ID   A0A397HPG1_9EURO        Unreviewed;      1126 AA.
AC   A0A397HPG1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-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=CDV56_106927 {ECO:0000313|EMBL:RHZ63063.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ63063.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ63063.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ63063.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TTI2 family.
CC       {ECO:0000256|ARBA:ARBA00034736}.
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:RHZ63063.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NKHU02000032; RHZ63063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397HPG1; -.
DR   STRING; 41047.A0A397HPG1; -.
DR   VEuPathDB; FungiDB:CDV56_106927; -.
DR   OrthoDB; 5402987at2759; -.
DR   Proteomes; UP000215305; Unassembled WGS sequence.
DR   GO; GO:0110078; C:TTT Hsp90 cochaperone complex; IEA:InterPro.
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; IPR016024; ARM-type_fold.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   InterPro; IPR018870; Tti2.
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   Pfam; PF10521; Tti2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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:UP000215305};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          57..210
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          237..297
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
SQ   SEQUENCE   1126 AA;  126099 MW;  5A3B81F5A08DCC89 CRC64;
     MATVAQTSSQ TPQPLVTVQL TPIENTLKEL LLDVAKYTRE RAIAAGASEA DTPHMVLRFT
     GGWVRDKLLG VDSHDIDVGI SSMTGYQFGM ALKDYLDIPE NLEKYKRNHP NGELNEAIVS
     LHKIEANPEK SKHLETVTTK IFGLDIDLVN LRKETYTDDT RNPQMEFGTA EEDALRRDAT
     INALFYNLNE SKVEDLTGRG FSDMRNKIIR TPLEPYQTFK DDPLRVLRLI RFASRLGYQI
     DSNTERAMQN SDISATLKVK ISRERVGTEL EKMLKGPDPR NALQFIDRLG LYHTIFANHQ
     DDVSADTSSW SLAYNALESL SHPVGASKAT LEKVRDFLMR NPLESYYAWM IAALAPWSSV
     PTRIAKGPKA KAFPPRAAEV ARDSLRSDNK MVSVLGDAAA SWRSIIDVKS SLLEGRMKGT
     SPEVRQQIGL YIKSWKKDWR LCILLAILQE IMRGREFLPV IQEYDRFISY IIQNDLQGVC
     EMKPIVNGGE IMKALEAKNG PWLSKALDMV FKWQLLHPEI TEKEKALEYL LDREDELELR
     AAARETLQRR DSSIIPEARL DSINIPGDLD LLWHNVSSYQ AQNTANTCEN LLVAQAFLTS
     QSSKSLSETE ENAVNNLYAW ASELALPSAV FATTEVGSSD VEKTETIREN KLQLELAVSV
     LVALNSLLRI QKSAHATDVI TALASFTSEQ DSWTTRDTYM KSKKTLERLS TNVRGEADSS
     FWSLVERILK ERIKPLFAKT KNPAITAEGR KNFHPVPLPR FDASIIDPAT KPWKISDVYA
     TTVLAWVIAQ YQAKDRPYLE AHVPLLVPPI LALIDDDSVA YKTRGCILLN QLLNPIRESR
     SDILQRTNLA SVFEDAVRPC LLSLPSITPE DDAIKLLGVA YPALLSLLQT NYHATTPRSA
     ANSSRDNYIS SVTRTLRENL ISSFHHISST NRSSTSSFAT FPYPRLSTLL VDQMYPLLLE
     LGIHTTKYLQ EIVPLLYSTL SNPFGTAYPP LLLSAIAVTR AVVLNAHPRL WRWRGEILGA
     LCSCWLRVVE EEGEIAERAF KGRSAGEDQE TGAALTKLKK ELRGAVYLLR FALENPAQAD
     GDVGQLEAKA AIRKELQELV DADESLADLL LVDIDPNDAD FFGIDP
//