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Database: UniProt
Entry: A0A369H8P7_9HYPO
LinkDB: A0A369H8P7_9HYPO
Original site: A0A369H8P7_9HYPO 
ID   A0A369H8P7_9HYPO        Unreviewed;       551 AA.
AC   A0A369H8P7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Poly A polymerase head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CP533_0729 {ECO:0000313|EMBL:RDA93059.1};
OS   Ophiocordyceps camponoti-saundersi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA93059.1, ECO:0000313|Proteomes:UP000253071};
RN   [1] {ECO:0000313|EMBL:RDA93059.1, ECO:0000313|Proteomes:UP000253071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA93059.1,
RC   ECO:0000313|Proteomes:UP000253071};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) 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:RDA93059.1}.
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DR   EMBL; PDHQ01000033; RDA93059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369H8P7; -.
DR   STRING; 2039874.A0A369H8P7; -.
DR   Proteomes; UP000253071; 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:UP000253071};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          56..210
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          237..299
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
SQ   SEQUENCE   551 AA;  61914 MW;  7104BF77E2CF5CAA CRC64;
     MYTKNQYSHT VITRPMTSRD GTISLLPAEK LLRELLLGCR AHIQKSGLAA ANDLEMWITG
     GWVRDRLLGI PCSDVDIALS TMTGSQFGEA LTEFFNLEEN NSYRDQASDL EIDTSSIFTG
     FHTTKQNLRK SKNLETTIGK VFGLDVDLVN LRKEVYDDDS RTPIMEFGTA EEDAFRRDAT
     VNSLFFNLDT QQVVDLTTRG LKDMAAGIIR TPLEPHKTFM DDPLRVLRLI RIGSKLGYTV
     EEATKSSMAD TDIHTALCAK VSRERVGIEV FKMMRQPNPQ FALQSLFEAD LYHAVFLERN
     SAIRETLQER LPSQEAKRPW PMTWPRAYKL LARLLADESS ELGRMLHAHE SVECLWLMAA
     YAPIGELRQE MLKKAVAAAA ESIKATNKHI KLLDNAMRNM NSVRDTIALV DGQQDKLPAR
     SSVGMAIRAW GDTWRPQVLF SLLAQIVYDT TLPSSLPSAE EESSLKGSLN RYNAFLAFVA
     REGLQDVYAI KPLLDGNAIM NLFGLQKGGR YLALAMTELV AWQLDHQTHG VEEAKEWLLQ
     QRDRLGVPAA T
//
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