ID A0A3B4T5C7_SERDU Unreviewed; 793 AA.
AC A0A3B4T5C7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000001275.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000001275.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000256|ARBA:ARBA00024620};
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; A0A3B4T5C7; -.
DR Ensembl; ENSSDUT00000001327.1; ENSSDUP00000001275.1; ENSSDUG00000000912.1.
DR GeneTree; ENSGT00940000156467; -.
DR Proteomes; UP000261420; Unplaced.
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; POLY A POLYMERASE; 1.
DR PANTHER; PTHR10682:SF6; POLY(A) POLYMERASE GAMMA; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..212
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20750"
FT DOMAIN 217..361
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 364..430
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT DOMAIN 424..504
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 508..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87954 MW; 5709C2A7D953211F CRC64;
MKEMSSTMPG GQQPQKHYGI TSAISLAPPR EIDHQYTKKL CDAMKPFGVF EDEEELNHRL
AVLGKLNNFV KEWIAEISEL KNLPPSAISC VGGKIFTFGS YRLGVHTKGA DIDALCVAPR
HVERSDFFQS FFEKLKQHEE IKDLRAVEDA FVPVIKFKFD GIEIDLLFAR LALQSIPDNL
DLRGDSILRN LDIRCIRSLN GCRVTDEILY LVPNKENFRL TLRAIKLWAK RRGIYSNMLG
FLGGVSWAML VARTCQLYPN AVAATLVHKF FLVFSKWEWP NPVLLKQPED SNLNLPVWDP
RVNPSDRYHL MPIITPAYPQ QNSTYNVSTS TRTIMSEEFK YGLSVTDEIL QGKAEWSKLF
EPPSFFQKYK HYIVLTASAS TEENHLEWIG LVESKIRVLV GNLERNEYIT LAHVNPQSFP
GSKENRNEND FVSMWFIGII FKKVENAESV NIDLTYDIQS FTDTVYRQAN NINMLKDGMK
IEATHVKKKQ LHQYLPPELV QKKKRSIAEL NRSSNGGSSK RISLDSSHLD SSRDTDSGTP
FSSPANKPSK PASDTDDGAS PPKQLFVEGS PSPSAAPAAK DQGMSIPVIG STSSSVTPVL
SSSVKPNATS SPREEPNGLE DSVNGAPTKR PHSPTQEDLA KRLKDTETPI SGSKAKPIPT
IDTSRTQRLP SMELPDASSP LPASNSCRVV KNSIKLALNR HNITPPKPPV FEGTLTTDTP
PASEEKGMSI PVIGSKHVAS KHVAPPVGSS IPTLVSRGAD PLNGAASKRP HSPSLEEQAK
RLKETEKARI HIA
//
