ID A1D0G7_NEOFI Unreviewed; 533 AA.
AC A1D0G7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:EAW24487.1};
GN ORFNames=NFIA_040630 {ECO:0000313|EMBL:EAW24487.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW24487.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027686; EAW24487.1; -; Genomic_DNA.
DR RefSeq; XP_001266384.1; XM_001266383.1.
DR AlphaFoldDB; A1D0G7; -.
DR EnsemblFungi; EAW24487; EAW24487; NFIA_040630.
DR GeneID; 4592496; -.
DR KEGG; nfi:NFIA_040630; -.
DR VEuPathDB; FungiDB:NFIA_040630; -.
DR eggNOG; ENOG502QSHE; Eukaryota.
DR HOGENOM; CLU_009942_5_0_1; -.
DR OMA; DIACHAI; -.
DR OrthoDB; 147994at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 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; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642:SF19; AMIDOHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G01480); 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EAW24487.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 50..529
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 533 AA; 58231 MW; 44CFE2809869A15C CRC64;
MKTIFTNGRI FSPSSNDLNA DNAFAESMVI EDDHIIYVGV QDEAPLGDYT IDLNSRIVVP
GFIDGHVHIL NFGLSLGKLD LMDCTCLEDI RKAIRLFAAS HPTAPRLLCR AWIQSTTSGI
ALASMLDDLD PRPIHIESLD LHSVWCNSAA LEEMGIYSTP DPPGGTIHRD ETGRPSGLLS
ESAVVDIVWP FLASITTQEE KLEALGQAFT AYTQAGYTGL VDMAMDETTW DVIQLYRQRH
NPPLHIAAYW LVPFSKNEET NFSHVDRAIQ LHAEFNPTNS PNLCIMGIKL ICDGVVDGCT
AALSQPYGNL TDPVEPIWPA DMLKAVVQRA DQAGLQCAIH AIGDKAVKQA IDVLAEVGTP
GRRHRIEHLE LTAPEDARRL GELGIIASVQ PVHSDPVLFR AWPELIGERC QRAFAYSEFV
DGGARLAIGT DAPTAAHLPL PNLYNATTRR SALEPGESAA TNSRFGLGLA EAVTAATEGA
AYARFAEGWT GCLKEGRRAD FVVLDMGWEA EELLEGKVCE TWFGGKRVYS EER
//
