ID A0A221KH69_VITFI Unreviewed; 517 AA.
AC A0A221KH69;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=VITFI_CDS2538 {ECO:0000313|EMBL:ASM78315.1};
OS Vitreoscilla filiformis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Vitreoscilla.
OX NCBI_TaxID=63 {ECO:0000313|EMBL:ASM78315.1, ECO:0000313|Proteomes:UP000199729};
RN [1] {ECO:0000313|EMBL:ASM78315.1, ECO:0000313|Proteomes:UP000199729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15551 {ECO:0000313|EMBL:ASM78315.1,
RC ECO:0000313|Proteomes:UP000199729};
RA Contreras S., Sagory-Zalkind P., Blanquart H., Iltis A., Morand S.C.;
RT "Complete Genome Sequence of the cosmetic ferment Vitreoscilla filiformis
RT (ATCC15551).";
RL Submitted (JUL-2017) 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; CP022423; ASM78315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221KH69; -.
DR KEGG; vff:VITFI_CDS2538; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000199729; 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:ASM78315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199729};
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 66..215
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 242..304
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 361..494
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 460..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 84
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 86
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 184
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 517 AA; 56990 MW; 1CE5D3EFB64ED33B CRC64;
MIRKFIKKLL GKAEAPAPET VAPPVPVIPL GQRVDVPVAA HGIDPKLLDD RAIKVVTTLQ
DAGHAAYIVG GAVRDLLVGR RPKDFDVATD ATPEQVKALF KRAFIIGRRF RIVHVVHGRG
REHEVIEVST FRAYLDASAA EQVSGNERSA KQDMAGKSHV VDASGRVLRD NVWGPQIEDA
ARRDFTVNAM YYDPRTQTVV DYHQGLADAQ ARVLRMIGDP PTRYREDPVR ILRVVRFAAK
LGFSIEPATL APLREMAPLL RNVPASRMFD EMLKLLQTGH ALASLAQLKA LGLDRGIFPV
LDAALADAPE GSERARFIEL ALQDTDRRVQ QGRAVAPSFL LACLLWHEVS QRWAVLRADS
EQPIAALSQA IEAVFEARVG DLSGRGKLAT DMREIWMMQP RFDRRGGRQP FSLVEQPRYR
AGYDFLRLRA DAGEASSDLA DWWEDFALGS DADREALQDT VRQVPRASRK AARPAAPAPA
APVAEGDVSE AEAQRKRRRR RRKPAGAEGN APAGDAP
//
