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Database: UniProt
Entry: R7QNT0_CHOCR
LinkDB: R7QNT0_CHOCR
Original site: R7QNT0_CHOCR 
ID   R7QNT0_CHOCR            Unreviewed;       426 AA.
AC   R7QNT0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDF40157.1};
GN   ORFNames=CHC_T00007020001 {ECO:0000313|EMBL:CDF40157.1};
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF40157.1, ECO:0000313|Proteomes:UP000012073};
RN   [1] {ECO:0000313|Proteomes:UP000012073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX   PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA   Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA   Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA   Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA   Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA   Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA   Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA   Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA   Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA   Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA   Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA   Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT   "Genome structure and metabolic features in the red seaweed Chondrus
RT   crispus shed light on evolution of the Archaeplastida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; HG002134; CDF40157.1; -; Genomic_DNA.
DR   RefSeq; XP_005710451.1; XM_005710394.1.
DR   AlphaFoldDB; R7QNT0; -.
DR   STRING; 2769.R7QNT0; -.
DR   EnsemblPlants; CDF40157; CDF40157; CHC_T00007020001.
DR   GeneID; 17318179; -.
DR   Gramene; CDF40157; CDF40157; CHC_T00007020001.
DR   KEGG; ccp:CHC_T00007020001; -.
DR   OMA; MDTQAFC; -.
DR   OrthoDB; 166496at2759; -.
DR   PhylomeDB; R7QNT0; -.
DR   Proteomes; UP000012073; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT   DOMAIN          48..256
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          293..417
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   426 AA;  47598 MW;  DE046F1796C6830C CRC64;
     MERVWDNGDI YKSVYEGLYC TGCEEYKDEK DLLEGLVCPS HLKPCSDRKE ENYFFALSKY
     QQKLEAFLED NPDFVLPQER RNEVLGWVKS GLRDFSVSRA NNPWGIPVPR DESQTIYVWF
     DALLGYVSAL LEDADTPDLD TALAKGWPAD VHIIGKDILR FHAVYWPAML MSAGVPLPKR
     VIGHGFLTKD GMKMGKSLGN TLDPVALVNT YGADAVRYYF LKAVDFGRDG DFSEQRFVEI
     VNADLANSLG NLLNRSLNLL KKNCGGVLPI SAADLGRDEA YAEEMQLRRV SASATENAFT
     SYADLDFMSA CNEVMRISNI ANMYIDRVAP WKKFKSDDMV EVREAERCIV SVLEGSRIVA
     AGLSPVVPEV SMKIYEALGF AADYASGLDW EKEMRWGKLP AGIVLGKPKP VFPRLELAVR
     EAVAVP
//
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