ID A0A1J0Z0B8_SPICI Unreviewed; 918 AA.
AC A0A1J0Z0B8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=aarS {ECO:0000313|EMBL:APE74682.1};
GN Synonyms=alaS {ECO:0000256|HAMAP-Rule:MF_00036,
GN ECO:0000313|EMBL:QIA73935.1};
GN ORFNames=GL982_10310 {ECO:0000313|EMBL:QIA73935.1}, SCITRI_00789
GN {ECO:0000313|EMBL:APE74682.1};
OS Spiroplasma citri.
OG Plasmid pSciBLH13-1 {ECO:0000313|EMBL:QIA73935.1}, and
OG Plasmid psciblh13-1 {ECO:0000313|Proteomes:UP000464221}.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2133 {ECO:0000313|EMBL:APE74682.1, ECO:0000313|Proteomes:UP000183717};
RN [1] {ECO:0000313|EMBL:APE74682.1, ECO:0000313|Proteomes:UP000183717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-A2 {ECO:0000313|EMBL:APE74682.1,
RC ECO:0000313|Proteomes:UP000183717};
RA Davis R.E., Shao J., Gasparich G., Gaynor B., Donofrio N.;
RT "Complete Genome Sequence of Spiroplasma citri R8A2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIA73935.1, ECO:0000313|Proteomes:UP000464221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BLH-13 {ECO:0000313|EMBL:QIA73935.1,
RC ECO:0000313|Proteomes:UP000464221};
RC PLASMID=psciblh13-1 {ECO:0000313|Proteomes:UP000464221}, and
RC pSciBLH13-1 {ECO:0000313|EMBL:QIA73935.1};
RA Yokomi R., Chen J., Rattner R., Selvaraj V., Maheshwari Y., Osman F.,
RA Vidalakis G.;
RT "Whole genome sequencing and comparative genomics analyses of six strains
RT of Spiroplasma citri.";
RL Submitted (JAN-2020) 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; CP013197; APE74682.1; -; Genomic_DNA.
DR EMBL; CP047429; QIA73935.1; -; Genomic_DNA.
DR RefSeq; WP_071937283.1; NZ_CP047429.1.
DR AlphaFoldDB; A0A1J0Z0B8; -.
DR STRING; 2133.SCITRI_00789; -.
DR GeneID; 54238689; -.
DR KEGG; sck:SCITRI_00789; -.
DR OrthoDB; 9803884at2; -.
DR Proteomes; UP000183717; Chromosome.
DR Proteomes; UP000464221; Plasmid psciblh13-1.
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}; Plasmid {ECO:0000313|EMBL:QIA73935.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00036};
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..720
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 918 AA; 104722 MW; 2233BAAB6B9A950F CRC64;
MTKFTANAIR KMWLDFFRSK DHYELPSVSL IPVDDPSLLW INSGVATLKP YFDGRKTPPS
PRLTNSQKSI RTNDIENVGY TARHHTLFEM LGNFSIGDYF KKEAIMYAWE FLTDKKWIGF
DPAKLYVTIY KDDQEAYEIW RNVIGLSDER IIKGDKDTNF WEIGAGPCGP NTEIFYDRGE
KYDPEQIGLK LLQDDLENDR YLEVWNIVFS QYNNNGNGTY TDLPRKNIDT GAGLERIASI
IQETPTNFET DLFMPIIKAV EKLVNVKYHY DETALFSNNS EQLKINTAFK VIADHIRAVT
FAIVDGAFPG NKDRGYVIRR LIRRASLYGK KIDLTEPFLF KLVGTVVKIM QEYYSYLVEK
QPIVEQAVLD EEKKFLKTLE QGSKLFNEVK TKYGTISKEH AFRLFESYGF PIELIEEEAH
EVGINVDRAG FDELLENAKT ISRTNRKDIK AIHLQSELFT KLDVASQFVG YEYEQVNNTE
IVFMFADDKP VTKLTNTTGY IILKETPFYA EKGGQAADHG LILKDNTTAY VLDVQQGPNK
QHLHFVKVEG TLAIGDLVNA SIDSDRRFYT RKNHSGTHLI HAALREVLGN HVMQTGSYND
AERLRIDITH NQAITPAEIT AVEGSVAKAI KTAIPCEIIY TDMQTALDVH HALAFFTEKY
DAEVRIVKFG TYSCELCGGT HVANSQDVED LLVTGLESKG AGTFRIHAIT SNKTIASYLN
EQFLKEKTEA INYFDKYNQG KAALLDQSLD QTWEQISNLT VSKPNWKQLK ELVAQFKEDF
KRWQKQYDNI LIQQFVKQYN TFLPQDKNGI NFLTHQFTTK VDINALKVLI DDYKARYRNL
LIFLVDVSDE TQATLIVGVS DDLHDRYQAG KIIQQLNPLL NGKGGGNNSV AQSGFNNKDK
TVLVKLLTNP LEFLKHHG
//
