(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9Q1_METMS

ID   D5E9Q1_METMS            Unreviewed;       924 AA.
AC   D5E9Q1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 60.
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   OrderedLocusNames=Mmah_0370 {ECO:0000313|EMBL:ADE35902.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35902.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35902.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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         ECO:0000256|SAAS:SAAS01118495};
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       ECO:0000256|SAAS:SAAS00346605}.
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|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00541819}.
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DR   EMBL; CP001994; ADE35902.1; -; Genomic_DNA.
DR   RefSeq; WP_013036845.1; NC_014002.1.
DR   EnsemblBacteria; ADE35902; ADE35902; Mmah_0370.
DR   GeneID; 8982504; -.
DR   KEGG; mmh:Mmah_0370; -.
DR   eggNOG; arCOG01255; Archaea.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; HOG000015496; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 7896at2157; -.
DR   BioCyc; MMAH547558:G1GHT-367-MONOMER; -.
DR   Proteomes; UP000001059; 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   HAMAP; MF_00036_A; Ala_tRNA_synth_A; 1.
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; IPR022429; Ala-tRNA_lgiase_arc.
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   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; SSF101353; SSF101353; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   TIGRFAMs; TIGR03683; A-tRNA_syn_arch; 1.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9Q1.
DR   SWISS-2DPAGE; D5E9Q1.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00424721, ECO:0000313|EMBL:ADE35902.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00017587}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00017589};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00017592,
KW   ECO:0000313|EMBL:ADE35902.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00017586};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00424727};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00424725};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00424723};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00424728};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00017591}.
FT   DOMAIN          58..757
FT                   /note="AA_TRNA_LIGASE_II_ALA"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   REGION          886..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          792..819
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   METAL           611
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   METAL           615
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   METAL           714
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   METAL           718
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   924 AA;  103808 MW;  F7F47E882F4C777D CRC64;
     MLEEEYDINF FYENGFIRKQ CQKCGSYFWT RDRDRDTCGD APCDPYSFID NPVFKKKFNL
     AQMREFYLSY FEKNGHTRIE RYPVIARWRN DIYLTIASIA DFQPFVTSGQ VAPPANPLTI
     SQPCIRLSDL DAVGRSGRHL TTFEMMAHHA FNKKSNEIYW KDRTVQLCDG LLNELGVDPF
     AVTYKEEPWA GGGNAGACVE VLIGGLEVAT LVFMNLQQSK NGDIVIKGDT YRKMDNYIVD
     TGYGLERLVW ASQGTPTVYD AIFPEVVGEL MELAGVEHRL EDEDYANILS QNARLAGLMD
     VSEKANLLEL RKQVASNIGI TADKLGTIME PVETAYAIAD HARCITFMLG DGIIPSNVKA
     GYLARLVIRR TMKMMQDLDI KIPLSDIVQM HINHLPEYPE FADRFDVISD ILDNEEKKFQ
     ETLQRGKKLI QKSAKHYKKK GEKMPLDTVI DMYDSHGIPA EISREAASEV GVEVELPDNF
     YSLVAERHSK SVQEHEKEIP YADRLKKLPP TKRLFYDEPN RMEFEAVVLD VFDNNIVLDS
     TLLYPEGGGQ PPDHGTFMVD DALLKVIDVQ IFDGIVIHTI EEIEDELHIR KGDMVTGKVD
     EKRRMAHARN HTATHIINDA ARQVLGEHIW QAGAQKFADR ARLDISHYKR IVPEEINEIE
     MIANQMVMEN KRVISEWMDR STAEKRYGFS LYQGGVPPGD RIRVLHVGSD IEACAGTHCT
     FTGQVGPIKI LKTERIQDGV ERIEYAAGEA AVVAFQERDK LLRSSAETLR VATEQLPTTI
     ERFFTEWKEF KKENTRLKKE LAESRVNQLV ENAEQLKEIR LINSRVDGAD ADELTRMAGE
     LASSDDIVAL LISDHEGAKI AAAAGDSAVS KGINVGNIVR EIANLTGGGG GGKPSMARGG
     GQDSSKIDEG LALGRRMVEE QLGD
//

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