ID V2WSJ9_MONRO Unreviewed; 602 AA.
AC V2WSJ9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ESK89828.1};
GN ORFNames=Moror_876 {ECO:0000313|EMBL:ESK89828.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89828.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89828.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89828.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(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:ESK89828.1}.
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DR EMBL; AWSO01000510; ESK89828.1; -; Genomic_DNA.
DR RefSeq; XP_007850869.1; XM_007852678.1.
DR AlphaFoldDB; V2WSJ9; -.
DR KEGG; mrr:Moror_876; -.
DR HOGENOM; CLU_009942_1_1_1; -.
DR OrthoDB; 147994at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:ESK89828.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..599
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 602 AA; 67150 MW; 84BAB14859933FAC CRC64;
MPEMQENTAL LPGKNQKYHY TPAHTNSVSK RTRRIGRKRL CAVVLLAVIL WAGVSFYHRK
SQEKGYALCT KEGHKVYTVD KENTVVQCIV VEGTGIVGTY SDIAHLRESG YRAMIRYTKP
GAIIVPGLSD SHVHSLEYGY SRALPLDSAR SIPDAVALVR EYILANPDIY SNKSKVIEGW
GWDKTIWPVE EYPTAADLEA DPVIRGRQVM LRSKDMHSSW VSKATLDVNA PFPEEYEGGV
IMRDENGNPT GIFQDEAQGL IKPPQLTDDD LMKRFMVTVN DALKYGVTSM HDAGSTPGPL
AFFQRVAAKR TLPIRMYAMK YFNETWDYPP PVPSEVELKN RLNNRSIKII GDGSLRSGGA
FLFEPYTDDP STVGFMRHSP EILKKRIPEL LKNGWQVNTH AIGDRANSEI LDAFEIAAND
GVDLRALRPR IEHAQIMRQI DIDRMGTLGV IASVQPTHAT DDMWYGEARL GPERVRGLYA
FRSILNSGAR ITTGSDIPVE GVNPLEGFYA AVTRVDKQGR SPHGPGGWFP EQKLTRLEAL
RGMTIEPAYA SFSEDILGSL EKGKKADFVV LSEDIMEIPA EKILEVNVHA TVLDGEVVYR
SF
//
