ID A0A316UEV8_9BASI Unreviewed; 647 AA.
AC A0A316UEV8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Poly A polymerase head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCV69DRAFT_297374 {ECO:0000313|EMBL:PWN23444.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN23444.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN23444.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN23444.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC ECO:0000256|RuleBase:RU003953}.
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DR EMBL; KZ819322; PWN23444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UEV8; -.
DR STRING; 1684307.A0A316UEV8; -.
DR OrthoDB; 5402987at2759; -.
DR Proteomes; UP000245942; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProt.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR13734:SF5; CCA TRNA NUCLEOTIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13734; TRNA-NUCLEOTIDYLTRANSFERASE; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 2.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245942};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 52..206
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 281..320
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT REGION 608..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 71318 MW; 387C6FB6AFC737A4 CRC64;
MTLANPSISL EPVEEEIVIL LDSCCDWINA ERPQPSEAEG GSRVEYTGEV TARIAGGWVR
DKLLGMDSHD LDVSLSVMTG LNFAILFKAF LLKREKGVAS GASSSTRSAA ASAMSRITKI
SANPEQSKSL ETATANILGL SLDFVNLRKE IYEGNSRIPI MSFGTPLEDA ERRDITINSL
FYNVKTRQVE DWTDKGLLDM RAGLIRTPLP PLTTFLDDPL RVLRCIRFAS RFNYKLDDDV
RACLTGTGHS MQTSASDDPR LRDVEMASIS HKGRELVRDA LMKKVSRERV GIEVDKMLSG
PNPLLALRLL KELDLYSLVF HIESLQASCT LRLASTQTPT STPDPQAASS LAIAASQILD
DLSPHPTTPT GIFEQLNVPQ EITSSLVKPE TRRILHFASA LLPLSDVEIE EKKGKWSWSG
EKILMAGLKL GRNNTLLPVM SLIRGIPFLS GPASIDSSRA SLLQHLPDGI DIPREALVAL
LLRDKNLHNP SIGIEWKTGL TMAFVKDVLD VQGDATRIES IVEAYSGFCK YVRDKRIEER
LDEKPLMDGK ELLSVLSLSP SPLLPKIQNA LLIWQLSRPP PSGAAEAEAA GEEARQWLKE
RWEAGAIVDV DKRGGPAVKS AGKKKGQQNK ERSEEVPHLE KRRKSEE
//
