ID A0A2G5KBE6_9RHOB Unreviewed; 382 AA.
AC A0A2G5KBE6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Poly(A) polymerase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BFP76_11345 {ECO:0000313|EMBL:PIB26499.1};
OS Amylibacter kogurei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Amylibacter.
OX NCBI_TaxID=1889778 {ECO:0000313|EMBL:PIB26499.1, ECO:0000313|Proteomes:UP000231516};
RN [1] {ECO:0000313|EMBL:PIB26499.1, ECO:0000313|Proteomes:UP000231516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:PIB26499.1,
RC ECO:0000313|Proteomes:UP000231516};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Amylibacter sp. strain 4G11.";
RL Submitted (AUG-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}.
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:PIB26499.1}.
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DR EMBL; MDGM01000003; PIB26499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5KBE6; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000231516; 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:UP000231516};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 27..149
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 188..235
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 382 AA; 42251 MW; F7461812309CFC42 CRC64;
MQIESEWLQH DNTQAVMSLL NDAGYEAYFV GGCVRNALLK ESATDIDIST NAHPETVMKI
AKHAGMKSIP TGIDHGTVTI VIAGDAYEIT TFRKDIATDG RRATIAFADN IIDDAKRRDF
TMNAIYADRF GKIFDPLDGL PDLLARRVRF IDDPNQRIAE DYLRILRFFR FTAWYGDTQN
GIDADGLAAC ARGMDGLKTL SRERVGSEVS KLLSAANPAP VIGAMAQTGI LAQTLLGAQH
QFLAPFVHLE QQFDVAPNWI ARLVCLTREP QDLRLARKDE NLRVNLVKLL DDNPPAHVAA
YRYGANLAYY AALILAASLE TTPPSDLSNN IALADGVEFP VKSVDLSDQL QGKSLGNALR
KLESRWIQSQ FTMTKQELLN EL
//
