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Database: UniProt
Entry: A0A2A7MH35_9CLOT
LinkDB: A0A2A7MH35_9CLOT
Original site: A0A2A7MH35_9CLOT 
ID   A0A2A7MH35_9CLOT        Unreviewed;       443 AA.
AC   A0A2A7MH35;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Polynucleotide adenylyltransferase {ECO:0000313|EMBL:PEG30827.1};
GN   ORFNames=CQ394_03650 {ECO:0000313|EMBL:PEG30827.1};
OS   Clostridium neonatale.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG30827.1, ECO:0000313|Proteomes:UP000220840};
RN   [1] {ECO:0000313|EMBL:PEG30827.1, ECO:0000313|Proteomes:UP000220840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG30827.1,
RC   ECO:0000313|Proteomes:UP000220840};
RA   Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT   "Effective Description of Clostridium neonatale sp. nov. linked to
RT   necrotizing enterocolitis in neonates and a clarification of species
RT   assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT   Rainey 2016.";
RL   Submitted (OCT-2017) 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|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:PEG30827.1}.
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DR   EMBL; PDCJ01000001; PEG30827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A7MH35; -.
DR   STRING; 137838.GCA_001458595_02190; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000220840; 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:PEG30827.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220840};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          26..145
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          173..231
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
FT   DOMAIN          281..438
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13735"
SQ   SEQUENCE   443 AA;  51854 MW;  366F7979ECE000F7 CRC64;
     MERLDIKIQK DVKYILNRLI KNNFEAYIVG GCVRDIILNK EPKDYDITTS AKPEEVIKLF
     DKVILTGIKH GTVTVVLNNE NYEVTTFRID GEYKDQRHPK EVKFVTSLRE DLSRRDFTVN
     AMAYNDIDGF KDYFNGLNDL KNKIIKTVGN PEKRFLEDAL RMLRAIRFSA QLNFEIEEET
     LNAIKKLKDN IIKISKERIR EEFNKIIIYN PRKIDLLREC GLLEFIIKEM RKAYGFNQNN
     MYHVYDLYMH TIICMENIDA KLHLRLAMLL HDLGKLETKT TDENGISHFY GHVECSIEIA
     KKVLKGLKYD NVTIENVLIL IKYHDYPLND KITVKRLLNK IGEELLYDLL KVKKADILGK
     NSLYKETQLK NLLDIEKCLN NIIENKECFN IKQLKISGNE LIKVGLKGKE IGEMLNYLLD
     MVMEDKAINN TEELIKFAKE KIN
//
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