ID A0A3D8QAB9_9EURO Unreviewed; 538 AA.
AC A0A3D8QAB9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Amidase domain-containing protein {ECO:0000259|Pfam:PF01425};
GN ORFNames=DSM5745_11249 {ECO:0000313|EMBL:RDW58558.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW58558.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW58558.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW58558.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW58558.1}.
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DR EMBL; PVWQ01000023; RDW58558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8QAB9; -.
DR STRING; 1810919.A0A3D8QAB9; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000256690; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR PANTHER; PTHR46072:SF5; GENERAL AMIDASE-C; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000256690}.
FT DOMAIN 78..524
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 233
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 230..233
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 538 AA; 58762 MW; DE1197635AFA7241 CRC64;
MAWEKKAQRK RDELAAKIPK EWLLDLELLK KADELDNILH IPRQSGILTE REIDITEGSD
ATALLSRLKD GELSAYEIAV AFCKRAAIAQ QLTRCLTEIF FDRAIERAKE LDRLFAVTGK
LVGPLHGIPI SLKDSYNVAG VQSTLGYVSF LDNPALTFNS PMVNILLDAG AVIYVKTHMP
QTMMTADSHS NVFGRTRNPY GRSLTAGGSC GGEGALIAMR GSIMGAGTDI AGSLRIPSLC
CGTYGFKPSV GRLPFAGQTP PGRIGLAGGI AVSTGPICTS MRDADLFFRT VVSSRPEDLD
DNSFGFPYLE PPQLESPLTI GMLPEDPALP LHPCMQRTLE IAARKLAAAG HRMVHLPAED
IPSLSDACDL AYRFFNMDPD RTPLRNVTDG GEPFIPSLSL MYNVKGGDPE PTLRQLYDLN
IEKAKVAAKT RQAWLKSGVD VVLAPAYQSC APLHDTYGKT IYTVIWNMVD YPACVIPFGN
ADKAADAEFV RDVKYSPEYK PDDVEGAPCH IQLVGRRLKD EVLLQHARLI EKVLTDGE
//
