ID W1N666_9GAMM Unreviewed; 469 AA.
AC W1N666;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=BJB45_19040 {ECO:0000313|EMBL:ERL51067.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL51067.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL51067.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL51067.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
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:ERL51067.1}.
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DR EMBL; AVBC01000034; ERL51067.1; -; Genomic_DNA.
DR RefSeq; WP_021819215.1; NZ_CP013106.1.
DR AlphaFoldDB; W1N666; -.
DR STRING; 1178482.AR456_19225; -.
DR KEGG; hhu:AR456_19225; -.
DR PATRIC; fig|1178482.3.peg.2263; -.
DR eggNOG; COG0617; Bacteria.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000019113; 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:UP000019113};
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 65..195
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 222..283
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 337..457
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 431..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 85
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 469 AA; 53425 MW; F9329E376DED5EC9 CRC64;
MIKGFTRFLQ SPSEHFRSLF GPQEAAAGPP TPRVIHRDEH PISRSQFSDA ALKVLYRLHN
SGYDAFLVGG CLRDSLLGMT PKDFDVATNA TPEQVKQLFR NSRIIGRRFR IVHVRFGREV
IEVTTFRGKP SDDHADHIAA QSDAGLLLRD NVWGNIEEDA LRRDFTINAL YYSIADFSIH
DFAGGLDDIE SRTLRLIGDP ATRYREDPVR MLRAIRFAAK LDFNLAPATE APIHDLAPLL
LQIPPARLFD ELLKLFLSGD GLATYRLLRE YGLFAMLFPE ADECIDELPW FESLIEQALT
STDQRIRDDR PVTPAFLLAA FMWGPVQRRQ ADIEADGMPS VPALQAAAQQ VISRELKHVS
IPKRFSMPMR DIWDLQQRLP QRRGKRAFQT REHPRFRAAY DFLLLREAAG ELEPGLGDWW
TAFQQADDHE QRRLLGKVGV DPASSPGPRK RRRRRRKPRS DSSTPPSSE
//
