ID A0A0V0QMA6_PSEPJ Unreviewed; 821 AA.
AC A0A0V0QMA6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain {ECO:0000313|EMBL:KRX03306.1};
GN ORFNames=PPERSA_08360 {ECO:0000313|EMBL:KRX03306.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03306.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03306.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03306.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00001818};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008927}.
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:KRX03306.1}.
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DR EMBL; LDAU01000136; KRX03306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QMA6; -.
DR EnsemblProtists; KRX03306; KRX03306; PPERSA_08360.
DR InParanoid; A0A0V0QMA6; -.
DR OMA; CPVVDSH; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR PANTHER; PTHR43097:SF5; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00749; tRNA-synt_1c; 2.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363037};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363037};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363037};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Ribonucleoprotein {ECO:0000313|EMBL:KRX03306.1};
KW Ribosomal protein {ECO:0000313|EMBL:KRX03306.1}.
FT DOMAIN 694..820
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 587..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 94460 MW; E026EC7E8624BE01 CRC64;
MQVRSNFDIQ AQYKKYKGVL KKAEQGKVVT RFAPEPSGYL HLGHVKAALI TYHYAKIYDG
KMILRFDDTN PSKEKQEYVD SIQEDLTRLG ITWSNISYTS DYFAYFEQKA EELIKQGLAY
CDNTPVEEMR AQRDTGIESE CRGQSVEENL RIWNCMKKAI NPEVLKKKIE DAKKPKKYES
KSGKQKEQQL KEEDLTNYAA YCLRAKISMD NKNKCMRDPV LYRCNFTPHH RQGTKYVIYP
TYDFACPLLD SYEGVTHAMR SMEYTDRVAQ YEWVIKKCQV KSVNIFEFSR LNFVNIILSK
RHLTWFVDTG RTEGWDDARM PTVRGILRRG LRVETLTEFM LGQGPSRKPS LMEWDKIWSD
NKKVIDPICP RFVSVRKDRA CKLTILNGPE KLIYNTAPLN GIKNAVPELK KLRPVAVSKN
MLLDFDDASH VKEGEKVTLV KFGNVVIKSI KEVGDHLELT AEHLPEDNDF KSTQKFTWLS
ADADLVTVNL IELNHLIQVP QMEEGMKLEE IVNEQTKYSN EFYAESLIRN LQVDDVLQFE
RRGYYRVDKV KLTRTGDKVV DMIYTPDGRT KAMTSYQTTA VKAEDLTKGS GAGKDKKAKK
EQQKQNQSGK QTKSDLTITA VSGHIESTLL QIVVEMTGAH VEWNLVSSSQ VQAQIKQLKV
TALPVLQTSE GIISTVRGVI YYLVASSNKL YGTNDAEKAQ IDQWASFVSS DLNQALLPLN
QSLWGHQELS QEKFQEQLKA ATPLLQFLNT NLNGKKFLVG KQISFADILL YTKLVYGFRT
YFSTEFRKEN QYLTSWFNNF SDNKTIIKYL RKNIYPAQSW N
//
