ID K1JVK4_9BURK Unreviewed; 479 AA.
AC K1JVK4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=HMPREF9465_01730 {ECO:0000313|EMBL:EKB30683.1};
OS Sutterella wadsworthensis 2_1_59BFAA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB30683.1, ECO:0000313|Proteomes:UP000005835};
RN [1] {ECO:0000313|EMBL:EKB30683.1, ECO:0000313|Proteomes:UP000005835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB30683.1,
RC ECO:0000313|Proteomes:UP000005835};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL Submitted (MAY-2012) 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:EKB30683.1}.
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DR EMBL; ADMG01000037; EKB30683.1; -; Genomic_DNA.
DR AlphaFoldDB; K1JVK4; -.
DR STRING; 742823.HMPREF9465_01730; -.
DR PATRIC; fig|742823.3.peg.1725; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_0_0_4; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000005835; 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:UP000005835};
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 56..181
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 208..268
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 322..441
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 424..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 76
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 150
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 479 AA; 54474 MW; 175123DD5FBEEEB0 CRC64;
MFGRIVNRVR DMFAPRSVVV KNPRVISADE HRIDPALVSA EARATCEALK RRGFQAYIVG
GAVRDLMLGV TPKDFDVATD ATPEQVKRCQ RRAVIIGRRF KLVHVIFGRE VIECSTFRAL
EGAGQRKDAT GRVVSDNVFG EMWEDAARRD FTINALYYDP QTQELFDYHR GFEDLAAKRL
RMIGDPAERY REDPVRMMRA VRIAAKLGFT IEPATEAPIP KMAKLLENVP SARLVDEVLK
LLTSGHAVAC LSKLRQEGLH KALLPLLDVI VSEPDGEEFL MLALKRTDER IAVGKKISPS
FLFGTLLWPQ VVKRWRYNED EKGMSRMAAL HAACVDVLAT QCQQLNIQRR YQADIHDLWM
LQARFERRTG KTAYALVSHP RYRAAYDFML LRSLLGHVPE SLVQWWDAFA LSDEETRAGM
IAEAQREARM TGDAARSHRR RAASAGGETP AEDGERRSSR RRRRSPRRSS RSRQERSDA
//
