ID A0A0A7FSH5_9CLOT Unreviewed; 448 AA.
AC A0A0A7FSH5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Poly A polymerase head domain protein {ECO:0000313|EMBL:AIY82523.1};
GN ORFNames=U729_1122 {ECO:0000313|EMBL:AIY82523.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY82523.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY82523.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY82523.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(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|RuleBase:RU003953}.
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DR EMBL; CP006905; AIY82523.1; -; Genomic_DNA.
DR RefSeq; WP_039312360.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FSH5; -.
DR STRING; 1561.NPD11_1881; -.
DR KEGG; cbv:U729_1122; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_3_1_9; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000030635; 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: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; cd00077; HDc; 1.
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; IPR003607; HD/PDEase_dom.
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 Reference proteome {ECO:0000313|Proteomes:UP000030635};
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..229
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 296..437
FT /note="CCA-adding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13735"
SQ SEQUENCE 448 AA; 51004 MW; C0D5D8431D39BD2B CRC64;
MNITIPSNVK YIIDEFYKNN YEAFMVGGCI RDALLCKVPK DYDIATSAKP EITEKLFKKT
IPTGIKHGTV TVLIDNEPYE VTTYRTEGKY KDNRRPDEVY FVSDIKEDLS RRDFTINAFA
YNSREGLKDF FGGLDDLNNS LIRSVGDANK RFNEDALRML RAIRFSTQLN FDIEENTLNA
IKNNKDLIKN ISSERIRDEL CKILVSKNVR KGLNLLEKCG LLQIIIPEIV PSIGFDQKNM
HHFEDVFNHT ISVIEKCPED LTIRLAALLH DIGKPDVFFI DDNGNGRFFG HNTRSEKIAR
DVLNRLRFDN KTIKAVCILV REHMNVLDNA SNLAIKRLIN RVSKENIYSL LALQKADILS
LNDPNVALYK VSDMKNKIDN IIDSNTPLTV KDLAIDGGIL IKELNLKPGK IIGETLDYLL
QLVLKDSSLN TTAILLEESK TFIKNKKG
//
