SYA_SALRD
ID SYA_SALRD Reviewed; 966 AA.
AC Q2S2B6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036}; OrderedLocusNames=SRU_1544;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00036}.
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DR EMBL; CP000159; ABC43801.1; -; Genomic_DNA.
DR RefSeq; WP_011404291.1; NC_007677.1.
DR RefSeq; YP_445665.1; NC_007677.1.
DR AlphaFoldDB; Q2S2B6; -.
DR SMR; Q2S2B6; -.
DR STRING; 309807.SRU_1544; -.
DR PRIDE; Q2S2B6; -.
DR EnsemblBacteria; ABC43801; ABC43801; SRU_1544.
DR KEGG; sru:SRU_1544; -.
DR PATRIC; fig|309807.25.peg.1598; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_10; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 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 InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 2.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..966
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347774"
FT REGION 927..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 750
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 754
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 966 AA; 107424 MW; 829FD9A0C260EC0A CRC64;
MSHDPMNPHL QSSADPSRSS EEIRQDFLQF FQAKGHEVVP SASLVPDGDG TLLFTNAGMN
QFKDVFLGTG QRPYSRAVDT QKCLRVSGKH NDLEEVGHDT YHHTFFEMLG NWSFGDYFKA
EAIRWAWELL VERWGLAPDR LYATVHEGDD DFGLSADAEA YDLWLSETPL PEERVLYEPS
KENFWMMGDT GPCGPCSELH VDLRPPEARQ ETPGRELVNV DHPQVMELWN LVFIQYNAQT
DGSLEPLDDQ HVDTGMGFER MVAVLQGKES TYDTDLFAPL LQAMADRSPR EEIRGYDDLH
IEDDDEHEQV RIALRVVADH IRAIAFAISD GVMPSNEGRG YVIRRILRRA VRYGYQTLEL
EEPFLHRLVD PLIEKMGGPF DGLAEQQEFI EQAIRSEEES FLETLGTGIE FFERVVPHVT
GFQDTDGEES DRLLGALRED AQAMDLLEKA YVDTDDENDI LHSFARTARG GTLPGQIAFL
LHDTYGFPID LTRLMARERD LDVDMEGYET LMDRQQERAR AASDFAVDQS DVQAWQSVSP
GEASVFVGYD RAVVPDAEVR AVRVVETGDT QQYEVELSRT PFYAEAGGQV GDTGTLRFGD
ESVQVLDTQR EGERIAHTVD TLPEPLDGPV EAAVDAERRN HIRAHHTATH LMHAVLRETL
GDHVQQKGSL VAPDRLRFDF SHFDAVDEDT LRHIERRVNT AIQQNIPKQE ARDVPIDEAL
DRGATALFDE QYGDRVRVIT FDPDFSMELC GGTHVDATGE IGLFRFLSEG SVASGVRRVE
AVAGKAALEH VESELETLTR ARRQFRSLHT SLPEAIAEVQ EERDRLAGEV DQLRRGQLSD
QLDTFIAENA ASVDGITVVT GRLDRASMDD LQELGQQFRD KLGEGAVGVL GSVGEDGEKA
YVVATVADDL VDDGALRAGD LVGTLGDRLG GGGGGRPSLA SAGGRDPEAL DTVLDGVPAL
VRDRLE
