ID B8GNB2_THISH Unreviewed; 465 AA.
AC B8GNB2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Poly(A) polymerase I {ECO:0000256|HAMAP-Rule:MF_00957};
DE Short=PAP I {ECO:0000256|HAMAP-Rule:MF_00957};
DE EC=2.7.7.19 {ECO:0000256|HAMAP-Rule:MF_00957};
GN Name=pcnB {ECO:0000256|HAMAP-Rule:MF_00957};
GN OrderedLocusNames=Tgr7_0882 {ECO:0000313|EMBL:ACL71973.1};
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL71973.1, ECO:0000313|Proteomes:UP000002383};
RN [1] {ECO:0000313|EMBL:ACL71973.1, ECO:0000313|Proteomes:UP000002383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL71973.1,
RC ECO:0000313|Proteomes:UP000002383};
RX PubMed=21475584;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
CC -!- FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which usually
CC targets these RNAs for decay. Plays a significant role in the global
CC control of gene expression, through influencing the rate of transcript
CC degradation, and in the general RNA quality control.
CC {ECO:0000256|HAMAP-Rule:MF_00957}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00957};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|HAMAP-Rule:MF_00957,
CC ECO:0000256|RuleBase:RU003953}.
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DR EMBL; CP001339; ACL71973.1; -; Genomic_DNA.
DR RefSeq; WP_012637461.1; NC_011901.1.
DR AlphaFoldDB; B8GNB2; -.
DR STRING; 396588.Tgr7_0882; -.
DR KEGG; tgr:Tgr7_0882; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_0_0_6; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000002383; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043633; P:polyadenylation-dependent RNA catabolic process; IEA:InterPro.
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 HAMAP; MF_00957; PolyA_pol; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR010206; PolA_pol_I.
DR InterPro; IPR025866; PolyA_pol_arg_C_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR NCBIfam; TIGR01942; pcnB; 1.
DR PANTHER; PTHR43051; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43051:SF1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12626; PolyA_pol_arg_C; 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_00957};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW Rule:MF_00957};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00957}; Nucleotidyltransferase {ECO:0000313|EMBL:ACL71973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002383};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00957,
KW ECO:0000256|RuleBase:RU003953};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00957};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00957}.
FT DOMAIN 57..190
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 217..279
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 336..456
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 159
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 465 AA; 52634 MW; E21E49CC7ABF9930 CRC64;
MEQHNTATPN HVSSPDASPA SPAIIPRAEH GVSRANISKS ALKVLYRLRE AGFRACLVGG
GVRDLLLGRE PKDFDVATDA HPEQVRQLFR NCRLIGRRFR LAHVQFGREI IEVATFRAPH
EVLNGDDDEE FNGDALVEDG RIIRDNVYGT IEQDAWRRDF TINALYYDIE DFSVVDYAGG
MADLKAGVLR LIGDPEVRFR EDPVRMLRAV RFAGKLGFRL DIACEQAIPR MAGLLEEVAP
ARLFDEAIKL FHSGYGLQTF EMLRRHDLFR FLFPATEEAL SHEEQGFPIT FVANALKSTD
ARIQEGKGVN PAFLYAVMLW EPVRRLADRL MENGELPWLV ALQQAGTAVL ADQCAHIAIP
KRISLPMREI WEMQPRLEQR RGARALRLMT HPRFRAAYDF YCLRAQSGEA LEEGCNWWTR
IQEVDEAEQR HMAGMDRPGG GGGGGGRRKR RRRPRRSDGN PAEPQ
//
