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Database: UniProt
Entry: A0A1Q9J236_9FIRM
LinkDB: A0A1Q9J236_9FIRM
Original site: A0A1Q9J236_9FIRM 
ID   A0A1Q9J236_9FIRM        Unreviewed;       444 AA.
AC   A0A1Q9J236;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Polynucleotide adenylyltransferase {ECO:0000313|EMBL:OLR38881.1};
GN   ORFNames=BIV16_12680 {ECO:0000313|EMBL:OLR38881.1};
OS   Roseburia sp. 831b.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=1261635 {ECO:0000313|EMBL:OLR38881.1, ECO:0000313|Proteomes:UP000186530};
RN   [1] {ECO:0000313|EMBL:OLR38881.1, ECO:0000313|Proteomes:UP000186530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=831b {ECO:0000313|EMBL:OLR38881.1,
RC   ECO:0000313|Proteomes:UP000186530};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
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|RuleBase:RU003953}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLR38881.1}.
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DR   EMBL; MJHW01000008; OLR38881.1; -; Genomic_DNA.
DR   RefSeq; WP_075680869.1; NZ_MJHW01000008.1.
DR   AlphaFoldDB; A0A1Q9J236; -.
DR   STRING; 1261635.BIV16_12680; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000186530; Unassembled WGS sequence.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 1.10.246.80; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR   InterPro; IPR032810; CCA-adding_enz_C.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   PANTHER; PTHR46173; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR46173:SF1; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   Pfam; PF13735; tRNA_NucTran2_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:OLR38881.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186530};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          23..143
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          170..231
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
FT   DOMAIN          296..436
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13735"
SQ   SEQUENCE   444 AA;  50751 MW;  BF80A72ED6A603AA CRC64;
     MKIVLPEHVK KIIDTLMAHG FEAYAVGGCV RDTMLGRQPQ DWDITTSAKP EEVKKLFLHT
     IDTGIQHGTV TILLDHIGYE VTTYRIDGEY EDARHPKEVL FTSNLLEDLK RRDFTINAMA
     YNDVAGLVDA FDGEGDLKRG IVRCVGNATE RFTEDALRML RAVRFCAQLG FTMEASTKDA
     IRQLAPNIAK ISAERIQVEL VKLLVSPHPE EIRSAYETGL TKVFLPEFDR MMETKQQNKH
     HKFTVGEHTI AALQQIPADK VLRLTMLFHD VAKPVCLTTD ENGCDQFYGH PKKGAQMAKS
     IMRRLKFDNE TTDAVVRLVT CHDDNPVLDE KEIRYAIFRN GEAQYPNLFA VKRADIAAQS
     DYHREEKNNY VNQYEKIYHE ILEKKQCLSL KSLALTGKDL IQAGMTPGKE LGEMLQFLLQ
     QVLEHPEWNQ KDTLLELYQK QKRS
//
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