ID I0K0H4_METFB Unreviewed; 915 AA.
AC I0K0H4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:CCG92993.1};
GN ORFNames=MFUM_880010 {ECO:0000313|EMBL:CCG92993.1};
OS Methylacidiphilum fumariolicum (strain SolV).
OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX NCBI_TaxID=1156937 {ECO:0000313|EMBL:CCG92993.1, ECO:0000313|Proteomes:UP000004837};
RN [1] {ECO:0000313|EMBL:CCG92993.1, ECO:0000313|Proteomes:UP000004837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolV {ECO:0000313|EMBL:CCG92993.1,
RC ECO:0000313|Proteomes:UP000004837};
RX PubMed=22740660; DOI=10.1128/JB.00501-12;
RA Khadem A.F., Wieczorek A.S., Pol A., Vuilleumier S., Harhangi H.R.,
RA Dunfield P.F., Kalyuzhnaya M.G., Murrell J.C., Francoijs K.-J.,
RA Stunnenberg H.G., Stein L.Y., DiSpirito A.A., Semrau J.D., Lajus A.,
RA Medigue C., Klotz M.G., Jetten M.S.M., Op den Camp H.J.M.;
RT "Draft Genome Sequence of the Volcano-Inhabiting Thermoacidophilic
RT Methanotroph Methylacidiphilum fumariolicum Strain SolV.";
RL J. Bacteriol. 194:3729-3730(2012).
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:CCG92993.1}.
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DR EMBL; CAHT01000097; CCG92993.1; -; Genomic_DNA.
DR RefSeq; WP_009061345.1; NZ_CAHT01000097.1.
DR AlphaFoldDB; I0K0H4; -.
DR STRING; 1156937.GCA_000953475_01743; -.
DR eggNOG; COG0013; Bacteria.
DR InParanoid; I0K0H4; -.
DR Proteomes; UP000004837; 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 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000004837};
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..721
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 759..793
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 915 AA; 104212 MW; 6D33A2BDC734E059 CRC64;
MNSNEIRQSF LDFFKERGHT ILPSASLVPE SPNLLFTNAG MNPFVPIFLG KQKCPYVPPR
VANSQKCLRA GGKHNDLEEV GYDTYHHTFF EMLGNWSFND YFKNEAIHWA WELLTEVWKI
PKERIYATVY KPAPEDPAEF DEDSFRIWFG LFQKSGLNPL VHIQFGSKKD NFWMMGETGP
CGPCSEIHID LTPEGNSEGT LINKNSPYCI EIWNLVFIQL DAKEDGSFSL LPSRHVDTGM
GLERICAIFK GTSYFQKFDA PISNYNTDLF IPLIRKLEDI SKISYKGTIP TENTVQDLTI
RQDIAFRVIV DHLRAIAFAI ADGILPSNLG RGHVLRRLLR RATRFGLVLG LKPPFLFELV
DPLVQTMGHY YIELIDKQRR IEEVVSSEEE LFAKTLSHGM AVFEEIKQKM LSENRKEILG
KEAFILYDTY GFPLDLTQLL AKEHGFSVDT KGFEQYMEEQ RQRSIVAHEE DIVSLTKTSE
FVGYEELEAE AEVVALLSAN RAIFDRTPFY AEMGGQVGDK GFILVDQKRI EVLDTIKSAS
GAHLHRLAFT DDLKPGSRVF LQVDKERRKN IAAHHTATHL LHWALRKVLG PETFQRGSYV
GPDRLRFDFA HSGPLSKEEL RAIEELINEK IELNDPVYWE EENYEKIKNN PSILQLFGEK
YGEKVRIVSI GNYSKELCGG THAKSTGELG YFKILGECGV SAGIRRIEAA CGKALLKFLK
AQAEEQDRKW NLLFSKDPSL RKLPKFTESL DFQSLIELFQ RRSEEIAELE KDIREKEKQK
AKKQEESFRL EAKSQVMELQ ARAEKFGSVP VIFYDCGIKP SSYLPILWNE LNKRVEGIAV
LSSRWEEKIN FFVGISPSLT QKIQAKAVLS KILLPLEGKG GGSATIAQGG CKDKKDLNLN
LIFEKARKAI NEFLG
//
