ID A0A2S5KWU5_9PROT Unreviewed; 455 AA.
AC A0A2S5KWU5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=C4K68_01420 {ECO:0000313|EMBL:PPC79112.1};
OS Proteobacteria bacterium 228.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=2083153 {ECO:0000313|EMBL:PPC79112.1, ECO:0000313|Proteomes:UP000238196};
RN [1] {ECO:0000313|EMBL:PPC79112.1, ECO:0000313|Proteomes:UP000238196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=228 {ECO:0000313|EMBL:PPC79112.1,
RC ECO:0000313|Proteomes:UP000238196};
RA Krishnan R., Ramesh Kumar N.;
RT "novel marine gammaproteobacteria from coastal saline agro ecosystem.";
RL Submitted (FEB-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}.
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:PPC79112.1}.
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DR EMBL; PRLP01000005; PPC79112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5KWU5; -.
DR OrthoDB; 5288233at2; -.
DR Proteomes; UP000238196; 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}; Nucleotidyltransferase {ECO:0000313|EMBL:PPC79112.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238196};
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 51..183
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 210..271
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 330..449
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 422..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 152
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 455 AA; 52977 MW; EA4DB8B6B58601F2 CRC64;
MNTGPAHHDT VPVVPQDSRI IQRDHHSISR KDITPSALKV LYRLQEAGFD AYIVGGGVRD
LLLHLHPKDF DVATNASPEE VHRLFRNSRM IGRRFKIVHV QFGREIIEVA TFRAHHAEQE
EQGSDHSRQA ANGMLLRDNV YGTLEEDVER RDFTINALYY TTKDFCIYDY HGGISDLNSR
VVRIIGEPEA RYREDPVRML RAVRFAGKLG FDIEPVTAAP IHELAPLLAA VSNARLFDEV
LKLLSSGHGL PTWKLMWQYG LIAPMLPDTW QSLQGDDEQT VQNRMMIELA LANTDKRIAE
DRPVTPAFLY AVLLWAPLLE ELSYLQDEER MPLIPAMHEA AQRIMDRQVK HIAIPRRISS
IMREIWELQF RLPRRQGKRP DQLMEHPRFR ASYDFLRLRE ESGEDLNGLG IWWERYQEQT
DDSRRSMIQD LKENYSEPPR SKRRRRPRKR TPTNE
//
