ID B9RS15_RICCO Unreviewed; 754 AA.
AC B9RS15;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=RCOM_0801640 {ECO:0000313|EMBL:EEF45875.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ973807; EEF45875.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RS15; -.
DR STRING; 3988.B9RS15; -.
DR eggNOG; KOG2245; Eukaryota.
DR InParanoid; B9RS15; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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: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; 1.
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 Nucleotidyltransferase {ECO:0000313|EMBL:EEF45875.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF45875.1}.
FT DOMAIN 28..222
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20750"
FT DOMAIN 227..371
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 375..433
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 85138 MW; A09AB93352D4B744 CRC64;
MVDSPSPNGA TSPLQSQTTT STTNKRYGIT KPISLAGPSE ADLLRNADLV KFLVDSGLYE
SKEENLKREE VLCRIDQIVK DWIKQLTRQR GYSDQMVDEA NAVIFTFGSY RLGVHGPGAD
IDTLCVGPSY VNREEDFFIL LHDILAEMDE ITELQPVPDA HVPVMKFKFQ GISIDLLYAS
ISLPVVPEDL DISHGSVLYD VDEQTVRSLN GCRVADQILK LVPNVEHFRT TLRCLKFWAK
RRGVYSNVTG FLGGVNWALL VARLCQLYPN AIPSMLVSRF FRVYTQWRWP NPVMLCAIEE
DELGFPVWDP RRNPRDRFHH MPIITPAYPC MNSSYNVSIS TLRVMMEQFQ YGNKICEEIE
LNKAQWSALF EPYLFFEAYK NYLQIDIIAA DADDLLAWKG WVESRLRQLT LKIERDTIGM
LQCHPYPNEY IDTSKQCPHC AFFMGLQRRK GVSGQEGQQF DIRGTVEEFR QEINMYMFWK
PGMDVYVSHA RRRQLPAFVF PDGYKRSRTS RHPNQQAGKP SDVSATSRAG SVEGHLKRKN
DHEVVDVRPD KPEKRASVSP QRLQSVSPES NTISSGRTSL VSFCEGVPLE SSTVADVDSN
SEGKLDRGHS DNGKVTFRGV VQVTETINHD PRISAQTSMD LDDIPIYLSK VEEAECKIMN
PDPKQELLDP YATSNSINGE APKTMGEDRI GDLGDILAAD SDSLLETDCL DVSRLSQSGL
LENLEPNTEM VKVVNSQDGA RSESLQKPVI RHAF
//