ID A0A1Q5MAP9_9ACTN Unreviewed; 1323 AA.
AC A0A1Q5MAP9;
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=Family 2 glycosyl transferase {ECO:0000313|EMBL:OKK11303.1};
GN ORFNames=AMK09_32445 {ECO:0000313|EMBL:OKK11303.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK11303.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK11303.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK11303.1,
RC ECO:0000313|Proteomes:UP000186200};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK11303.1}.
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DR EMBL; LIVO01000017; OKK11303.1; -; Genomic_DNA.
DR RefSeq; WP_073738554.1; NZ_LIVO01000017.1.
DR STRING; 1703920.AMK09_32445; -.
DR OrthoDB; 3734530at2; -.
DR Proteomes; UP000186200; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43685:SF2; GLYCO_TRANS_2-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43685; GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186200};
KW Transferase {ECO:0000313|EMBL:OKK11303.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 703..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 139608 MW; 9F6D849B3DF19206 CRC64;
MSVHSHSTAP YAAAAAPEFP RHVVTAVLVA HDGARWLPDV LAGLLGQERP VQSVVAADTG
SADDSARLVT EALGADRVLH LARRTSFGTA VDEASRTAGV LTPDDLPYLK RPSGWDPVTR
SWRDDNYDLP ELPHGEPVQW LWLLHDDCAP EPDALAEMLR VVDNDPHAAI VGPKLRGWYD
RRQLLEVGVS IANSGRRWTG LDRREQDQGQ HDQVRTVLSV SSAGMLIRRD VWEELGGFDR
RLPLMRDDVD LCWRAHMAGH RVLVAPDAVL RHAEASARER RPIDCAGRSV SSPHRVDKAG
AVYTMLVNAR GKLLLWALIR LVLGTLLRTL AYLVGKVPGQ ALDEVAGLLG TLLRPGRILA
ARRQRGKGVI DPAELRGLFP APGATVRATV EQVAGNFGGS TEAESGGSRH GAVESGPGGD
DADFLEIDQF AKLKRVGRKP GPVLFAVLLL VSLVACRSLI GGGALAGGTL LPAPGDVSEL
WGRYADAWHT VGTGGTQTAP PYLAMISALS ALFLGSTGFA LTLLLVCSVP LAGLTAYFVS
RPLIPSRLLR AWASVAYAFL PAATGALATG RLGTAVLLVL LPLIARAAVS AHGMRGSGDS
RGSWRATWAY TLLLTLTMAF TPIVWPLAVV LGVGVLALRR NDITAYGLRF LAAVGTPLLV
LAPWSLSLLT SPSSFLKEAG LEAGTGSASA LDLLGISPGG PKAAGGVLLL GIVLAALAAL
LRGERQFAVR TAWAVALVGL AFAGLANGSG WAGPATLVYG AALIAAALVG ADGARIRVAE
LSFGWRQPVA VLIALAAGIA PVLAAAGWMI GGAAGPLERR DPVQVPAFVA EESGTRDQPR
TLVLDGTSPS SVAYTLVRGS GARLGDAELA AAGGGNSHLD KVVANLVAGS GADQGSQLSG
FAIRYVLVRD GAPKQMSRVL DATPGLSRLS QLDGSALWRV DRQVARIMIV PSAAGAEPLP
VGSSPVEAHT EIPAGGAGRV LRIADAADPG WQATLDGRPL TRKTVDGWAQ GFELPTEGGS
LNLTYEASIT HSAWIWAQAA LGVVLLVLAL PGRRREIDDD LPEETVPVPA EPVAGEGRRA
RRLRAAAQAE GEDGDEDGDE DGDAGERAEY APPQQPAAEP QPHSADGQDV FVPQQADGDT
GEYAAVPQQA DGDTGQYPAV PQQQYGEWDA QQYQGADYPQ YQEGQYQEGQ YQDGQYGAGQ
QQNAPGAYDQ YGYQQQQGDY TSYGQGQYTN APYDPANPQY DPNAQYGTGE QYGNAPYDPN
TPYDPNAQYG TGQYGDQQPY DPQGHDQNQN QNQNRDQNQN PDENPAPGQN PWPTGNASRG
ESE
//
