UniProt: A0A2I5THZ5

Database: UniProt
Entry: A0A2I5THZ5_SERS3

LinkDB:  A0A2I5THZ5_SERS3 
Original site:  A0A2I5THZ5_SERS3

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (2)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (8)   
   InterPro (5)   
   Pfam (3)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   A0A2I5THZ5_SERS3        Unreviewed;       485 AA.
AC   A0A2I5THZ5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=CWC46_08625 {ECO:0000313|EMBL:AUG99865.1}, Ser39006_008630
GN   {ECO:0000313|EMBL:AUH04185.1};
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=104623 {ECO:0000313|EMBL:AUH04185.1, ECO:0000313|Proteomes:UP000017700};
RN   [1] {ECO:0000313|EMBL:AUH04185.1, ECO:0000313|Proteomes:UP000017700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH04185.1}, and ATCC 39006 / SC
RC   11482 {ECO:0000313|Proteomes:UP000017700};
RX   PubMed=24336377; DOI=10.1128/genomeA.01039-13;
RA   Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA   McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA   Brugger K., Brown S.D., Salmond G.P.;
RT   "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT   for analysis of the biosynthesis and regulation of prodigiosin, a
RT   carbapenem, and gas vesicles.";
RL   Genome Announc. 1:E01039-E01039(2013).
RN   [2] {ECO:0000313|EMBL:AUH04185.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH04185.1};
RA   Wang G., Yang Y., Su Y.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AUG99865.1, ECO:0000313|Proteomes:UP000233778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUG99865.1,
RC   ECO:0000313|Proteomes:UP000233778};
RA   Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA   Fineran P.C.;
RT   "Complete genome sequence of Serratia sp. ATCC 39006 LacA.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUH04185.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH04185.1};
RA   Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA   Fineran P.C.;
RT   "Complete genome sequence of Serratia sp. ATCC 39006.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP025085; AUG99865.1; -; Genomic_DNA.
DR   EMBL; CP025084; AUH04185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I5THZ5; -.
DR   STRING; 104623.Ser39006_03729; -.
DR   KEGG; sera:Ser39006_008630; -.
DR   KEGG; serq:CWC46_08625; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000017700; Chromosome.
DR   Proteomes; UP000233778; 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:AUH04185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017700};
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          81..214
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          241..301
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
FT   DOMAIN          359..478
FT                   /note="Polymerase A arginine-rich C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12626"
FT   REGION          456..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..485
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ   SEQUENCE   485 AA;  56281 MW;  EDFF0463FFE62A2C CRC64;
     MISRYFYCTV NSSSLSRCII FTRVANFCRK VLNRENEMAE SGTEPQPLTV IPRDQHTISR
     RDISENALKV LYRLNKAGYE AYLVGGGVRD LLLGKKPKDF DITTNATPEQ VRKLFRNCRL
     VGRRFRLAHV MFGSEVIEVA TFRGHHEQNG EPQIKNAAQR DQNGMLLRDN IFGTIEEDAQ
     RRDFSINSLY YSISDFTVRD YTNGMSDLRQ GIIRMIGEPE TRYREDPVRM LRAVRFAAKL
     NMKLSPETAE PIPRLAALLH DIPSARMFEE SLKLLQAGYG YPTYVMLCQY QLFQPLFPLI
     SSHFTEEGQT NLERMIIQVL KNTDQRIQND MRVNPAFLFS AMLWYPLIEH AQKLTQESGL
     AYFEAFALAM NDVLDEQCRS LSIPKRITSL IRDIWQLQLR LSRRQGKRAY KLMEHPKFRA
     AYDLLALRAD IEHHPELQRL TQWWGEFQVA PPPRQQVMLN SLDDGPTPHR RSRRPRKRPA
     APGKS
//

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