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Database: UniProt
Entry: M0FPJ0_9EURY
LinkDB: M0FPJ0_9EURY
Original site: M0FPJ0_9EURY 
ID   M0FPJ0_9EURY            Unreviewed;       326 AA.
AC   M0FPJ0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Formyl transferase {ECO:0000313|EMBL:ELZ61203.1};
GN   ORFNames=C467_01683 {ECO:0000313|EMBL:ELZ61203.1};
OS   Halorubrum hochstenium ATCC 700873.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1227481 {ECO:0000313|EMBL:ELZ61203.1, ECO:0000313|Proteomes:UP000011689};
RN   [1] {ECO:0000313|EMBL:ELZ61203.1, ECO:0000313|Proteomes:UP000011689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700873 {ECO:0000313|EMBL:ELZ61203.1,
RC   ECO:0000313|Proteomes:UP000011689};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(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:ELZ61203.1}.
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DR   EMBL; AOJO01000007; ELZ61203.1; -; Genomic_DNA.
DR   RefSeq; WP_008581206.1; NZ_AOJO01000007.1.
DR   AlphaFoldDB; M0FPJ0; -.
DR   STRING; 1227481.C467_01683; -.
DR   GeneID; 72714702; -.
DR   PATRIC; fig|1227481.4.peg.313; -.
DR   OrthoDB; 27277at2157; -.
DR   Proteomes; UP000011689; Unassembled WGS sequence.
DR   GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004810; PurU.
DR   PANTHER; PTHR42706; FORMYLTETRAHYDROFOLATE DEFORMYLASE; 1.
DR   PANTHER; PTHR42706:SF1; FORMYLTETRAHYDROFOLATE DEFORMYLASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF13740; ACT_6; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PIRSF; PIRSF036480; FormyFH4_hydr; 1.
DR   PRINTS; PR01575; FFH4HYDRLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011689};
KW   Transferase {ECO:0000313|EMBL:ELZ61203.1}.
FT   DOMAIN          7..81
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          301..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  35847 MW;  F1666132C6DFEA8A CRC64;
     MTRELTEITV VGGDKTGLIA RVTSLLFERG INIEDLDQAV REGVFRMTTR VDTAEMETSR
     GELRRALAEL GRELDVDIQV RFPSDRDARR IALLVTKETH APEALLEAEA NGDLADDGEE
     AEIPVVIGNR GDLRSLAERY DKPFYDVGDG SGNTDEERLL DLLAEYDVDL IALARYMRIL
     SPEVVFRYEG RIINVHPSLL PAFPGAEAYR QAKDAGVRIA GVTAHYVTTD LDQGPVIAQR
     AFDVPPNADV DEIKRRGQPL EADVLLDAVR LHLADAIAVH RGTVHVREEV DVDAQLGLSE
     AAVEANPDEP VDGEPLTRSR PSPSDD
//
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