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
//