ID   A0A077JLC5_9CYAN        Unreviewed;       905 AA.
AC   A0A077JLC5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Poly(A) polymerase/tRNA nucleotidyltransferase family protein {ECO:0000313|EMBL:BAP18378.1};
GN   ORFNames=ETSB_1662 {ECO:0000313|EMBL:BAP18378.1};
OS   cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP18378.1, ECO:0000313|Proteomes:UP000031625};
RN   [1] {ECO:0000313|EMBL:BAP18378.1, ECO:0000313|Proteomes:UP000031625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP18378.1};
RX   PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA   Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA   Archibald J.M., Inagaki Y.;
RT   "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT   recent adaptations to an intracellular lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
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; AP012549; BAP18378.1; -; Genomic_DNA.
DR   RefSeq; WP_044107217.1; NZ_AP012549.1.
DR   AlphaFoldDB; A0A077JLC5; -.
DR   STRING; 1228987.ETSB_1662; -.
DR   KEGG; ceo:ETSB_1662; -.
DR   HOGENOM; CLU_015961_5_0_3; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000031625; 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; 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   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          327..386
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          390..445
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   905 AA;  102936 MW;  18A8CF292F8A1416 CRC64;
     MDLILCHQNV DFDALGAAVG LSCLKIDSRI VLTGGAHPAV RDFLALYRDE FALIELHIIN
     PKQIRTLIVV NSQKCDRLGT VSSWFDLPHI KTIEIYDHHL NTNSYSDIPS TFTKIEPVGA
     TTTLIVERMQ RESVHPNPIE ATVMALGIHV DTGSLTFSQS TSRDAYALAW LMERGANVKT
     IDEYCDPRFS LKLQQLLQKA LENFQKIEIR GYTITSVLLK TETYIPGLSS LAELLIKLTE
     SDALLLGYFD DKCRNNKPDK KGLLTIIGRT RIEGTNLQQL FQSYEGAGHK QAGSLMLQEV
     EPQSTLDKLL QEFIAQIPYP LTARDLMSSP VKTIRPETTI EQAQKILFRY GHSGLSVVDE
     NEYLVGIISR RDIDLAFHYG LSHAPIKGHM AQYFKTITPD TILPEIESIM VTNDVERLPV
     VENNKLLGIV TRTDLLRQIY QARREKKNKN SNPIPLVSCF LPSISQRLSS PVWKLLQLAA
     KEAKKRGWHL YIVGGAVRDF FLSEEEKLLL LQDIDLVVDG FHHSAGVGAG VELASTLRKT
     FPNARLSVHG EFQTAALVWD RDPQLGSLWV DIATSRTEFY PYPAANPKVE ASSIHQDLYR
     RDFTINALAV RLTSPREGEL LDFFGGMLDL QLRQIRVLHA NSFIEDPTRI YRAVRFAARL
     GFKIEPQTKA YINNAIKSGI YKQLKSKNYA VPALKTRLKI ELKSILEAHY WKQALKLLAD
     LDALLCLHSK LALDDILWWQ TCYISRWLKY LDPENNLEHW LLRLEVLISQ LDTVESIKIA
     LDFQLPKDSI IRLKVLSEVE LEIKKKLLKN NIISEKTRLL NLYRLPTLIL VAVRSSKEIR
     RTIWQYITKW SNIQPLLNGN DLKAMGYKPG PTYKIILDRL LTASLDKKIK TKEEAENLVK
     QMMSD
//