ID A0A445BU27_ARAHY Unreviewed; 716 AA.
AC A0A445BU27;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=Ahy_A08g038698 {ECO:0000313|EMBL:RYR42219.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR42219.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR42219.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR42219.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYR42219.1}.
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DR EMBL; SDMP01000008; RYR42219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445BU27; -.
DR OrthoDB; 1351913at2759; -.
DR Proteomes; UP000289738; Chromosome a08.
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:UP000289738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 26..220
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20750"
FT DOMAIN 225..369
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 373..432
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT DOMAIN 432..505
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 514..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 81168 MW; D2E05CE0644AE622 CRC64;
MVVSDAPNGG GSSSPPLVVE QTNTLGITKP ISLAGPTDAD LHRNAELEKF LLDSGLYESN
EEAATRREVL QRLDQTVKSW VKQLTRQRGY TDQMVEDANA VIFTFGSYRL GVHGPGADID
TLCVGPSYVN REEDFFIILH NILAEMEEVT ELQPVPDAHV PVMKFKFQGI SIDLLYASIS
LLVVPEDLDI SHGSVLYDVD EPTVRSLNGC RVADQILKLV PNVEHFRTTL RCLKFWAKRR
GVYSNVTGFL GGVNWALLVA RICQLYPNAI PSMLVSRFFR VYTQWRWPNP VMLCTIEENE
LGFPVWDPRR NPRDRYHIMP IITPAYPCMN SSYNVSASTL RVMKEQFRYG NKICDEIELS
KAQWSALFQP YFFFEAYKNY LQVDILAADT DDLLAWKGWV ESRLRQLTLK IERDTNGMLQ
CHPYPHEYAD TSRHCAHSAF FMGLQRKEGE KGQEGQQFDI RGTVDEFRQE INMYMYWKPG
MEIFVSHVRR KQLPLFVFPD GYKRNRMSRH ISHSAEKMGE DAAKSNLGSS ERSVKRKNDH
EMLDEKLGKP EKRASISPQR LVCVSPESCS SQMSIDGTKG VRLAKNAGTK CEIKSSNGLL
ENGISTEGAY VHLSETGGVH PKNDSQNSRC SEVQNENGVD RNKAGEMDLD CLESAETASS
KSLSNCKESA VDMDQRLDNT HNFQRTEYSD YVPTASSQAL NCEEDEFELN HMTFGR
//
