ID A0A1G1W9N6_9BACT Unreviewed; 429 AA.
AC A0A1G1W9N6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00012261};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261};
DE Flags: Fragment;
GN ORFNames=A2Y57_04105 {ECO:0000313|EMBL:OGY24392.1};
OS Candidatus Woykebacteria bacterium RBG_13_40_7b.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802594 {ECO:0000313|EMBL:OGY24392.1, ECO:0000313|Proteomes:UP000177103};
RN [1] {ECO:0000313|EMBL:OGY24392.1, ECO:0000313|Proteomes:UP000177103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC {ECO:0000256|ARBA:ARBA00010759}.
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:OGY24392.1}.
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DR EMBL; MHCQ01000028; OGY24392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1W9N6; -.
DR Proteomes; UP000177103; Unassembled WGS sequence.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042586; F:peptide deformylase activity; IEA:InterPro.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR CDD; cd00487; Pep_deformylase; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR Gene3D; 3.90.45.10; Peptide deformylase; 1.
DR HAMAP; MF_00182; Formyl_trans; 1.
DR HAMAP; MF_00163; Pep_deformylase; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
DR InterPro; IPR023635; Peptide_deformylase.
DR InterPro; IPR036821; Peptide_deformylase_sf.
DR NCBIfam; TIGR00460; fmt; 1.
DR NCBIfam; TIGR00079; pept_deformyl; 1.
DR PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF01327; Pep_deformylase; 1.
DR PRINTS; PR01576; PDEFORMYLASE.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF56420; Peptide deformylase; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
FT DOMAIN 158..339
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT NON_TER 429
FT /evidence="ECO:0000313|EMBL:OGY24392.1"
SQ SEQUENCE 429 AA; 48299 MW; D973CA00276D952C CRC64;
MILPLTKNTD PVWKKKFENV AKITPEIRKL INEMKETLEF VGGGVGLAAP QVGSPLRLFI
VDYLNFKEVF VNPELRVLSK ELIENEEGCF SVPGFRGVVP RSKRVEIKYL NLQGEKKKLT
ASGFLARILQ HEYDHLSSTF YFQRIIDKKQ LFQIRPIKIV FFGTPPFSVT ILRKLIGNTI
VGDLQLSLVV TSPDKQSGRN QKPTPSPVKE LALKYNLKVE TPENLKDKSF ISSLSSLTPD
LIVLASYGKI VPKEILDIPK FGSLNVHPSL LPKYRGPSPI QTAILNGDEG TGVSIMLMED
KVDSGPILAQ VRIKISENDT YETLSKKLSE QSGRFLVDTI YLYLGKRVKP ESQDESQATY
TKLIKKEDGF IDLAKPPKKE VLERMTRAYY PWPGVWTRLP ATDGAAYGGQ AKHQGKILKF
LPDRKVQLE
//
