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Database: UniProt
Entry: Q1CX59_MYXXD
LinkDB: Q1CX59_MYXXD
Original site: Q1CX59_MYXXD 
ID   Q1CX59_MYXXD            Unreviewed;       673 AA.
AC   Q1CX59;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=DUF393 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=MXAN_6900 {ECO:0000313|EMBL:ABF91176.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91176.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF91176.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000113; ABF91176.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1CX59; -.
DR   STRING; 246197.MXAN_6900; -.
DR   EnsemblBacteria; ABF91176; ABF91176; MXAN_6900.
DR   KEGG; mxa:MXAN_6900; -.
DR   eggNOG; COG3011; Bacteria.
DR   HOGENOM; CLU_020557_2_0_7; -.
DR   OrthoDB; 9801773at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR   InterPro; IPR007263; DCC1-like.
DR   InterPro; IPR009613; LMF.
DR   PANTHER; PTHR14463; LIPASE MATURATION FACTOR; 1.
DR   PANTHER; PTHR14463:SF5; LIPASE MATURATION FACTOR 2; 1.
DR   Pfam; PF04134; DCC1-like; 1.
DR   Pfam; PF06762; LMF1; 2.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  75861 MW;  20FA82D3B362081A CRC64;
     MSLGRGGRPR PGCSAASTAG ARGYGDVVRG TAQRSRMMAR ISRGVLLTRP LVLFDGDCAF
     CRRWAARWRW RTGDRVRYRP GSGWRRWLLG IPKADMRRAM QLVEPSGRVS QGAEALFRAL
     AASPRRGTRV AARLGLMPGV LQLAQGVYAV VARNRRQAAG VDRWLFGRAV VPHEYRWVRW
     AFLRLLGGTF LIAFTSLGRQ VRGLYGTQGL RPVAERLAAE RREEASALAR WRRIPSLFWL
     DASDATLVRG CWKGQVLSLA LLFNVAPRFS VSLLWALYLS YVAVGREFLS FQWDVLLLEM
     GLLAALTAPG GLRPGLGRDE PSALDVFLFR LLVFRLYFGS GLSKLQSGDR TWRELSACEH
     YYETAPLPTR GGWYAHHLPR RLQRASTGAV LWLETVVPFL AFGPRRLRQF AFWSLSGLQT
     AISATGNYGF FNVQAWVLGV WLLDDAALRR VLPLKDGPPA QPRPWWRTGV SALVVSPLLV
     LGASEVLRRF EGWQRYRPER VGAMLTWLES QARPLRSVNP YGLFSVMTVQ RPEIIVEGSD
     DGVQWKEYSF HYKVGDPARP PRQVAPHQPR LDWQMWFAAL GSPPGWFVAF LARLLEGSPD
     VLGLLAGNPF PDRPPRMVRA VLYDYRMTDA AERRRTGIWW RRERLGLYVP PLSLAPGPRP
     RGRIPALQWH AGA
//
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