ID A0A1Q7TWM6_9CHLR Unreviewed; 714 AA.
AC A0A1Q7TWM6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE RecName: Full=Polysaccharide biosynthesis protein CapD-like domain-containing protein {ECO:0000259|Pfam:PF02719};
GN ORFNames=AUG84_00260 {ECO:0000313|EMBL:OLD92888.1};
OS Chloroflexi bacterium 13_1_20CM_4_66_7.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805062 {ECO:0000313|EMBL:OLD92888.1, ECO:0000313|Proteomes:UP000187287};
RN [1] {ECO:0000313|EMBL:OLD92888.1, ECO:0000313|Proteomes:UP000187287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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:OLD92888.1}.
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DR EMBL; MNIW01000004; OLD92888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7TWM6; -.
DR Proteomes; UP000187287; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR Pfam; PF13727; CoA_binding_3; 1.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..577
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
FT REGION 618..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 77740 MW; C3E91928B9EADE6D CRC64;
MIGLPSMPNI RNRYLFATDL LLLAAAPWLA YALRFEGLVW NAADRRTALV YAGLSVVLKL
GVFLPFGMYS RLWRQASIPD MAKIVEATAL STSVCAALGL VVLPLSGLTP LRLPISVLIL
DSFLTVTAVS APRLLIRGLG TLQRFAQMDH GRRALIAGAG AAGEMILREL RANPQLGLTP
VGFVDDDPRK HDHRLNDLPV LGALSEIPAI IARYRIDEIV IAMPTAPGRA LRTVVRAATD
AHIPTRTVPA LFEILSGRVS LSHLRKVEIQ DLLRREPVQT NLGLVRAMVS GHTVLVTGAG
GSIGSELARQ LAQLEPTRLV LLGNGENEIF DILNELRAAH PALHLSSLIA DVRDLPRMRS
VFRRLHPHAV FHAAAHKHVP LMEENVADAV TNNVGGTGNI VDCAVECGTQ HFVLISTDKA
VRPTSVMGAT KRVAEMIVQE AAVRHGRNFV SVRFGNVLGS RGSVVPIFLS QIRAGGPLTI
THPDMRRYFM TIPEAVQLVL QAGALGRGGE VFVLDMGEPI QIVDLATDLV RLSGLEVGRD
IEIRYTGIRP GERLYEEPFF RHEEVLPTAH PKILRAKNNH VLAGARVSVD LLAAAGREAR
SDEELRQLLR RLVPDFGTAS ADDQRDRPRA AAHARASRGQ LAGPRIFVER RTPQDRRGGE
RRTRVTAVSL DRRASERRTG VERRFAVLNA AAEILEPDSA MPRRSAAGTA TGTA
//
