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
//