ID F0S2H1_DESTD Unreviewed; 881 AA.
AC F0S2H1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Polynucleotide adenylyltransferase region {ECO:0000313|EMBL:ADY73043.1};
GN OrderedLocusNames=Dester_0388 {ECO:0000313|EMBL:ADY73043.1};
OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73043.1, ECO:0000313|Proteomes:UP000007102};
RN [1] {ECO:0000313|EMBL:ADY73043.1, ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX PubMed=22675590; DOI=10.4056/sigs.2465574;
RA Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfur-reducer
RT Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT hydrothermal vent.";
RL Stand. Genomic Sci. 5:407-415(2011).
RN [2] {ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL Submitted (FEB-2011) 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; CP002543; ADY73043.1; -; Genomic_DNA.
DR RefSeq; WP_013638001.1; NC_015185.1.
DR AlphaFoldDB; F0S2H1; -.
DR STRING; 868864.Dester_0388; -.
DR KEGG; dte:Dester_0388; -.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR eggNOG; COG2524; Bacteria.
DR HOGENOM; CLU_015961_5_0_0; -.
DR InParanoid; F0S2H1; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000007102; 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:ADY73043.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007102};
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 315..371
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 378..435
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 881 AA; 100511 MW; 8C7596D40FA180D6 CRC64;
MGIVITTHKN MDLDALGAVI AAKKLYPDAT VVLPGTKGND VVKLLSENPE LIDFVEEENF
NPQSVKKIVI VDTDNINRIP DSIRKLIKEK NVETIVYDHH SAEVSFKDIE HHYKASGSVT
SLMVLLLKGK GITPTPIEAS VMLAGIYSDT GNFRFSSTSP IDFLAAAYLV SIGANIEFVK
KYLPSDLSDK ELDILKNLKD NLKITEVHGN LIGITYGRFD SYIKDISSLV SKLLEISGLP
AIIAVLEFEG SVSLIGRSKT PKVDVSKVAE HFGGGGHVEA ASASIKRKTV FEVLEELKKV
LEEVVEPLKK AKDIMTYPPI VVSFDSSIEE ARTTLMKNSI NAAPVVDKKR NIVGIVNRTL
IDKAIYMGLK EEPIFEIMER DFLQVLPETP IGDVEKVIID RHQSFVPVVQ DGKPIGVITR
TDILMNLYKD EISDISKFYE KRALSSPKYK NIVQKLKESL PKDLLDLIKK IGEFADEFGV
NAYIVGGFVR DLILGRKNFD VDIVIEGDAT EFAKKVAKKA NAKVHTFERF KTATVVFPDG
FRIDFASART EVYKAPGALP EVDMAPLKKD LMRRDFTINT LAIKLNKKEF GKLIDFFGGL
RDIKDRKIRI LHSLSFVEDP TRILRALRFA TRYRFELGKH TEKLLKIAVQ RKLFKTVEGQ
RIYHELKQIF LEDNPLRVVN KLAYYKVLSS IFPTIVWDKK KKDLFERIRK VIIWHKLNFQ
EKEIRYDLLY FGALLIGQSF QKIDTYLDNL SVPEKDREIL KEILLKASYL LKEVNKERKN
SEIYKLVSRF KEEVLLFAAS LTEEEWKREK ILEYLKSWRF TKPAVTGDNL KAIGLKPGPI
FREILNELKY RLIDKEIPED KEKQLDFVKF LIKEEEKYAK R
//
