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Database: UniProt
Entry: A0A150WK36_BDEBC
LinkDB: A0A150WK36_BDEBC
Original site: A0A150WK36_BDEBC 
ID   A0A150WK36_BDEBC        Unreviewed;       397 AA.
AC   A0A150WK36;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Poly A polymerase {ECO:0000313|EMBL:KYG64082.1};
GN   ORFNames=AZI86_14865 {ECO:0000313|EMBL:KYG64082.1};
OS   Bdellovibrio bacteriovorus.
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=959 {ECO:0000313|EMBL:KYG64082.1, ECO:0000313|Proteomes:UP000075320};
RN   [1] {ECO:0000313|EMBL:KYG64082.1, ECO:0000313|Proteomes:UP000075320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R0 {ECO:0000313|EMBL:KYG64082.1,
RC   ECO:0000313|Proteomes:UP000075320};
RA   Ploux O.;
RL   Submitted (MAR-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:KYG64082.1}.
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DR   EMBL; LUKE01000003; KYG64082.1; -; Genomic_DNA.
DR   RefSeq; WP_061836048.1; NZ_LUKE01000003.1.
DR   AlphaFoldDB; A0A150WK36; -.
DR   Proteomes; UP000075320; 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:UP000075320};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          31..151
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          178..236
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
SQ   SEQUENCE   397 AA;  44594 MW;  B77119D7057347B5 CRC64;
     MATVQSILET HPHWPAVEDI YHKLGARGYK AFLAGGCVRD ALLGISANDL DVATDATPEE
     IEKIFANTVA VGKSFGVMRV LIGDADIEVA TFRSDGEYKD GRRPEGVHFS TPEMDAQRRD
     FTVNALFYDL NSQEVLDFVQ GKADLAKKTL RTVGDAEKRF AEDHLRLLRA ARFVGQLDFA
     LEVTTFAALK RMAPKVMTVS GERLHEEMGK LLRTAAVQKG LDVLVSSGLM AELFPFRAED
     ANGEYLSLAH HTWQSFALFF RQAPLTEVKS QLARLRFSVK EQRAIERVWG LWHQPEEFFK
     LSLAKQLLKM SEEGVPWALT ILKAQKKFLS EIDLLTNAWA KMGETLPKPF LSGTDVQGLQ
     GKAIGDCLAE AFELQLEHKH RSREEALEWL KSYKKKA
//
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