ID A0A2U9BHH1_SCOMX Unreviewed; 427 AA.
AC A0A2U9BHH1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=tRNA-nucleotidyltransferase 1 mitochondrial {ECO:0000313|EMBL:AWP03371.1};
GN ORFNames=SMAX5B_014190 {ECO:0000313|EMBL:AWP03371.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP03371.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP03371.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CP026248; AWP03371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BHH1; -.
DR STRING; 52904.ENSSMAP00000025236; -.
DR OrthoDB; 5402987at2759; -.
DR Proteomes; UP000246464; Chromosome 6.
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; PTHR46173; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR46173:SF1; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 53..176
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 210..261
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 427 AA; 49141 MW; F1B719E1F39644D1 CRC64;
MWSRVLGPGV VGRTALCWRS LYTMQLKTGE FQSLFTDGLN GLVEIFGKHK HELRIAGGAV
RDLLSGKRPE DVDFATTATP EEMKLMFQMA GIRMINNKGE KHGTITARLH NENFEVTTLR
VDVETDGRHA EVEFTTDWLK DAERRDLTIN SMFLGLDGTL YDYFKGYEDL QNRKVRFVGS
AEQRIQEDYL RILRYFRFYG RVALEPGDHE PETLTAIREN GHGLAAISGE RIWVELKKMV
VGNHAAHLLE LMYRLKLAQY IGLPPGGDVE VMKQVWQNAK DHSPKPMTVL AALFHCPKEV
DKMDFRLKVS REEKNLALFL VKHRRELCKS RDEPHSSKPF TDFIIDSREL DSQAKVCELL
KYQGEEKLLA ELSRWSIPRF PVSGHDLRRM GVVSGKEIGA TLQNLRDIWK TSRYQMDKEE
LLSYVKP
//
