ID V2X933_MONRO Unreviewed; 324 AA.
AC V2X933;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Methionyl-trna formyltransferase {ECO:0000313|EMBL:ESK90252.1};
GN ORFNames=Moror_7706 {ECO:0000313|EMBL:ESK90252.1};
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:ESK90252.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK90252.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK90252.1,
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:ESK90252.1}.
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DR EMBL; AWSO01000462; ESK90252.1; -; Genomic_DNA.
DR RefSeq; XP_007850462.1; XM_007852271.1.
DR AlphaFoldDB; V2X933; -.
DR STRING; 1381753.V2X933; -.
DR KEGG; mrr:Moror_7706; -.
DR HOGENOM; CLU_033347_0_3_1; -.
DR OrthoDB; 179280at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.12230; -; 1.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ESK90252.1}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..324
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004713595"
FT DOMAIN 75..178
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 203..306
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 324 AA; 35748 MW; 7D534B921EB8B685 CRC64;
MRKSSAGLFW LLVRCFLLVT PLHLKVALLA PLRVLAESLD LPVHLIPQKK VDFKHWKVPE
PFSDLSGRPP PLEHVIVTAS FGRIIPLKIL NLFSQDRRLN VHPSLLPQYR GAAPIQHTIL
NDDRETGVCI IDMLKRSEGI DAGPIWAINR VAVPDDATFP SLRDRLAVSG GQLLVTVLRD
MLSRKATRTI QAEFPDAKPA PPISFNDSLL NFTTMTADSI VRRHRAISHQ RPLATQISGG
HTVQIHDPSV VIRPPKFTPT TPGHACLSKP TKSLLVCCAE GTVLSVPFLK QEGKALLGAQ
AWWNGAQSLG LVKDKHISLC VDRQ
//
