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Database: UniProt
Entry: A0A099S8U7_9CLOT
LinkDB: A0A099S8U7_9CLOT
Original site: A0A099S8U7_9CLOT 
ID   A0A099S8U7_9CLOT        Unreviewed;       455 AA.
AC   A0A099S8U7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Polynucleotide adenylyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DP68_04920 {ECO:0000313|EMBL:KGK89029.1};
OS   Clostridium sp. HMP27.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK89029.1, ECO:0000313|Proteomes:UP000030009};
RN   [1] {ECO:0000313|EMBL:KGK89029.1, ECO:0000313|Proteomes:UP000030009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMP27 {ECO:0000313|EMBL:KGK89029.1,
RC   ECO:0000313|Proteomes:UP000030009};
RA   Tan B.F., Foght J., Budwill K.;
RT   "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal
RT   degrading methanogenic culture.";
RL   Submitted (APR-2014) 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:KGK89029.1}.
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DR   EMBL; JMFY01000009; KGK89029.1; -; Genomic_DNA.
DR   RefSeq; WP_035306946.1; NZ_JMFY01000009.1.
DR   AlphaFoldDB; A0A099S8U7; -.
DR   STRING; 1487921.DP68_04920; -.
DR   eggNOG; COG0617; Bacteria.
DR   Proteomes; UP000030009; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
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; IPR006674; HD_domain.
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; PF01966; HD; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030009};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          27..147
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          174..231
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
FT   DOMAIN          259..367
FT                   /note="HD"
FT                   /evidence="ECO:0000259|Pfam:PF01966"
FT   DOMAIN          387..447
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13735"
SQ   SEQUENCE   455 AA;  51554 MW;  B8BAA060A7050E85 CRC64;
     MNFKIHIPKN PALAIKMLVD AGFEAGVVGG CTRDAIMEEE PHDWDICTSA TPDEIQVVFR
     DFKQLGIGLK HGTVVIIMDG EEIEITTYRI DGEYSDCRRP NNVYFTKNLI EDLSRRDYTQ
     NAIFFNEFQG IIDPFNGVSD IEHKIIRCVG NANKRLQEDA LRILRGIRFA STLGFKVEES
     TKTAMLRNKE LLKNISKERI TVEFVKMLQG KNAVNILDEF QDIITYIIPE TKSMVGFKQH
     NPYHIYDVWK HTLVATNNVE GLILKLTMFF HDIGKTSCYT IDGQGIGHFY GHADISAKIT
     SEIFKRMKIT NAEGINAADL KDIIELIKYH DIMIHPTKPS VKKMLWKLDG SALQFKRLLS
     VKRADALAQS PTNLANRLKE IHTIEELLNE VLTETNCFTL KDLAITGKDL IALGIPPGKS
     IGKLLNKLLE SVIDEKLLNE KETLLSEAQK YINLS
//
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