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Database: UniProt
Entry: B9RS15_RICCO
LinkDB: B9RS15_RICCO
Original site: B9RS15_RICCO 
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
//
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