ID Q0U815_PHANO Unreviewed; 1179 AA.
AC Q0U815;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=SNOG_12099 {ECO:0000313|EMBL:EAT80511.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80511.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445345; EAT80511.2; -; Genomic_DNA.
DR RefSeq; XP_001802333.1; XM_001802281.1.
DR AlphaFoldDB; Q0U815; -.
DR STRING; 321614.Q0U815; -.
DR EnsemblFungi; SNOT_12099; SNOT_12099; SNOG_12099.
DR GeneID; 5979243; -.
DR KEGG; pno:SNOG_12099; -.
DR VEuPathDB; FungiDB:JI435_120990; -.
DR eggNOG; KOG2245; Eukaryota.
DR HOGENOM; CLU_004292_0_0_1; -.
DR InParanoid; Q0U815; -.
DR OrthoDB; 5479694at2759; -.
DR Proteomes; UP000001055; 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 Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR040459; MJ1316.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR PANTHER; PTHR10682:SF23; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF13563; 2_5_RNA_ligase2; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF04457; MJ1316; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR SUPFAM; SSF56219; DNase I-like; 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:UP000001055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 297..538
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT DOMAIN 659..713
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 764..900
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 1111..1176
FT /note="MJ1316 RNA cyclic group end recognition"
FT /evidence="ECO:0000259|Pfam:PF04457"
FT REGION 1067..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1084
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 131340 MW; 44F5F253CABB364D CRC64;
MAGIKDSQHY DAIRINSNDT ALCIIAPDTA CGNVDRLREL YDKAYGKWPA HINLVYPFVA
PENLPRAQEQ LKTYFDEHLD TSKSRTTILS DAGIFKHRNN STVFLQESQS QSDSSLASLR
SMALQALGQK PAPSNLHLTI GQTENNTLFS QQFLLSKARL LPKLQFRIGA LAILVRDRSG
PDDCMKLWGV IDVARPEEAW RPSTPEHWIG QFPTVATDLH VGDNEGGEAV VKNISTANRN
LQSGPIYCFD PHQNAWSVCE NTSKNGTDAS NLKISSYNVL IDSEYPPTHE RDPFLISTIL
SESAAADVLV LQEVSDDFLS YILSNPDIQE RYQYVSHGPP SQSDIGPLPN LRNVVILSRW
CFSWKFVSFQ QKYKGALVAK FGGLISNETC SQQGLVVAGV HLTAGLTDSS VAAKNQQLQA
LRDYLVDQHD ADAWVIAGDF NIPTSTYTID TALKDGSISK ETVATLSSIE TEFSDAGLID
TWAVARVEAT DEVVSSTYDE LFDGEEGATF DPRNNILAAA TSETSIGRPQ RYDRILARFQ
DNFRVSRCNH FGLPSEVDGS QVVPSDHAGI RSTLEFLKPS TATEGQSLEQ ENRMKIALKR
AGPCLSQSAE LDSVLASGGM FPSEEEVQQR KDALEILKRV VYGTSSDDVT STSDVPMIIV
PVGSYALGVW TSGSDIDCLC IGTISSKTFF KLARQRLVKA HDQGVRVLRK VEANTGTMLE
LWSEFAGLPA SDPIFNLSIL SLRKLKPYRD LLYIQRTLPS LSAFRLAYRC IKLWAVRRGI
YSAKFGYLGG VHITLMLSWA AKCLAHDSGS ITAPDLVSSF FHHFAHFNWT NDMMYDAFFH
KQKPRYHRSA REPMVVLGFH APNSNIAHTS TLPGLHTLVS EMKAADEALS DPSMTWKKFF
GSTDNSPQAA LSPISGASDF LSAHSSYVKI DIQFWGRTLA KGKSLVGWVE SRCLSLVVDI
YKMLPDLAVR IWPARFTDSD TIEGGDYHGC YLIGLSRPSN EHALNTQEDK ASAKQALDKI
LDRFLTQLKT DERNYDSSVC WIDISLAKAN DVKSLRLDDR EWGDYVAELD PDSDDEEEIE
ELSDDVEEPL KRAIPQRPKP TATPLSSSKL RPASDVLHRL RWDPNLDPAE YIIGYEDRFL
GPRETGLEKW KTEQTDDEFI PQHRILYFKK KVARVVMVR
//
