ID A0A0B4I6A4_METMF Unreviewed; 537 AA.
AC A0A0B4I6A4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:KID98446.1};
DE Flags: Fragment;
GN ORFNames=MAJ_05629 {ECO:0000313|EMBL:KID98446.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID98446.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KID98446.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID98446.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KID98446.1}.
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DR EMBL; AZNE01000024; KID98446.1; -; Genomic_DNA.
DR RefSeq; XP_014577440.1; XM_014721954.1.
DR AlphaFoldDB; A0A0B4I6A4; -.
DR HOGENOM; CLU_009942_6_2_1; -.
DR OrthoDB; 147994at2759; -.
DR Proteomes; UP000031176; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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 PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 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:KID98446.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031176}.
FT DOMAIN 62..533
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KID98446.1"
SQ SEQUENCE 537 AA; 58826 MW; B35B9FC3E47A2518 CRC64;
MASHPSTAGL ENATAYINGR VFTVDENQTW AEAFIVSAEG VFALVGSTDT VMAAARQHGM
VVHDLHGRFV MPGIHDAHVH LLTAGLSHFS NIHLGLDEIM PMSEATDKLK SSSCGCEYAH
AFGRWLSADV FRIKDFDRAH LDEEYPDTPV IIRAGAGHSL HLNTAALRES GYDLANESYP
NGAYVGRRPD GSLNGEVAEL ATTKALLACP KPPVAHVRRA LKYAVHRLHQ AGVTSCQEAA
TNTLMLSTLR DMDRDGQLQL DAYTHIVYAP EFIAEESQPE LIQLLDRAES FKTQHVDTRF
VKIILDGVPL DPYFTQAGLD KDGNVEQEKL FLYDLQEAVL RYDQRGMTCK IHCTGEGATR
LALDAIEAAR ARNPNGPRHE IAHCSGVHPD EYPRFRPLNT TAEMSPSVFF CQTFSPEEDV
LQDWNFPQML RHGAHISIGS DWGVPESPDL LPGVEGILDA VGSGDRAKGA AMVLRMLTLA
GAEAVGRDKE TGSIQAGKRA NFIELDRDLS LGEPGAFTDA KVRRTWFEGE LVYTASV
//