ID A0A2S2FHS7_9GAMM Unreviewed; 484 AA.
AC A0A2S2FHS7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ECO:0000313|EMBL:AWL29922.1};
GN ORFNames=DJ533_15770 {ECO:0000313|EMBL:AWL29922.1};
OS Acinetobacter defluvii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1871111 {ECO:0000313|EMBL:AWL29922.1, ECO:0000313|Proteomes:UP000245977};
RN [1] {ECO:0000313|Proteomes:UP000245977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA30 {ECO:0000313|Proteomes:UP000245977};
RA Hu Y., Qin J., Feng Y., Zong Z.;
RT "The complete genome of Acinetobacter defluvii strain WCHAD010030.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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; CP029397; AWL29922.1; -; Genomic_DNA.
DR RefSeq; WP_065994383.1; NZ_CP029397.2.
DR AlphaFoldDB; A0A2S2FHS7; -.
DR STRING; 1871111.GCA_001704615_00472; -.
DR KEGG; adv:DJ533_15770; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000245977; 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:AWL29922.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245977};
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 34..159
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 186..247
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 296..408
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 399..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 54
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 128
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 484 AA; 55291 MW; 77FD23B07B95FBF3 CRC64;
MQTLRASKCG LSTAQLPSSI LDVIDSLTKA GYEAYIVGGG VRDLMLGQSP KDYDAVTNAT
PSQVKEVFGR RCRIIGRRFE LAHVYSGREL IEVATFRAPP KKAITSAAGM ILRDNNWGTI
EQDFSRRDFS INALYYQPRK GIVLDFCNAV DDIKSKTLRL LGDPALRFEE DPVRMLRTLR
FAAKLNFNID PAILEVFTLE MTQLLRDVSP HRLYDESQKL FTMGHLSQVM PMLIDFDIWQ
QLFADLKTEI TPFMARAAKN TDQRIQIGKT INPAFFYAVL LWENFLRRCD FYQAKGVVAA
EARAQAGLDV LKRQATRTII PRFAETFIRE VWEMQTRLLN PKPQQIEALS GHARFRAGFD
FLLLREKSGD PSTQGMGAWW EAYQTMSTDE KERAISSYNR QRAKNRRKVT TEEPVESKVS
AQIEPLVKEA ETRSRRSRKA PVEEKKSLTN VVSHQTDSIH PDHPILKRKR VQRDLSNVIF
GPTQ
//
