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Database: UniProt
Entry: A0A0F5H129_9MOLU
LinkDB: A0A0F5H129_9MOLU
Original site: A0A0F5H129_9MOLU 
ID   A0A0F5H129_9MOLU        Unreviewed;       874 AA.
AC   A0A0F5H129;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   ECO:0000313|EMBL:KKB26850.1};
GN   ORFNames=MMELEA_05330 {ECO:0000313|EMBL:KKB26850.1};
OS   Mycoplasmopsis meleagridis ATCC 25294.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=1264554 {ECO:0000313|EMBL:KKB26850.1, ECO:0000313|Proteomes:UP000033750};
RN   [1] {ECO:0000313|EMBL:KKB26850.1, ECO:0000313|Proteomes:UP000033750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25294 {ECO:0000313|EMBL:KKB26850.1,
RC   ECO:0000313|Proteomes:UP000033750};
RA   Yacoub E., Blanchard A., Sirand-Pugnet P., Mardassi B.B.A.;
RT   "Genome sequence of Mycoplasma meleagridis strain ATCC 25294.";
RL   Submitted (MAR-2015) 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}.
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:KKB26850.1}.
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DR   EMBL; JZXN01000016; KKB26850.1; -; Genomic_DNA.
DR   RefSeq; WP_046096942.1; NZ_JZXN01000016.1.
DR   AlphaFoldDB; A0A0F5H129; -.
DR   STRING; 29561.MM26B8_00280; -.
DR   PATRIC; fig|1264554.4.peg.477; -.
DR   OrthoDB; 9803884at2; -.
DR   Proteomes; UP000033750; Unassembled WGS sequence.
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   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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   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:UP000033750};
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          4..706
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   BINDING         558
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         562
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         663
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         667
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   874 AA;  101411 MW;  039C51D276110320 CRC64;
     MKKLNSKEIR QSWIDFFKSK DHLEIESKSL IPINDPSLLW INSGVATLKD YFSGKKIPPK
     NRLVNSQKAI RTNDIENVGL TARHHTFFEM LGNFSIGDYF KKEAIAYAFE YLTKILEIDI
     EKLFFTYFKD DLETKELWIK HGVKEDHLIS GDRETNFWDI GSGPCGPNTE IFFDRGEKYD
     KRGIELLKND IENDRYIEIW NIVFSTFNND GENNYTELKQ KNIDTGAGLE RIASILQDAP
     TNYDSDLFIN IIKEIEKFTV YKYDSNNYFI GNNEQELINR NFKIIADHLR TVVNAIADGA
     KISSLGRGYI IRRLIRRAIY KSMQLGIKEI FLHKLVKVVH DSLPFEYDVE YVSREIKKEE
     ELFNKTINNG KEILDKYLQT NKDLIDGRFA FKMLDTYGFP IELTMEIASQ FNKKINLDEF
     EKAKEEHSNK SRGSKVSGMK DVINSLSLIK GKIDNFIGYE NLENQTKILM LLDEENEVDE
     IDGIGYLIIE NTPFYATSGG QNHDEGYILQ NGRKIEILDV FKDKYGNHVH KVKGKINKNN
     ILECYVDKEK RLNLARNHSA THLVFSALRK VLGPQIEQLG SDITYERFTF DFPANEKPTD
     KQIEEIENIM QDIIKQNIKR EYIITTTEEA KKLGAIMTIE ETEYMDPKNV RMVKWGNITS
     DLCGGTHIPN SALMENFKIV EVERKQAGIF RIRVVTSNKL VDRYYAEKNI SLAEEFNNIL
     NKIKNLDSKY DFELELKNLN NYQKYLKLTE SINKIREDFK KVNKENSNFE FDYENTKFEK
     INDKNIYINL EINSPQIKVI ASSLREKYPN SYIILGNKYE NEILLAIATK NENANALFQK
     IAKKLNGRGG GSPILAMGKI NSIENIEEVI KEII
//
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