ID A0A3N6P5R9_9CYAN Unreviewed; 910 AA.
AC A0A3N6P5R9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=CBS domain-containing protein {ECO:0000313|EMBL:RQH31367.1};
GN ORFNames=D5R40_23205 {ECO:0000313|EMBL:RQH31367.1};
OS Okeania hirsuta.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Okeania.
OX NCBI_TaxID=1458930 {ECO:0000313|EMBL:RQH31367.1, ECO:0000313|Proteomes:UP000269154};
RN [1] {ECO:0000313|EMBL:RQH31367.1, ECO:0000313|Proteomes:UP000269154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAB10Feb10-1 {ECO:0000313|EMBL:RQH31367.1,
RC ECO:0000313|Proteomes:UP000269154};
RX PubMed=30444349;
RA Moss N.A., Leao T., Rankin M., McCullough T.M., Qu P., Korobeynikov A.,
RA Smith J.L., Gerwick L., Gerwick W.H.;
RT "Ketoreductase domain dysfunction expands chemodiversity: malyngamide
RT biosynthesis in the cyanobacterium Okeania hirsuta.";
RL ACS Chem. Biol. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC ECO:0000256|RuleBase:RU003953}.
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:RQH31367.1}.
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DR EMBL; RCBY01000166; RQH31367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6P5R9; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000269154; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd04595; CBS_pair_DHH_polyA_Pol_assoc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.10.310.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000269154};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 325..384
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 388..444
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 910 AA; 102609 MW; D2EF1D0428E6A7C4 CRC64;
MNIILCHTTA DFDALGAAVG LTHLHPGSRL VLTGGCHPTV KQFLALHRDE FAIIERRSVN
PKQIRSIYIV DTQTRSRLGK TAQWLDLPHL SEIIIYDHHC EIQTDIPATQ TYIEAVGATT
TLIAEKLQTL QNNSTPVLTP AEATIMALGI HADTGSLTFD HTTPRDAVAL AWLMQQGASL
PVISEYAEPG LSPQLQDLLK IALENIQRST VRNYQIGWIL LHTDEYIPGL SSLASSLIDL
TEIDALLLGH THSFKDTTEK SLSIIGRSRI PDTNLSELLQ PLGGGGHLRA AAVTLRDSNP
EATLEKLVDQ LKNQIPQPPT ARDLMSSPVR TIPPETSIEE AHRILLRYGH SGLSVVDSSR
ELVGIITRRD IDIALHHGFS HAPVKGYMTP QLKTISPKTT LQEIEELMVT YDIGRLPVLE
NNRLVGIVTR TDVLRELHQQ QRPQNEQLGC IPGETCKSIA ELLQERLAPQ LWQLLTCVAE
LAEKRGWQLY LIGGGVRDLL LSKFDETLLL TDIDLVVDGC HSESAEKAPA VELAKALQKI
YPTARLEVHG QFQTAALLWH NDPVLDSLWI DIATARTEFY PYPAANPEVE ASSIRQDLYR
RDFTINALAA RLTEPRAGEL LDFFGGLSDL QGKQMRVLHA NSFIEDPTRI YRAVRFAVRL
GFEIEAKTEE YIRYAINSGV YHRQNIGKAE KNRRVPALET RLKSELKYIL QANYWKPALK
LLGNLGALRC IHRTLELDRK LWQQVCLMDR CLQRFDAQKS LSHWQMRLEV LIAYLESEYR
GLVGKNLQLP VDSVKRLEQL ELAKGKVMDS LPECNSPSQV VWLLRKYDLP MLILIAVQCE
RWVRRRVWQY LTQWANVKPV LNGNDLKEMG YKPGREFKLI LDDLLTATLD GVVSDRSDAE
KFLARYYPLR
//
