ID A0A1Q5DTE6_9ACTN Unreviewed; 614 AA.
AC A0A1Q5DTE6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:OKI99102.1};
GN ORFNames=AMK18_24240 {ECO:0000313|EMBL:OKI99102.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKI99102.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKI99102.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKI99102.1,
RC ECO:0000313|Proteomes:UP000186839};
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:OKI99102.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LISW01000005; OKI99102.1; -; Genomic_DNA.
DR RefSeq; WP_073864567.1; NZ_LISW01000005.1.
DR AlphaFoldDB; A0A1Q5DTE6; -.
DR OrthoDB; 3653265at2; -.
DR Proteomes; UP000186839; Unassembled WGS sequence.
DR InterPro; IPR038732; HpyO/CreE_NAD-binding.
DR PANTHER; PTHR40254; BLR0577 PROTEIN; 1.
DR PANTHER; PTHR40254:SF1; BLR0577 PROTEIN; 1.
DR Pfam; PF13454; NAD_binding_9; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000186839}.
FT DOMAIN 8..191
FT /note="FAD-dependent urate hydroxylase HpyO/Asp
FT monooxygenase CreE-like FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF13454"
FT REGION 297..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 66013 MW; 83890BFF9E926961 CRC64;
MSARPALAVI GAGPRGTGLV ERLAANAPAL YGDRPLDLHL IDPHPPGSGR IWRRDQSPLL
WMNSMAQDVT MFTDDTVRQE GPVREGPALD AWAADVREGR TPCAEAAADP RLRAEIETLR
GRDFPSRRLQ GAYLRWVYAH AVAALPPAVT VHEHRAPALR VTGPRDGRQL VHLAGRDAPL
AADLVVLTLG HLDAGPDGEQ RALSAFADRH GLVHLPPAFT ADSDLSALPA GEPVIVRGLG
LAFIDLMVLL TEGRGGRYEN GAYVPSGREP VLYAGSRRGV PYRAKIGYGL EGERPPLPRF
FGPERSAELR DRPQPPDFRR DIRPHVDKEL GHAHYHRLFT AHPERTAADR AAFEEKYAAA
GPGSAELRDL IADAVPDPAD RLDLDALDRP LDKIRHTSSD ALQEAVRAHI AADLARRNDP
GHSEDLAVFL GLLSVYGTLV RLGDIGDEWH GFFSYLASGP PGPRLRQLLA LSRAGVVRFL
GAGTTVEADE ERGVFRAASA TVPGARVEAR ALVEARLPAP APGRTRSPLL RTLYEDGAAA
TASGLLAVDP GDGRIVDRAG RPHPRRFALG PHTGARTSGA FTRPRTGGPA FGQNDATARA
ALVLLRRLHP DPGD
//