ID   A0A0E0AAW6_9ORYZ        Unreviewed;       702 AA.
AC   A0A0E0AAW6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G19560.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM06G19560.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM06G19560.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0AAW6; -.
DR   EnsemblPlants; OGLUM06G19560.1; OGLUM06G19560.1; OGLUM06G19560.
DR   Gramene; OGLUM06G19560.1; OGLUM06G19560.1; OGLUM06G19560.
DR   HOGENOM; CLU_011511_4_4_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
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:SF36; NUCLEAR POLY(A) POLYMERASE 4; 1.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 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:UP000026961};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          21..215
FT                   /note="Poly(A) polymerase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20750"
FT   DOMAIN          219..343
FT                   /note="Poly(A) polymerase central"
FT                   /evidence="ECO:0000259|Pfam:PF04928"
FT   DOMAIN          346..405
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   DOMAIN          406..480
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   REGION          472..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  77551 MW;  ECA749F6070CBD91 CRC64;
     MAACNAATAA AVAEQPQKQY GITKPISLAE PAEVDLQKTA DLEKFLVEAG LYESPEESAR
     REEVLGELDK IVKDWVKQLT SQRGYTDQMV EEANAVLFTF GSYRLGVHGP GADIDTLCVG
     PSYVNREEDF FIVLHDILAQ TEEVTELQPV PDAHVPVMKF KFHGISIDLL YASVSLLVVP
     PDLDISQGSV LYDVDEVTVR SLNGCRVADQ ILRLVPNVEV TGFLGGVNWA LLVARVCQLY
     PNAVPSMLVS RFFRVFTQWQ WPNPVMLCAI EEDELGFPVW DPRKYHRDRS HHMPIITPAY
     PCMNSSYNVS TSTLRVMMEQ FQFGNKICQE IDISKANWSA LFEPFQFFEA YKNYLQVDII
     AEDGEDLRLW KGWVESRLRQ LTLKIERDTY GMLQCHPYPH EYADPSRQCA HCAFFMGLSR
     KEGAKIQEGQ QFDIRGTVDE FRHDIGMYGY WRPGMELAVS HVRRKQIPSY VFPEGYKRPR
     PSRHINHPQQ SNKNDVEDGT ANRSPDGQPK RKHDTAGVYD SEPGRSVKRA SISPSISPVH
     QKTSSPPSGN IADASGASGG SPVSLANGNL EQANCLNSPL ASEKSLDSVT SGSKCVGVEA
     VCPSDATKEH DNCGSNMKNC TTTTVAVSLK RVAEKVVSEL VGSESLGGNK SGELLERAED
     MGSALVENVH FGGNGVVQTG LPEELEPNNG IEVVSKAHAG LV
//