ID Q115V7_TRIEI Unreviewed; 909 AA.
AC Q115V7;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Polynucleotide adenylyltransferase region {ECO:0000313|EMBL:ABG50717.1};
GN OrderedLocusNames=Tery_1421 {ECO:0000313|EMBL:ABG50717.1};
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG50717.1};
RN [1] {ECO:0000313|EMBL:ABG50717.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG50717.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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; CP000393; ABG50717.1; -; Genomic_DNA.
DR AlphaFoldDB; Q115V7; -.
DR STRING; 203124.Tery_1421; -.
DR KEGG; ter:Tery_1421; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_3; -.
DR OrthoDB; 9805698at2; -.
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 ECO:0000313|EMBL:ABG50717.1};
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 909 AA; 102516 MW; 69E898B7560F4FC8 CRC64;
MDLILCHTTA DFDGLGAAVG LTHLHPGSRL LLTGGCHPTV KEFLALHRDE FAIIERRSVN
PEKIRSIYIV DTQTRSRLGK TAEWLDLPHL SEIVIYDHHC ETQTDIPATQ TYIEAVGAST
TLIVEKLQTL KNNSSPILTP AEATIMALGI HLDTGSLTFD NTTPRDATAL AWLMQQGASL
SVIGEYVEPG LSPQLQDLLK LALENLQRST VRTYQIGWIL LNTDQHVRGL SSLASSLIDL
TEIDALLLAH THSLKNTTEK SLNIIGRSRI PETNFNQLFQ PLGGGGHSRA AAVSRRDTNP
QATLEKLVDQ LKNQIPHPPT AKDLMSSPVR TIPPETSIEE AHRILLRYNH SGLSVVDSSG
KLVGIISRRD IDIALHHGFS HAPVKGYMTP QLKTISPETN LPEIERLMVT YDIGRLPVLE
NNSLVGIVTR TDVLRELHQQ QRPQYQQLGC IPGETCKSVA ELLQERLAPQ LWQLLSCVAE
LAEKRGWQLY LIGGGVRDLL LSEFDETLLL TDIDLVVDTC RSKSVANAPA VNLGKALQKI
YPTARLEIHG QFQTAALLWH HDLVLDSLWI DIATARTEFY PYPAANPEVE VSSIRQDLYR
RDFTINALAA RLTKPGTGEL LDFFGGLLDL QQKQIRVLHA NSFIEDPTRI YRAVRFAVRL
GFEIESKTEE YIRYAINSGV YDRENVKKGE KNRRAPALET RLKSELKYIL QAPYWKPALR
LLGNLGALRC IHRTLVLDRN LWRQVCLLDR CLQGFDPDKK LSHWQMRLEV LIVSLESGYR
SLVGKNLQLS VDSVKRLEEL ELAKVMVMEN LPKCDTPSQV VWLLREYDLG MLILIIVQCD
RWMRRQIWQY LTQWANVKPV FNGNDLKLMG YKPGRQFKLM LDDILAATLD GKVSDRSEAE
KFLAQYYPQ
//
