ID A0A0G4M2C9_9PEZI Unreviewed; 389 AA.
AC A0A0G4M2C9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
DE Flags: Fragment;
GN ORFNames=BN1708_004652 {ECO:0000313|EMBL:CRK28441.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK28441.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK28441.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK28441.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC haloalkanoic acid dehalogenase family. {ECO:0000256|ARBA:ARBA00008106}.
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DR EMBL; CVQH01020751; CRK28441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4M2C9; -.
DR STRING; 100787.A0A0G4M2C9; -.
DR OrthoDB; 1351643at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0019120; F:hydrolase activity, acting on acid halide bonds, in C-halide compounds; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR006328; 2-HAD.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01493; HAD-SF-IA-v2; 1.
DR NCBIfam; TIGR01428; HAD_type_II; 1.
DR PANTHER; PTHR43316:SF3; HALOACID DEHALOGENASE, TYPE II (AFU_ORTHOLOGUE AFUA_2G07750)-RELATED; 1.
DR PANTHER; PTHR43316; HYDROLASE, HALOACID DELAHOGENASE-RELATED; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 271..376
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT NON_TER 389
FT /evidence="ECO:0000313|EMBL:CRK28441.1"
SQ SEQUENCE 389 AA; 43570 MW; 813832CF9E3B6390 CRC64;
MSSSSSAELI KTQVKAMTFD VFGTTVDWRS SVTDELTNRA ASKSGELPND DRTANLRRLT
RDDWGHFAQQ WRNTYSTFVR GFIPGETPWK DVDTHHYDAL VDLLAEWQLG GIYSDEEVRE
LSLVWHRLRP WDEAAKGLRL LGGQYVTSML SNGNASLLRD LDDFGSLNFQ RRLSGEDFKA
YKPNPKVYLG AAQSLEMTEP GHVAMVAAHL DDLEGARKCG LRTVYVERPG EEAWKKDEDR
YRNAKDWVDI WIGEKDGGFV ELARRLGVEY DFPVEPPNPF EGIFAAVARK SPATGRGVDG
SSDGWHVEEA LSLDEALLGF TRGPAFGAFM EGRAGVIKQG ALADWVVLDE RLDALEIDDL
RSLKVKQTWV GGRMVYEYPG GEGLEVEDL
//
