ID A0A0V1MRW9_9BILA Unreviewed; 641 AA.
AC A0A0V1MRW9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|ARBA:ARBA00013056};
DE EC=3.1.1.96 {ECO:0000256|ARBA:ARBA00013056};
GN Name=GTF3C5 {ECO:0000313|EMBL:KRZ74541.1};
GN ORFNames=T10_9569 {ECO:0000313|EMBL:KRZ74541.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ74541.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ74541.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ74541.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000256|ARBA:ARBA00033671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000256|ARBA:ARBA00000741};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KRZ74541.1}.
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DR EMBL; JYDO01000049; KRZ74541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MRW9; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IEA:InterPro.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IEA:InterPro.
DR Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR Gene3D; 3.30.200.160; TFIIIC, subcomplex tauA, subunit Sfc1, barrel domain; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR InterPro; IPR019136; TF_IIIC_su-5_HTH.
DR InterPro; IPR040454; TF_IIIC_Tfc1/Sfc1.
DR InterPro; IPR041499; Tfc1/Sfc1_N.
DR InterPro; IPR042536; TFIIIC_tauA_Sfc1.
DR PANTHER; PTHR13230:SF5; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 5; 1.
DR PANTHER; PTHR13230; GENERAL TRANSCRIPTION FACTOR IIIC, POLYPEPTIDE 5; 1.
DR Pfam; PF09734; Tau95; 1.
DR Pfam; PF17682; Tau95_N; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; DTD-like; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..344
FT /note="Transcription factor IIIC subunit Tfc1/Sfc1 triple
FT barrel"
FT /evidence="ECO:0000259|Pfam:PF17682"
FT DOMAIN 417..515
FT /note="Transcription factor IIIC subunit 5 HTH"
FT /evidence="ECO:0000259|Pfam:PF09734"
SQ SEQUENCE 641 AA; 73679 MW; 7957A9782863E14B CRC64;
MVLSNTLKDS VLLLIYSLKN VVPENNFSYG TVLTLLSRSD EPKKISTMSW RTRFGARNAG
RDSKDRCCCR MCPLREGVVL IGAWKVIEFF FGSISLLSGY LHGGITPIWL AVGFLFETFL
LACTLMLFVG LRRRIAVLLL PFLVLQILIL ISMFIIVMYS VWLLKGERSP LDEEMEVDNI
FTNFTLHALL KGNKLDFHLS MNPSEAAQFY CTFVDKLRQN YREDLVKDVM SSKSNSLQEF
MVICYPGIVK NVDKALESLG GMKEIEKHKA GSLELNFHRK SNVFSRPALS RPREGAFLII
RARRLIQASP SSSKQATYSV QLEVVGTLSS IHDFNSSLFD FQYLPMRKNE NGQYSEIYSA
LVPSTKEQAE RWFTPPIPDP ELFLIPFSFT RLFTASESIL SREVTNYDLE TPGRAAETAT
DEFPAEPSPL AMKQVKRNTF DPAVHEALEK AFNERPMWLK YSLIVKLKLD ERDVRRLLPK
FAFHIISGPW GRNWCRYKYD PREDTNSWKF QTMHFPFFRF GGESALSEAF VKWHLKVSSI
GIRSSKEWDK LLTTEPTFQY TEGCLPSLRS MWYQMCDIHL PAVEELLSYR LRENQAESHP
TDGWLKSGTL DEIRELIKLD FKKTIDTLNA RASQSKADKN D
//
