ID D5CQ21_SIDLE Unreviewed; 447 AA.
AC D5CQ21;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=Slit_0947 {ECO:0000313|EMBL:ADE11185.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE11185.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE11185.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE11185.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) 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; CP001965; ADE11185.1; -; Genomic_DNA.
DR RefSeq; WP_013029083.1; NC_013959.1.
DR AlphaFoldDB; D5CQ21; -.
DR STRING; 580332.Slit_0947; -.
DR KEGG; slt:Slit_0947; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_0_0_4; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000001625; 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:ADE11185.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001625};
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 55..181
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 208..269
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 322..436
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 415..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 150
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 447 AA; 51046 MW; 69D922B519971A99 CRC64;
MIKRLIKRVF GKTVPVRVAG AAHVIPFELH KVSRDGISYG ARRVTDGLQA AGFKAFVVGG
AVRDLLLDRQ PKDFDVATDA TPEEVKRVFR RARIIGRRFR LVHVMFGEET VEVSTFRRAI
DAEDAETDEH GRILRDNEFG DQEQDAARRD FTANGLFYDP ATQEIFDYHH GYEDIRANTL
RMIGDPEVRY REDPVRMLRA VRLSAKLGMK LDPATAAPIS KMKELLSNVP EARLFDEMLK
LLLSGQALPC IKKLRAMELH HGMLPMLDVI LEQPMGEKFV MLALQNTDQR IAEEKPTSPA
FLFAALLWHE VLAAWKARQD AGERPVGAMH AAMDEVLDRQ RAQLAIPRRY DTVMKELWLL
QPRFEQRGGQ RPLRLLALPR FRAAYDFLLL RCQSGEVDAE LGAWWEEFQH ASDERRNEML
LPDSGGPKKR RRRNKKPAAA QAELPID
//
