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Database: UniProt
Entry: A0A1N7EIU1_9RHOB
LinkDB: A0A1N7EIU1_9RHOB
Original site: A0A1N7EIU1_9RHOB 
ID   A0A1N7EIU1_9RHOB        Unreviewed;       385 AA.
AC   A0A1N7EIU1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Poly(A) polymerase {ECO:0000313|EMBL:SIR87888.1};
GN   ORFNames=SAMN05421666_0274 {ECO:0000313|EMBL:SIR87888.1};
OS   Roseovarius nanhaiticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=573024 {ECO:0000313|EMBL:SIR87888.1, ECO:0000313|Proteomes:UP000186019};
RN   [1] {ECO:0000313|EMBL:SIR87888.1, ECO:0000313|Proteomes:UP000186019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29590 {ECO:0000313|EMBL:SIR87888.1,
RC   ECO:0000313|Proteomes:UP000186019};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTNV01000001; SIR87888.1; -; Genomic_DNA.
DR   RefSeq; WP_076530305.1; NZ_FTNV01000001.1.
DR   AlphaFoldDB; A0A1N7EIU1; -.
DR   STRING; 573024.SAMN05216208_1860; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000186019; 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:UP000186019};
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          186..238
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
SQ   SEQUENCE   385 AA;  41056 MW;  F88FEFF71336EBDB CRC64;
     MRIEEAWLTE APLVTIFDAF EAAGHRVYLV GGAVRNALLG EPVGDLDLAT DAVPEQMMQL
     AEAAGIKAIP TGIGHGTVTL VLQGTPFEIT TFRQDVETDG RHATVDFTDD ITRDARRRDF
     TMNALYVGAD GTVIDPLGGL PDVMARRVRF IEDAGTRIRE DYLRILRFFR FHAQYGGARG
     MDSDGLAAVA DNLDGLDGLA RERVGSEVLR LLAAPDPAPA VAAMDRVGVL TRLLPGADSR
     ALAPLIHLEA EAGSIGPDSV RRLAALGGED AQGHLRLSNA DSARLDVLKG GLGDMTSPEV
     LGYLNGAEAA RDILLLRAAI FEQPLDPGAL AAANHGARQR FPIVAADLMP AYQGAALGAR
     LRALEARWIA SRFTLGRDDL LEESA
//
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