASAVEKL
     VLLGPGPNPF PEGAVKVFSD RAASVRAKGM DASGVAQAVA SAATSPRTQR QSPVLVSAVR
     QSLLATHPEG YAKGCTALAK SKDTTIRIER LDVPALLIAG RDDKISPPAL ADTYARRLPN
     AKLEVLEGVG HWHVIEDVGA VARALRGFL
//
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