ID A0A1H8H146_9RHOB Unreviewed; 389 AA.
AC A0A1H8H146;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Poly(A) polymerase {ECO:0000313|EMBL:SEN49487.1};
GN ORFNames=SAMN04489859_100842 {ECO:0000313|EMBL:SEN49487.1};
OS Paracoccus alcaliphilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34002 {ECO:0000313|EMBL:SEN49487.1, ECO:0000313|Proteomes:UP000199054};
RN [1] {ECO:0000313|EMBL:SEN49487.1, ECO:0000313|Proteomes:UP000199054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8512 {ECO:0000313|EMBL:SEN49487.1,
RC ECO:0000313|Proteomes:UP000199054};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FODE01000008; SEN49487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8H146; -.
DR STRING; 34002.SAMN04489859_100842; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000199054; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
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 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:UP000199054};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 28..150
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 181..236
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 389 AA; 41902 MW; 4B809EE59B889895 CRC64;
MTVLPTHILD DPALQAVLQA IGADGHRAFL VGGAVRNALL DQPVQDIDIA TDARPDQVIE
LAARAGLKSV PTGLDHGTVT VVAKGSGFEV TTFRRDVETD GRRATVAFSG DLAEDAARRD
FTMNALYADA SGQVIDPVGG LPDLHARRLR FVGQPEQRIR EDYLRILRFF RFLAWYGREA
EPSAVAACRA LRDGLDGISR ERVGQEMRKL LRAPDPCASI RLMIDTGVLD KVLPGATPLR
FFGFEALGGN GGLWLGRLAA LSQGDLTDAL RLSRHEAQGH KALVTAMAGN WSFNRIAYHL
DGTQAESAAL LVQTCDTGQA RPRNGWPEAR EAARNARLPI SARDLQPDLS GPDLGRGLKA
AEQAWIDSGF TLVAPALIST ALHAGKEDI
//
