GLD2_DANRE
ID GLD2_DANRE Reviewed; 489 AA.
AC Q503I9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Poly(A) RNA polymerase GLD2 {ECO:0000250|UniProtKB:Q6PIY7};
DE EC=2.7.7.19;
DE AltName: Full=PAP-associated domain-containing protein 4;
GN Name=tent2 {ECO:0000250|UniProtKB:Q6PIY7};
GN Synonyms=papd4 {ECO:0000250|UniProtKB:Q6PIY7}; ORFNames=zgc:110560;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP
CC monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In
CC contrast to the canonical nuclear poly(A) RNA polymerase, it only adds
CC poly(A) to selected cytoplasmic mRNAs. May not play a role in
CC replication-dependent histone mRNA degradation (By similarity).
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
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DR EMBL; BC095312; AAH95312.1; -; mRNA.
DR RefSeq; NP_001018436.1; NM_001020600.1.
DR AlphaFoldDB; Q503I9; -.
DR SMR; Q503I9; -.
DR STRING; 7955.ENSDARP00000096574; -.
DR PaxDb; Q503I9; -.
DR GeneID; 553626; -.
DR KEGG; dre:553626; -.
DR CTD; 167153; -.
DR ZFIN; ZDB-GENE-050522-536; tent2.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; Q503I9; -.
DR OrthoDB; 803033at2759; -.
DR PhylomeDB; Q503I9; -.
DR PRO; PR:Q503I9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0034062; F:5'-3' RNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0070566; F:adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:2000626; P:negative regulation of miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0043489; P:RNA stabilization; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..489
FT /note="Poly(A) RNA polymerase GLD2"
FT /id="PRO_0000341552"
FT DOMAIN 386..440
FT /note="PAP-associated"
FT REGION 93..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 489 AA; 55562 MW; E8C2FA195F44B8E3 CRC64;
MLPRPYIFSH NDGPSSHLFQ HVLPHNVSQQ QRIEAHLNST NNFIGPPMNA PRFIPTYQWT
PVELSDVACS PNGPMGNNRK RRIQDNSDIN LKRQRFSCPS PHNQSARNSN FTSQPVTRPV
TGREVTCPTC SSATFIPGGC VPSLGETCHQ NAFSPSSVKD KLSQQILNLF FACEQQSDDL
EKKESCRAAL QTDIQKIFPC AKVFLGGSSL NGFGSRSSDA DLCLVIEEGP VNHRKDAVYV
LSLVRKLLYK LSYIEKPQLI RAKVPIVKFR DRISGVEFDL NFNNTVGIRN TFLLRTYAFV
EKRVRPLVLV IKKWANHHCI NDASRGTLSS YTLVLMVLHY LQTLPEPVIP CLQRDYPTCF
DPKMDIHLVP SGPSDIPAFV SRNQSSLGDL FLGFLRYYAT VFKWDKQVIS VRMARTLPKS
NCKEWKDKFI CVEEPFNRTN TARAVHERMK FEAIKAAFIE SHRLLQLRKD LNFILPKSKQ
MARPQTAPR