ID A0A3L8SKL1_CHLGU Unreviewed; 382 AA.
AC A0A3L8SKL1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Methionyl-tRNA formyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00014185};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261};
GN ORFNames=DV515_00006482 {ECO:0000313|EMBL:RLW03680.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW03680.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW03680.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW03680.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW03680.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|ARBA:ARBA00010699}.
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:RLW03680.1}.
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DR EMBL; QUSF01000015; RLW03680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SKL1; -.
DR STRING; 44316.ENSEGOP00005005581; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR InterPro; IPR005794; Fmt.
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 InterPro; IPR041711; Met-tRNA-FMT_N.
DR NCBIfam; TIGR00460; fmt; 1.
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 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 107..210
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 233..340
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 382 AA; 42787 MW; C2936493E5F8D1AA CRC64;
MRARVLRAWR ERVSAAGPPW RVLFFGTDRF AVTALRALWA AGPRLGLPAR CLQRLVHPRE
PGEDSLVSRL EVVTLPSRLP GHLPVRSCAR ELQLPVHEWP HTGPAGQFDV GVVASFGRLL
SEELILQFPY GVLNVHPSCL PRWRGPAPII HTVLHGDKVT GVTIMEIRPK RFDVGPIIKQ
EEVAVPPCCT AQELEGMLAK MGASMLLAVL KNLPESLKNK KEQPKEGVTF APKISIAKSC
IKWEEQTAAQ IIRLHRAIGS MFPLQTLWKG TAIKLLDFVE VDNIPFFSDQ IQNDCEVVPG
SVLFHKKSQT LMACCKEGWV GIKTVVLKKK LTAVDFYNGY MHSWFQQNPT TVHRECRFQT
LKLSTAKKTL KERGILAQDV KP
//
