ID E6W6K8_DESIS Unreviewed; 875 AA.
AC E6W6K8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Polynucleotide adenylyltransferase region {ECO:0000313|EMBL:ADU65008.1};
GN OrderedLocusNames=Selin_0252 {ECO:0000313|EMBL:ADU65008.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65008.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU65008.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002432; ADU65008.1; -; Genomic_DNA.
DR RefSeq; WP_013504897.1; NC_014836.1.
DR AlphaFoldDB; E6W6K8; -.
DR STRING; 653733.Selin_0252; -.
DR KEGG; din:Selin_0252; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_0; -.
DR InParanoid; E6W6K8; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000002572; 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; 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; IPR003156; DHHA1_dom.
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; PF02272; DHHA1; 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 ECO:0000313|EMBL:ADU65008.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572};
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 316..374
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 378..434
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 875 AA; 99091 MW; A924D1713309FA9A CRC64;
MRLITSHQNP DFDAFASMVA AACLHPGATI VIIGSLSQNI QDYLELYPLP AGISLYKESE
VNIADISHMV VVDASDGRRL GKLRKAFGKV PTIVYDHHQD GVDEEVADRD IEHHYCNCGA
NSSFMVRLLQ KQHIALEGWL ATLLLCGIYE DTGHLSYSST RPLDCYCAGD LIAAGADLKQ
VHQILSRDWK DADIHILSDL LKNFETFSIM GVSVGISHAD FHIYVPDVSE MLSNVMGVRR
CTLLIVFLRM EGRIYCIVRS TSMVGANDVA ALFEGGGHHE AASATVKEMT LVQAMDFTRA
SLKEIISRSK RTRTIMSSPA ITIESHKSTQ EAYEQFSRDG VNCLPVVEPD GSLYGILSKN
QCMKALFHGL GGRSVTSITD TDIQYIEADE PFSRAEHILL SGRQAMVPVV EAKRVTGVIT
RTDLLREYRH DTDETLPAQE RARSTHRPRH VRKMLVEVMG RQAFAYLEEA SQLANEMDIQ
VYLVGGIVRD LVLRVKNQDM DFVVAGDGIS FGNRLAERLG GRIRVHERFN TGVIILPGDD
FRIDVASSRN EYYDHPGALP NVSPGSIKRD LYRRDFSINA MAVSLNTFEL IDYFGGVQDI
RDKKIRVLHN LSFIEDPTRI FRAVRFEQRY SFQIGEQTIK LLRSARDLDL IQHISGHRIY
EELRHMFLEQ EPAKHMARLF ELDLMRSIHP ALGYDQKTMK LVESMEDLLV VSDFLRLEDV
RRDALYCALI LRTIKAEQIM ALPILQELPQ RDREIIAFGC SKAGMLLHEL GRTGKLWQKL
RLVKRHEEEV LLLAIVYGNQ QASAHFLREY LRSYRTIHPI LRGDELMALG VPRGHQVGDA
LLMLTAYIIG RDANRPDRRE EENFVRRIVL RAVEQ
//
