ID A0A3N5XW88_9ALTE Unreviewed; 428 AA.
AC A0A3N5XW88;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:RPJ64862.1};
GN ORFNames=DRW07_18100 {ECO:0000313|EMBL:RPJ64862.1};
OS Alteromonas sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=2259342 {ECO:0000313|EMBL:RPJ64862.1, ECO:0000313|Proteomes:UP000275281};
RN [1] {ECO:0000313|EMBL:RPJ64862.1, ECO:0000313|Proteomes:UP000275281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0105 {ECO:0000313|EMBL:RPJ64862.1,
RC ECO:0000313|Proteomes:UP000275281};
RA Ye M.-Q., Du Z.-J.;
RL Submitted (NOV-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:RPJ64862.1}.
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DR EMBL; RPOK01000007; RPJ64862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5XW88; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000275281; 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:RPJ64862.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275281};
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 27..159
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 188..249
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 305..423
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 400..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..428
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 45
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 47
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 428 AA; 48895 MW; 93D4EBA1BAF748EE CRC64;
MHPVRNNMMS PNALKVTQGL QKAGFDAYLV GGCVRDVFLG VTPKDFDVVT NATPEQVKET
FRNCRVIGRR FKLAHVVFGR EIIEVATYRG HHGDDESTQG KLARSKQDEQ GQLLRDNVYG
TIEEDAERRD FNINAMYYDP HSGDVIDFAG GIAAIESGTF SLIGDAEKRY REDPVRMLRA
VRFAAKLNMQ IAEEAARPIH EMAGLLSNIP PARLYEEVLK LLLAGSAQAT YAMLQEYGLF
AVLFPQVQPF LVDETSRESQ FVQKVLHNTD TRINNNQRVT PAFLYAAILW YPLESHSNKL
MQEAGLSAHD AFNIAMGEVL HRQCQRIMIP KRFSTVIRDI WHLQRRLPKR FGKRAYQLLE
HPKFRAGYDF LLFRGEIEGG DLYELAQWWT QFQTAAPAKQ KKLLSGLKNQ GSKSHHRRRK
PKRQQHDA
//
