ID V2XTH5_MONRO Unreviewed; 528 AA.
AC V2XTH5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutamyl-trna amidotransferase subunit a {ECO:0000313|EMBL:ESK96131.1};
GN ORFNames=Moror_7272 {ECO:0000313|EMBL:ESK96131.1};
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:ESK96131.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK96131.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96131.1,
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 -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
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:ESK96131.1}.
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DR EMBL; AWSO01000054; ESK96131.1; -; Genomic_DNA.
DR RefSeq; XP_007844526.1; XM_007846335.1.
DR AlphaFoldDB; V2XTH5; -.
DR STRING; 1381753.V2XTH5; -.
DR KEGG; mrr:Moror_7272; -.
DR HOGENOM; CLU_009600_18_1_1; -.
DR OrthoDB; 1769858at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895:SF109; AMIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transferase {ECO:0000313|EMBL:ESK96131.1}.
FT DOMAIN 82..510
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
SQ SEQUENCE 528 AA; 55811 MW; C501757E218C8E4D CRC64;
MAPNLNDLSN IERRLNMKIK PEDREDYLQL LAAMDAAAQV VLAMDDYTLP VNVDRFPRTN
IHVPPDSENK LRGWACKTTV KGSGSGALDG RTICLKDNIC LANVPCRFGT AVINNFVPEV
DATVVTRILE AGGTISGKAT CEDMSHGAAS FTSYNGPVEN PFAHGFSTGG SSSGCGALIG
SGEVDMGIGG DQGGSIRIPA SLCGIVGLKA TFGLIPYTGV LSSEASLDHV GPMARNVTDV
ALLLQAIAGY DGIDDRQLGV PSVDSVPTYA ASLSGILSDP LPLSYVKIGV LKEGFASPHL
APDVEAVVKS AINRFATLGA AVIEVSVPGH SNSGSLMQVL NKMGSSQARL GRANARRGLY
ISNFYDRLLP WNEDKWSKVH SFVKGTAISG EYAFEKYPAV YGRASNIVRK LKESYDAVLK
EVDVIVMPTV PITAPRHVAR DASPLAATKK TAGLTDNTSI FNGTGHPALS LPVGFAAPAP
SDVIHPGDEN IKLPVGLQIV GPWWGEELCL KVGAAWEAGW DWKTGFPR
//
