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Database: UniProt
Entry: A0A1P8RUW6_9FLAO
LinkDB: A0A1P8RUW6_9FLAO
Original site: A0A1P8RUW6_9FLAO 
ID   A0A1P8RUW6_9FLAO        Unreviewed;       870 AA.
AC   A0A1P8RUW6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   ORFNames=BWZ20_05415 {ECO:0000313|EMBL:APY07768.1};
OS   Winogradskyella sp. J14-2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1936080 {ECO:0000313|EMBL:APY07768.1, ECO:0000313|Proteomes:UP000187462};
RN   [1] {ECO:0000313|EMBL:APY07768.1, ECO:0000313|Proteomes:UP000187462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J14-2 {ECO:0000313|EMBL:APY07768.1,
RC   ECO:0000313|Proteomes:UP000187462};
RA   Kim J.H., Chi W.-J.;
RT   "Genome sequence of Winogradskyella sp. J14-2 isolated from seawater in
RT   Jeju island.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00036};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00036}.
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DR   EMBL; CP019388; APY07768.1; -; Genomic_DNA.
DR   RefSeq; WP_076617360.1; NZ_CP019388.1.
DR   AlphaFoldDB; A0A1P8RUW6; -.
DR   STRING; 1936080.BWZ20_05415; -.
DR   KEGG; wij:BWZ20_05415; -.
DR   OrthoDB; 9803884at2; -.
DR   Proteomes; UP000187462; 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   CDD; cd00673; AlaRS_core; 1.
DR   Gene3D; 2.40.30.130; -; 1.
DR   Gene3D; 3.10.310.40; -; 1.
DR   Gene3D; 3.30.54.20; -; 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   NCBIfam; TIGR00344; alaS; 1.
DR   PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 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:0000256|HAMAP-Rule:MF_00036};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00036}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00036};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00036};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00036}; Reference proteome {ECO:0000313|Proteomes:UP000187462};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00036};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_00036}; Zinc {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   DOMAIN          1..708
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   BINDING         563
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         665
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         669
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   870 AA;  98223 MW;  5522CAA6EE62084E CRC64;
     MTSQDIRSKF LSFFEGKKHL VVPSAPMVLK NDPTLMFVNS GMAPFKEFFL GNSEPKNNRI
     ADTQKCLRVS GKHNDLEEVG YDTYHHTLFE MLGNWSFGDY FKKEAIAWAW ELLTEVYGID
     KDILYVTVFE GSDDNDKLKM DQEAYDIWKQ YISEDRILMG NKKDNFWEMG DQGPCGPCSE
     IHVDIRSAEE KAKVDGKSLV NMDHPQVVEI WNLVFMQYNR KANGSLDVLP NKHIDTGMGF
     ERLCMVLQGV QSNYDTDVFT PIIREIETIT NKDYGKDEKI DVAIRVISDH VRAVAFSIAD
     GQLPSNTGAG YVIRRILRRA VRYGFTFLDK KEPFIYRLVD VLSKKMGTAF PEIKAQKQLI
     ENVIKEEEAS FLRTLEQGLI LLNGIVSDTK GDTVSGEKAF ELYDTYGFPI DLTALILSEK
     NLKLDEKGFE EQLQIQKNRS RKASETSTED WTILVDDAEQ EFIGYDALEA NVKITRYRKV
     TSKKEGDMFQ LVFNLTPFYA EGGGQVGDKG YLQDNHGDTV YIIDTKKENN VIIHFTKNLP
     DDLNDTFKAV VDQKQRFRTE CNHTATHLLH QALREVLGTH VEQKGSAVHS KYLRFDFSHF
     SKLTVEELRD VENFVNARID GKLPLEEQRN VPMDKAISDG AMALFGEKYG DTVRTVRFGQ
     SIELCGGTHV KNTGDIWHFK IVSEGAVAAG IRRIEAITYD AVKDFYFENN RAYFEMKDLL
     NNAQEPVKAL QNLQDENASL KKQIEQLLKD KAKNLKGDLK NEITALNGVN FIAKKVDLDA
     SGIKDLCFEL GGEVDNLFAL FGADNNGKAL LSCYISKNLV AEKDLNAGQI VRELGKHIQG
     GGGGQPFFAT AGGKNPAGIE EALEDAKNYL
//
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