ID A0A1G5SAY7_9PROT Unreviewed; 456 AA.
AC A0A1G5SAY7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:SCZ84157.1};
GN ORFNames=NSMM_1080007 {ECO:0000313|EMBL:SCZ84157.1};
OS Nitrosomonas mobilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=51642 {ECO:0000313|EMBL:SCZ84157.1, ECO:0000313|Proteomes:UP000198729};
RN [1] {ECO:0000313|EMBL:SCZ84157.1, ECO:0000313|Proteomes:UP000198729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:SCZ84157.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMWO01000011; SCZ84157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5SAY7; -.
DR STRING; 51642.NSMM_1080007; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000198729; 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:SCZ84157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198729};
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..188
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 218..276
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 330..445
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 434..456
FT /note="Disordered"
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 158
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 456 AA; 52113 MW; E888BDDC1D3CA3F3 CRC64;
MIRKFLRRIF SSDTDTPSSR KNFRAIAFAE HCISRDHISR SSLRVAQTLQ QAGFSAYIVG
GAVRDLLLGL KPKDYDIATN ATPEEVRGLF RRSRIIGRRF RLVHVISRNE TVEVSTFRGN
TGHDLPQSCP AGTQTDADGR LLHDNIFGSQ EEDVLRRDFT INALFYDPTT EEIIDYLHGF
EDVRAKRLSV IGNPEQRFRE DPVRMLRAVR LASKLSIQID DRTAAPIGDL APLLRNVPPA
RLFDEMLKLL FSGHALTGVL DLRTRGLHHG LLPMLDVVLE QPLGERFITL TLKNTDERVR
QDQPVAVGFL FAALLWHEVL AAWQVRVNAG EPSIPALHQA MAEILSAQRT RLAIPRRHDS
MICAIWSMQP RFYARAGRKP FRLLEQPYFR AAYDFMLLRC ESGEIEPEIA QWWQAFKNAD
QATRESMLDA ETIPKRRRKS RSRRKDVANE KTIISQ
//
