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   27-MAR-2024, entry version 84.
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.ENSDARP00000138757; -.
DR   PaxDb; 7955-ENSDARP00000096574; -.
DR   GeneID; 553626; -.
DR   KEGG; dre:553626; -.
DR   AGR; ZFIN:ZDB-GENE-050522-536; -.
DR   CTD; 167153; -.
DR   ZFIN; ZDB-GENE-050522-536; tent2.
DR   eggNOG; KOG2277; Eukaryota.
DR   InParanoid; Q503I9; -.
DR   OrthoDB; 1080369at2759; -.
DR   PhylomeDB; Q503I9; -.
DR   PRO; PR:Q503I9; -.
DR   Proteomes; UP000000437; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; ISS:UniProtKB.
DR   GO; GO:0031124; P:mRNA 3'-end processing; 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   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF40; POLY(A) RNA POLYMERASE GLD2; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 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
//