ID A0A2A2ADH1_9BURK Unreviewed; 579 AA.
AC A0A2A2ADH1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 ORFNames=CK625_11695 {ECO:0000313|EMBL:PAT35649.1};
OS Vandammella animalimorsus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Vandammella.
OX NCBI_TaxID=2029117 {ECO:0000313|EMBL:PAT35649.1, ECO:0000313|Proteomes:UP000218054};
RN [1] {ECO:0000313|EMBL:PAT35649.1, ECO:0000313|Proteomes:UP000218054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML00-0135 {ECO:0000313|EMBL:PAT35649.1,
RC ECO:0000313|Proteomes:UP000218054};
RA Bernier A.-M., Bernard K.;
RT "WGS of Clinical strains of the CDC Group NO-1 linked to zoonotic
RT infections in humans.";
RL Submitted (AUG-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}.
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:PAT35649.1}.
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DR EMBL; NSJB01000012; PAT35649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2ADH1; -.
DR Proteomes; UP000218054; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000218054};
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 89..238
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 268..328
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 381..497
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 13..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 109
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 207
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 579 AA; 63825 MW; 045C321EA9247D71 CRC64;
MIKQFIEKLL AKRPRQRPAA QAGQAPAASA RSARASASAT GAANAASAQR KIFGKRHEVP
VSEHGIDPSL VDRRALEVVD TLQSKGFEAY IVGGAVRDLL LGLRPKDFDV ATNATPEQVK
SLFRRAFIIG RRFRIVHVVF GRGREHEVIE VTTFRAYLDN QAADRISGNE KTSRQALAGV
QHAVDASGRV LRDNVWGSQQ EDAARRDFSI NAMYYDPRSQ IVVDYHHGID DARRRTIRMI
GEPEARYRED PVRMIRAIRF AAKLDALGFT LGSKTAQPIA ALRPLLQDIP PSRLFDEMLK
LLQTGHAMAS VAQLRALGLA KGIYPLLDLI VERADWPLVE LALRDTDRRV AEGKPVAPSF
LLACVLWDDV QRAWEREQQS GQHPSPALSH AISEVFERRV GDVSGRGKLG ADIREIWTMQ
PRFARRSGKG PYSLVQQPRF RAGLDFLRLR GRAGEAAQDW AAWWEEFSLA DDATRADMLE
QERQRSQQAK QAAESGRKAK KPRQRSAPAA GEPTTTPETE SALPEGAEPQ DHQELAQPLS
SSAKRRRRRK KSPGSTAASP AQAAAPGAAQ PPSGSAGHA
//
