ID G0PCX2_CAEBE Unreviewed; 1333 AA.
AC G0PCX2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=CAEBREN_01393 {ECO:0000313|EMBL:EGT51314.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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 EMBL; GL380255; EGT51314.1; -; Genomic_DNA.
DR STRING; 135651.G0PCX2; -.
DR EnsemblMetazoa; CBN01393.1; CBN01393.1; WBGene00140118.
DR eggNOG; KOG2245; Eukaryota.
DR HOGENOM; CLU_258933_0_0_1; -.
DR InParanoid; G0PCX2; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
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 InterPro; IPR003125; WSN.
DR PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR PANTHER; PTHR10682:SF10; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF20750; PAP_NTPase; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR Pfam; PF02206; WSN; 1.
DR SMART; SM00453; WSN; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1333
FT /note="polynucleotide adenylyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003406761"
FT DOMAIN 45..113
FT /note="Domain of unknown function WSN"
FT /evidence="ECO:0000259|SMART:SM00453"
FT REGION 1309..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 148590 MW; 6933B0D960933DCE CRC64;
MHRIYRLLII ASLLTSITVN SSPSFFIVEL DPHLISREER DASDDPFSIL QSRISSLARI
VSGVTLYNGL VDGSIPVDEA IGELMNIGSF SLDDLMKSGE QKVKGFAEKL KAASTKMADN
SIELETAIMD YLKMKEMWNE VGDLNKLPDN SKFEELKSMN SLDLKDIEDF KLTDALNKLD
TNSIADIPKI KSAVGKIAEV SKKAVELMDE KHVLSTLADM TSFHKYVNLI SFVENSRPYK
KLDSSYAASM KADVNELQGI DNNGTSVISI IKRITLSQSG SQDFDRKHTS GFVNGYADLK
HLPKDFDDSF VSKKFRWLVL DDGLTTISNL ENGMKTLSEK WTELRKDKIR KAVQKAEFIG
EKLKGISGVS NLVEGLISKL VKYPEPMYLH DYSSEISEMS QHLFELFRKG EAIREISTRL
EQNKDVITQM NTSRVMSIRL FMTLLQAIQP AVEVLQKGEK VNKLAELLVK QPKSYTGIKT
DVPSTSCQAF FNAIKNHQGD DLEKVGTAAE LSILIRELKT DTDFSTHIGT ASTIVSGSVD
SIQSIRTAVG DIKKSSADNT QTFSQLKDLQ KFSKPLGDTS AVIDKIQKVL EKEKQLKNFV
NNGEIVMQLA GSQKIMISGE IKELAKKLWY GFYDVSIKSK ILLDEVKRKE VGVKEPSDDK
LESYGPIIGS LDGLGDVTLN VDKRIMAIGK LLPSITDQDT ELKLKTLKQS LTELGSLDLT
FARQSSSLKG MPQVLAGIND VFLGTKPTST VDPKTGENVC GVQVSPEDGC EPSMTEEEFY
ASPEDNDTST KGKPGNNVTL YLKINMSSAS SAAATTTTKI YGVSQPISLA QPTPKDLSLT
CSLLQELKSV GSFEAKEETT KRIQVLQFLN ATVKKWIQGI SSARLPNGKF FEAGGQVVSF
GSYRLGVHSS GGDIDSVVIA PRQVSRTDFF TSLKDILLRN PNVKNLNAVE KAFVPIMTFE
FAGVDVDLLF ARLDLAVIPE KIDLTDDNLL KNMDQESVRS LNGVRVAEKL LQLVPNRESF
CMTLRAIKVW AKSHGVYSNA MGFFGGITWA LLVARTCQLY PNATPSRLVQ KVFYVFSTWN
YPSPIVLCMP TRERPDMLAL DNLCWGRNHA DRFHLMPIIT PAFPEQNSTH NVSRSTMEVI
KKEMADALII CNDVFEGKCD WKFLFEEVNF YSQYKHFVVM KLDAKKEETE NSYGGFLESR
LRVLVGAFER NRGIKLAHLN PKKCQPTSKS QSLWFIGLEF DEVVKNMDLT REIDNFKWNL
NVQAKQIAGF EDVELDISYV KRSQLIKYLP AAELKKGRFF VAKGSAEDNK ENAGGLKRKC
DNPMSSVVSK KQC
//