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Database: UniProt
Entry: A0A1C6V885_9ACTN
LinkDB: A0A1C6V885_9ACTN
Original site: A0A1C6V885_9ACTN 
ID   A0A1C6V885_9ACTN        Unreviewed;       731 AA.
AC   A0A1C6V885;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   SubName: Full=Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase {ECO:0000313|EMBL:SCL62485.1};
GN   ORFNames=GA0070603_3412 {ECO:0000313|EMBL:SCL62485.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL62485.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL62485.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL62485.1,
RC   ECO:0000313|Proteomes:UP000198605};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMIB01000002; SCL62485.1; -; Genomic_DNA.
DR   BioCyc; GCF_900091475:GA0070603_RS16955-MONOMER; -.
DR   Proteomes; UP000198605; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000198605};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:SCL62485.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     57       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    329    354       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    620    646       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    652    672       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      102    289       NodB homology. {ECO:0000259|PROSITE:
FT                                PS51677}.
FT   REGION        1     27       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   731 AA;  80468 MW;  38D5632BF3528EC5 CRC64;
     MGVWRAGRRL DGTGDVPAPP GLTTWGRRQR RRDRRRWLLA AVATFILLNL LAIGAYANAR
     FTPDHRAEGP AGTATVPKPV RDGGTVVDFP DGRLEARRMP PKTIALTFDD GPDPKWTPQV
     LDVLARHHAP ATFFVVGSQV ARHPELAERM AREGHELGIH TFTHPQMADL PAWRRKLEYS
     QTQAAIAHLT GVSTSLARLP YSSGVDSLDD ASWPVVRETG RWGYVSVFND TDSRDWARPG
     VPAIVRNATP DGDRGAVVLM HDSGGDRSQT VAALDRFIPE MQARGYRFTT VSQGLGQPGA
     GTARLDALDR ARGALLVWGV RAADGTIRLL WLLLIVVGLL TLARTLLLFG YAVAHARRRR
     APTWSWGGVV TDPVTIIVPA YNERTTIAAA VRSLATGSHP GIEVLVVDDE SDDGTAEEVE
     RLGLPNVRVA RVPGGGKAAA LNAGVALARH DLLVMVDADT VVDPDAIHRL VQPFADPRVG
     AVAGNVKVGN RRRLLGRWQH IEYVIGFSLD RRLYDTLHCM PTIPGALGAF RREAVRAAGG
     LSRATLAEDT DLTMGIHRAG WRVVYEETAV ARTEAPVTLP ELWRQRYRWS YGTMQALWRH
     RRALVERGPS GRFGRRGLPF IALFSVLLPL LAPVVDIFAV YGLFFLDRYE TVAAWLAVLV
     VQVVTAILAF RLDREPLRPL WALPLQQFVY RQVMYLVLLH SVITALSGGR LKWQKLRRTG
     EVAAAHTQPV T
//
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