ID E3CY64_9BACT Unreviewed; 871 AA.
AC E3CY64;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=CBS domain containing protein {ECO:0000313|EMBL:EFQ23597.1};
GN ORFNames=Apau_1171 {ECO:0000313|EMBL:EFQ23597.1};
OS Aminomonas paucivorans DSM 12260.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Aminomonas.
OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ23597.1, ECO:0000313|Proteomes:UP000005096};
RN [1] {ECO:0000313|EMBL:EFQ23597.1, ECO:0000313|Proteomes:UP000005096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ23597.1,
RC ECO:0000313|Proteomes:UP000005096};
RX PubMed=21304733;
RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT strain (GLU-3).";
RL Stand. Genomic Sci. 3:285-293(2010).
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}.
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DR EMBL; CM001022; EFQ23597.1; -; Genomic_DNA.
DR RefSeq; WP_006300798.1; NZ_CM001022.1.
DR AlphaFoldDB; E3CY64; -.
DR STRING; 584708.Apau_1171; -.
DR PaxDb; 584708-Apau_1171; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_0; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000005096; Chromosome.
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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
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 InterPro; IPR032828; PolyA_RNA-bd.
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 Pfam; PF12627; PolyA_pol_RNAbd; 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:UP000005096};
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 314..370
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 376..432
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 871 AA; 96325 MW; 8FA9902CA822285C CRC64;
MKLITTHVGA DFDSLASMVA VRKLYREGTL CFSGAASRNV RDFLKRHAGR LRVTTPRKVS
LEEVDTLIVV DARSLGRIGP FAALARDPRV KVHLFDHHPP VSDEIPSDYA LVETAGSTTT
LLVELLLERH VPISPFEATL FTLGIYEDTG ALTFGATGER EYAAAAALRR LGADLSVIPT
WIELAFTLLE RELLDRMMEA AYERFLSGSR VVFCALEFPQ YVEGISLFAH RLRDAFDADV
VVAVVSMDRR TYITVRSREG AVDAVRLLAR FQGGGTPPGA AVALPRTDPT ELLQALEKDL
EGALTPVVEV GRIMSSPVMA VAPDQTVEEA YRLMIRYGHA ALPVVQEERL VGLITRKDLD
KAQLHGLGAV PVVEFMTESV LTVSSRAPVG EAHRIMVSAN IGRLPVVDQE TLVGIVTRTD
LLRALYPVSL PPGERALSPG LPWMENRADL LEKGLDPGLR DRLRALGRVA QGQGARLFGI
GGFVRDLLLG RPNQDVDLVV EGDAVAFLES FKGSDVRVSV HRRYRTGTLV FPEGQKIDVA
TARREFYEYP VAPPTVSSDS LKHDLYRRDF SVNAMALSLN PATWGELVDY FGGRVDLERR
LLRVLHNLSF VEDPTRVLRG VRLERRLRFH MGDDTEKLAR NCVRGGLLSL LSGPRLRSEL
ELILLEPEAA SMAVRLRDLG VLEGVFPGLR PGDRTQRTLR RLAAFRKRMG RDLPDSGSDR
WLAALGALLG EGSGWVQRNA LDRLSLSARE RCWVERGLEG LGAAESFLGT RADPPLSSIY
GFLRDAPVPA ALLWAAATEQ WRVRRRILLY LTRLFRVEPM LTGRDLLEMG CPKGPWVGRL
LGDLRGARLD GEVETLEDER AWAIRRLGEG G
//
