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Database: UniProt
Entry: W5MQ36_LEPOC
LinkDB: W5MQ36_LEPOC
Original site: W5MQ36_LEPOC 
ID   W5MQ36_LEPOC            Unreviewed;       718 AA.
AC   W5MQ36;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010495.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000010495.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00024620};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC       {ECO:0000256|ARBA:ARBA00010912}.
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DR   EMBL; AHAT01003930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MQ36; -.
DR   STRING; 7918.ENSLOCP00000010495; -.
DR   Ensembl; ENSLOCT00000010510.1; ENSLOCP00000010495.1; ENSLOCG00000008632.1.
DR   eggNOG; KOG2245; Eukaryota.
DR   GeneTree; ENSGT00940000154598; -.
DR   HOGENOM; CLU_011511_1_2_1; -.
DR   InParanoid; W5MQ36; -.
DR   OMA; ESEIMIA; -.
DR   Proteomes; UP000018468; Linkage group LG7.
DR   Bgee; ENSLOCG00000008632; Expressed in larva and 13 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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   Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR007012; PolA_pol_cen_dom.
DR   InterPro; IPR048840; PolA_pol_NTPase.
DR   InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR   PANTHER; PTHR10682:SF9; POLY(A) POLYMERASE ALPHA; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          20..213
FT                   /note="Poly(A) polymerase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20750"
FT   DOMAIN          218..316
FT                   /note="Poly(A) polymerase central"
FT                   /evidence="ECO:0000259|Pfam:PF04928"
FT   DOMAIN          370..430
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   DOMAIN          424..495
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   REGION          503..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..590
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  79794 MW;  67C2B7A7E744CA02 CRC64;
     CSPVANQAVQ ALQQPTKHYG ITSPISLALP KEADLVLTQK LTEALKPYGV FEEELELQRR
     ILVLGKLNTL VKEWIRDISE TKNLPASIID NVGGKIFTFG SYRLGVHTKG ADIDALCVAP
     RHVERSDFFT SFYEKLKEQE EVKDLRAVEE AFVPVIKLSF DGIEIDILFA RLALQTIPED
     LDLRDDGLLK NLDIRCIRSL NGCRVTDEIL HLVPSIENFR LTLRAIKLWA KRHNIYSNIL
     GFLGGVSWAM LVARTCQLYP NAVASTLVHK FFLVFSKWEW PNPVLLKQPE DCNLNLPVWD
     PRVIIYPVFH KLQVCLYPHC FVNFMYHIFL NNVRPFILHF SCVLAPCNNM SYTVFFHEKC
     AYILIFKIPR HYIVLLASAP TEKQHLEWVG LVESKIRILV GNLEKNEFIT LAHVNPQSFP
     GPKEGSEKEE FSTMWVIGIA FKKMEGAENL NVDLTYDIQS FTDTVYRQAI SSKMFEPDMK
     ITAMHVKRKQ LHQLLPNLVI QKRRKHSTEG VKPVNESSLD LSLDSDNSMS VPSPTTAFSS
     SLRRLSPAAP VANSQASEGP CRGEGAGSSV SPGVPSDGTP PKPVAVAPPP KPAAARGVSS
     TPVIKRPLLA AGGSAAKPAA KRTGSPIQEE TPKKPRAEED PSESRVSGDN TAQPDVKPSV
     EMEALPGHSR ALSSTAPCPQ ENTPIFQRIP STDLSDVPLL PANPIPVVKN SIKLRLSR
//
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