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Database: UniProt
Entry: D8IQI0_HERSS
LinkDB: D8IQI0_HERSS
Original site: D8IQI0_HERSS 
ID   D8IQI0_HERSS            Unreviewed;       874 AA.
AC   D8IQI0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
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:ADJ65092.1};
GN   OrderedLocusNames=Hsero_3614 {ECO:0000313|EMBL:ADJ65092.1};
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ65092.1, ECO:0000313|Proteomes:UP000000329};
RN   [1] {ECO:0000313|EMBL:ADJ65092.1, ECO:0000313|Proteomes:UP000000329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1 {ECO:0000313|EMBL:ADJ65092.1,
RC   ECO:0000313|Proteomes:UP000000329};
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA   Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA   Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA   Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA   Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA   Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA   Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA   Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA   Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA   Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA   Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA   Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA   Weiss V.A., Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT   fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-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   -!- 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; CP002039; ADJ65092.1; -; Genomic_DNA.
DR   RefSeq; WP_013235555.1; NC_014323.1.
DR   AlphaFoldDB; D8IQI0; -.
DR   STRING; 757424.Hsero_3614; -.
DR   KEGG; hse:Hsero_3614; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_4; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 9803884at2; -.
DR   Proteomes; UP000000329; 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   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   Gene3D; 6.10.250.550; -; 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|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:UP000000329};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00036}.
FT   DOMAIN          1..708
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   COILED          731..758
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         665
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   BINDING         669
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   874 AA;  94327 MW;  F8841CCBA921C083 CRC64;
     MNSAEIRDKF LKFFESKEHT IVRSSSLVPG NDPTLLFTNS GMVQFKDVFL GTDKRNYVRA
     ASVQRCLRAG GKHNDLENVG YTARHHTFFE MLGNWSFGDY FKRESLKWAW ELLTQVYGLP
     ADKLWATVYQ TDDEAYDIWT KDIGLPPERV VRIGDNKGAP YASDNFWQMA ETGPCGPCSE
     IFYDHGPDVW GGPPGSPDAD GDRYIEIWNN VFMQFDRQLD PATGEYTLTP LPAPCVDTGM
     GLERLAAILQ HVHSNYEIDL FQALIKAAAR ETGETDLSNA SLRVIADHIR ATSFLIVDGV
     IPGNEGRGYV LRRIIRRALR HGHKLGQTKP FFHKLVKDLV VQMGAAYPEL PEAAERVEMV
     LKQEEERFGE TLEHGMKILE AALAANTGKL DGETAFTLYD TYGFPLDLTA DICRERNVEL
     DEAGFTAAME RQKSAARAAG KFKMAAAIEY TGDKTRFVGY ESLAQSAKVV ALYVAGSPVQ
     KIEAGQDAIV VLDTTPFYAE SGGQCGDAGA LEAANGLFAV ADTQKIQAEV FGHHGQLIKG
     SLAVGDAVQA KVDADQRART MRNHSATHLM HKALREVLGS HVSQKGSLVD ADKTRFDFSH
     NAPMTAEEIR RVEEIVNREV LANVATGAQL MGYDDAIAAG AMALFGEKYG DQVRVLSIGT
     STELCGGTHV TRTGDIGLFK IVSEGGVAAG IRRVEAVTGE GALALVQSLS SRVAEAAAAL
     KTQPEELLPR IGQVQDQVKA LEKELASLKS KLASSQGDEL VNQAVDINGI KVLAATLEGA
     DVATLRETMD KLKDKLKTAA IVLGSVKDGK VSLIAGVTAD ATAKVKAGEL VNFVAQQVGG
     KGGGRPDMAQ AGGTEPAALP GALQGVAGWV QSKL
//
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