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Database: UniProt
Entry: A0A1Y1R7W4_9GAMM
LinkDB: A0A1Y1R7W4_9GAMM
Original site: A0A1Y1R7W4_9GAMM 
ID   A0A1Y1R7W4_9GAMM        Unreviewed;       465 AA.
AC   A0A1Y1R7W4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-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   ORFNames=B0D91_01380 {ECO:0000313|EMBL:OQX39532.1};
OS   Oceanospirillales bacterium LUC14_002_19_P2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX   NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX39532.1, ECO:0000313|Proteomes:UP000192421};
RN   [1] {ECO:0000313|EMBL:OQX39532.1, ECO:0000313|Proteomes:UP000192421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX39532.1};
RA   Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT   "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL   Submitted (FEB-2017) 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:OQX39532.1}.
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DR   EMBL; MUIA01000067; OQX39532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1R7W4; -.
DR   Proteomes; UP000192421; 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:0006378; P:mRNA polyadenylation; IEA:InterPro.
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:UP000192421};
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..198
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          225..285
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
FT   DOMAIN          339..458
FT                   /note="Polymerase A arginine-rich C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12626"
FT   REGION          441..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..465
FT                   /note="Basic residues"
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        167
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ   SEQUENCE   465 AA;  53831 MW;  C38BDDED29F6C5CA CRC64;
     MTGKRSGFIH RLFSYVTGKQ SDTQPQAPVP TLSILPRDQH TISRRHISDN ALKVLHRLNS
     HGYQAYLVGG CIRDLMLDLH PKDFDIATDA TPEDVRGLFR NSRIIGRRFK LIHVVFGREV
     IEVATFRASH RAEDDEHDSS VSHHSQKGRI LRDNVYGTIE DDAIRRDFTM NSLYYTTTDF
     SIHDYCGGVQ DIHDRTIRLI GDPETRYRED PVRMLRAIRF AAKLDFHIAD NTAAPISQLA
     HLLKDIPAAR LFDEVLKLFL SGRAESTYYL LQDYHLFESL FPVTQPSLKE TPEFVQIIIN
     ALHNTDLRIQ EDKPVTPAFF FAAMLWPALV RVRDRYQNEG MPPVPALQQA ATQVISQQCR
     RTAVPKRFTI PMREIWEMQS RLECRQPRRV DELATHPRFR AAYDFLLLRE QSGETIGDAG
     QWWTDYQTSS RDDDRQALLK QLLSVPGNKR KRRRRRPRKR PGNPA
//
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