ID A0A061GIW2_THECC Unreviewed; 801 AA.
AC A0A061GIW2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=TCM_037229 {ECO:0000313|EMBL:EOY29805.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY29805.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY29805.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001887; EOY29805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061GIW2; -.
DR EnsemblPlants; EOY29805; EOY29805; TCM_037229.
DR Gramene; EOY29805; EOY29805; TCM_037229.
DR Proteomes; UP000026915; Chromosome 9.
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:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..215
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20750"
FT DOMAIN 220..364
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 368..426
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT DOMAIN 428..501
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 90220 MW; 153F86FF3673146A CRC64;
MDTRSPNGSS PQQSQSLKKY GITKPISLAG PSEADVQRNT ELEKFLIESG LYESKEEAVK
REEVLGHINE IVKSWVKQLT RQRGYTDQMV EEANAVIFTF GSYCLGVHGP GADIDTLCIG
PSYVNREEDF FIILHDILAE MEEVTELQPV PDAHVPVMKF KFQGISIDLL YASISLLVVP
DNLDISHGSV LHNVDEQTVR SLNGCRVADQ ILKLVPNVEH FRMTLRCLKF WAKRRGVYSN
VTGFLGGVNW ALLVARVCQL YPNAIPSMLV SRFFRVYTQW RWPNPVMLCS IEEDELGFPV
WDPRKNPRDR FHHMPIITPA YPCMNSSYNV SISTLRVMME QFQCGNRICE EIELNKSQWN
ALFEPYLFFE AYKNYLQVDI VSAEADDLLA WKGWVESRLR QLTLKIERDT NGMLQCHPYP
NEYVDTSKQF PHCAFFMGLQ RKEGVSGQEG QQFDIRGTVD EFRQEISMYM YWKPGMDIYV
SHVRRRQLPA FVFPDGYKRP RSSRHPGQQT GKICEDITRS QSGSVERQIK RKHEDEAFDE
KMDKPDKRSS ISPQRLESVS PESSASRSGG TSHISDGQMV TLERPTTWDV DSNSVLRQSS
GLLDSEKRNV GISIQQARTV DQGSLTLSGQ TSLDVVHNLS VVRNVESAEQ MGEPFLRQES
HSPCEVPDSE LRETCKTGVN QEKTGDYSSA YMNDAETGSS RRILNWKGGG VGVDQEVVKP
CNQTAVVEIA ESVFGSSSNA QNLNCEGVVC SADLDSLLEN GHLNANGVFQ NSLSEELKPN
IALGKVVNSQ DGARLSLKSM A
//
