ID A0A1M3HLD4_9SPHI Unreviewed; 407 AA.
AC A0A1M3HLD4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Acyltransferase 3 domain-containing protein {ECO:0000259|Pfam:PF01757};
GN ORFNames=BGO55_08375 {ECO:0000313|EMBL:OJW59278.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW59278.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW59278.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW59278.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJW59278.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKTZ01000005; OJW59278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3HLD4; -.
DR STRING; 1895841.BGO55_08375; -.
DR Proteomes; UP000184242; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..364
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
SQ SEQUENCE 407 AA; 46028 MW; 60CBBF1B685B67ED CRC64;
MEEISNYFVL PVVAIALIAV SFAAPLSGVE AKAHRYSTID GLRGYLATFV FLHHAATWYY
FVHVQEWSYE PTKLYLHFGS TSVALFFMIT SFLFISKLAD AMGGQVDWLK LYVSRVLRIM
PLYLFAIVVL FLLAGMISGF ILAVPVRHLL TDAGRWLLFM EPEINGVPGT RYIISGVQWT
LAFECLFYCS LPFMALLFFR IKSPLVLFLT AGICMAIFVY VIFTSYPERA WYGIAQFGGG
IPAAFLQRSP RVRRFCSRFW MAPILILICY FVLSRYKSIL APLPFLGVTV VFTFIACGNS
LFGLLTIRAS RLLGQVSYSV YLLHGLLLYC GFKFVLGFPL GRRLTPLGHW VAMTGFCIML
MVLASLSYRW IEQPCINVSG RAAKSLRRRF KKQTGPFGRA TEVNQSL
//
