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Database: UniProt
Entry: D4G7M4_RIEPU
LinkDB: D4G7M4_RIEPU
Original site: D4G7M4_RIEPU 
ID   D4G7M4_RIEPU            Unreviewed;       426 AA.
AC   D4G7M4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE            EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN   OrderedLocusNames=RIEPE_0060 {ECO:0000313|EMBL:ADD79827.1};
OS   Riesia pediculicola (strain USDA).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Riesia.
OX   NCBI_TaxID=515618 {ECO:0000313|EMBL:ADD79827.1, ECO:0000313|Proteomes:UP000001700};
RN   [1] {ECO:0000313|EMBL:ADD79827.1, ECO:0000313|Proteomes:UP000001700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA {ECO:0000313|EMBL:ADD79827.1,
RC   ECO:0000313|Proteomes:UP000001700};
RA   Kirkness E.F.;
RT   "Genome sequence of Riesia pediculicola USDA.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; CP001085; ADD79827.1; -; Genomic_DNA.
DR   RefSeq; WP_013087809.1; NC_014109.1.
DR   AlphaFoldDB; D4G7M4; -.
DR   STRING; 515618.RIEPE_0060; -.
DR   KEGG; rip:RIEPE_0060; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_0_3_6; -.
DR   OrthoDB; 9803884at2; -.
DR   Proteomes; UP000001700; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00673; AlaRS_core; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:ADD79827.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          4..426
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
SQ   SEQUENCE   426 AA;  50298 MW;  D5755A6A23BAB505 CRC64;
     MINRNTHEIR KIFLRFFQEK DHLILPGSKL VPSERNSSLL FTNAGMNQFR ENFFKKEKLS
     SFTRVATSQY CIRAGGKFSD LENVGYTNSH HTLFEMLGNF SFGDYFRSES IEYAWELLTS
     KKWFGISKNK ILITVHHLDE ESYDIWANQI GISKNKIFKI EDKENHKYHS ENFWKMGKTG
     PCGPSTEIFY NFDEKDDFDG SLESFERRKK NFIEIWNIVF IQFNLNSSNK LEPLRYKSID
     TGMGLERIAS VIQNVKSNYQ IDTFKKLIQS IRSQFSAICF KDYTLRILSD HIRSIVLIIN
     ENIKPSNVGR GYVIRKIIRR AVRKGYLDGI REPFLYKIVS CFTRSNEKDF KYVKINQKII
     EHTIKKEEKQ FLKIILVGIK FLKEKLKNFN YRFISEKDIF LLHDTYGLPI DIAMKICKEH
     GTSIKR
//
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