ID V4J4T1_9GAMM Unreviewed; 443 AA.
AC V4J4T1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=N838_02525 {ECO:0000313|EMBL:ESQ09419.1};
OS Thiohalocapsa sp. PB-PSB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ09419.1, ECO:0000313|Proteomes:UP000017935};
RN [1] {ECO:0000313|EMBL:ESQ09419.1, ECO:0000313|Proteomes:UP000017935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA Orphan V.J.;
RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT consortia of the Sippewissett salt marsh.";
RL Submitted (AUG-2013) 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:ESQ09419.1}.
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DR EMBL; AVFR01001255; ESQ09419.1; -; Genomic_DNA.
DR AlphaFoldDB; V4J4T1; -.
DR PATRIC; fig|1385625.5.peg.7534; -.
DR Proteomes; UP000017935; 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:UP000017935};
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 37..171
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 199..261
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 315..426
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT ACT_SITE 55
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 57
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 443 AA; 50059 MW; 594CF6B609375E03 CRC64;
MPTPLIVPRP EHTISRANIS QNALKVLYRL SQAGHQAFLV GGGVRDLLLG HEPKDFDIAT
DATPEQVRSV FRNCRLIGRR FRLAHVFFGS EIIEVATFRG APAAQDTDPN SDAGDRLVEN
GIILRDNVYG TIAEDALRRD FTINALYYNI ADFSLVDYAG GLDDIRDGRL RLIGGDAEAR
YREDPVRMLR AVRFACKLGF MIEPSCEAPL THMAPLLSEV PAARLFEEIL KLFHSGYALN
AFEKLRHYGL FARLFPETDQ ILARQDHDFP ITFVSRGLDN TDQRIAAGKS VAPQFLFAML
LWEPVRLRCQ QLLDQGLAWP EAMALASHEV ASRQQRRIAI PKRFGLPMRE IWSLQPRLER
RQGKRSMALI GHPRFRAAYD FLLLRAEAGE VDAEVAEWWT RFQDVDAAER ARMSGGTKRK
RRRRRKTSTA EAGGEVTSDH PSA
//
