ID A0A1Q4DJ49_9PSEU Unreviewed; 619 AA.
AC A0A1Q4DJ49;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:OJY44363.1};
GN ORFNames=BGP03_16360 {ECO:0000313|EMBL:OJY44363.1};
OS Pseudonocardia sp. 73-21.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY44363.1, ECO:0000313|Proteomes:UP000186163};
RN [1] {ECO:0000313|EMBL:OJY44363.1, ECO:0000313|Proteomes:UP000186163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-21 {ECO:0000313|EMBL:OJY44363.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OJY44363.1}.
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DR EMBL; MKVV01000060; OJY44363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4DJ49; -.
DR STRING; 1895809.BGP03_16360; -.
DR Proteomes; UP000186163; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd06421; CESA_CelA_like; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OJY44363.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 51..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 569..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 68000 MW; 0F897921979BD76C CRC64;
MSIDLSCPSE QADDGGLGRF GVLAGPLTEP PDGPYRVRFQ RLHTAGGRGR AIRTGLIITL
NVAVEVAFVL WLLSPDHHPD FDNPWQINVA NVFVIGAVTL VEGMRLINVF SLSLASLLAR
DPVPVMPDPS LRVAFLTTIV PGKEPLEMVR TTLRAARRIR YEGRLDVWLL DEGDSDEVRE
MCAAEGVRHF SRKGVEQYNQ AHGAFKARTK HGNYNAWLDA HGYRYDVFMS VDPDHVPTPD
YADRMLGYFR DPDTAFVVGP QCYANVDNFV TRAAESQQFP FHSVIQRAGN AYGVAMLVGT
NNAVRIDALG CVGGLMDSIT EDFATGLAIH SRRNPETGGR WRSVYTPDVV AVGEGPSSWA
DYFSQQLRWS RGTFELLRGP FWRRLHRLSG LRPLHYVLIA TFYPSMALGW VLGLINATLY
LTLGASGIVV PPTVWLALYV DATLFQLWVY VRNRRHNVSP FEDEDSPGLR GMVMSVLASP
IYAASLLATV LRMPARFVVT AKDAASTRDS LRAFWRHLIW ALLLVGAIVV AFCEGYANVD
VLMWPVFALL ITITPLLVSW LESAPEAVEP APAGTDAPSP HSEVRPDPVA EIGTGITAES
MSGSAAVPEF APGDLESVS
//