ID A0A423X1L8_9PEZI Unreviewed; 524 AA.
AC A0A423X1L8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Poly A polymerase head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_02327 {ECO:0000313|EMBL:ROW09547.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW09547.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW09547.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW09547.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC ECO:0000256|RuleBase:RU003953}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROW09547.1}.
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DR EMBL; LKEA01000004; ROW09547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X1L8; -.
DR STRING; 356882.A0A423X1L8; -.
DR Proteomes; UP000283895; 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 CDD; cd05398; NT_ClassII-CCAase; 1.
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; 1.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 40..185
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 213..272
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 524 AA; 58925 MW; AF782BE90C3CE1A8 CRC64;
MRTTLQLDPI EKQLKCLLLD VATHIDTTEA KKPDEKVVLR WAGGWVRDKL LGKQSHDIDV
AINCMTGEVF GEKLRGFCDI SENKEKHSLR PEDIGNLHKI EKNPEKSKNL ETATVKLFGL
DVDFVNLRTE TYTEDSRNPQ VEFGTAEEDA LRRDATVNAL FYNIHTSEVE DFVGGLPDME
AGIIRTPMDP FKTFMDDPLR VLRLVRFASR LQFSIAATTM ENMGDARVLD ALRAKISRER
VGVEVEKMLK GEHPRDAIRL IDQLGLYHTV FTDSTKSQPP QPSLEGWTDV YESLHKLASE
PVSTPGSVYN VLVTSEEARY YAWVLACIVP FAQFPNPTGG NPKKQLPPAS LAAREGIKAP
NKLADIITGA VRHLDEICEL KVKVNNGDPC MDERDRFGMA IRGWEARGTN WRLQVLFAML
HEMITQAKAA NGKDSTSAIQ EIQSSWKEFL NHLEKLDLME APSMKPLVDG RTLLQALGIK
KPDKWMSPAL DICMAWQLRN PKETDPAGAI EEVRQRKEEL GIAI
//
