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Database: UniProt
Entry: A0A261QLL7_9BACI
LinkDB: A0A261QLL7_9BACI
Original site: A0A261QLL7_9BACI 
ID   A0A261QLL7_9BACI        Unreviewed;       877 AA.
AC   A0A261QLL7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-MAY-2019, entry version 6.
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   ORFNames=CEW92_03115 {ECO:0000313|EMBL:OZI13130.1};
OS   Bacillaceae bacterium SAS-127.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   unclassified Bacillaceae.
OX   NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI13130.1, ECO:0000313|Proteomes:UP000217062};
RN   [1] {ECO:0000313|EMBL:OZI13130.1, ECO:0000313|Proteomes:UP000217062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAS-127 {ECO:0000313|EMBL:OZI13130.1,
RC   ECO:0000313|Proteomes:UP000217062};
RA   Verma A., Pal Y., Krishnamurthi S.;
RT   "Indiibacillus sp. (SAS-127) genome sequencing.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
CC       two-step reaction: alanine is first activated by ATP to form Ala-
CC       AMP and then transferred to the acceptor end of tRNA(Ala). Also
CC       edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its
CC       editing domain. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00015829}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-
CC         alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657,
CC         Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497,
CC         ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036, ECO:0000256|SAAS:SAAS01125460};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00832879}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic
CC       domain, the editing domain and the C-terminal C-Ala domain. The
CC       editing domain removes incorrectly charged amino acids, while the
CC       C-Ala domain, along with tRNA(Ala), serves as a bridge to
CC       cooperatively bring together the editing and aminoacylation
CC       centers thus stimulating deacylation of misacylated tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00575517}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OZI13130.1}.
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DR   EMBL; NKXN01000012; OZI13130.1; -; Genomic_DNA.
DR   Proteomes; UP000217062; 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   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 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; 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   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; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249969};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250154}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000217062};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00299154};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249928, ECO:0000313|EMBL:OZI13130.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423853};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250206};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217062};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250135};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250194};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00423813}.
FT   DOMAIN        4    711       AA_TRNA_LIGASE_II_ALA.
FT                                {ECO:0000259|PROSITE:PS50860}.
FT   COILED      419    446       {ECO:0000256|SAM:Coils}.
FT   COILED      706    726       {ECO:0000256|SAM:Coils}.
FT   COILED      734    761       {ECO:0000256|SAM:Coils}.
FT   METAL       566    566       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       570    570       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       668    668       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       672    672       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   877 AA;  97491 MW;  D8855630D81130D8 CRC64;
     MKTLTGAQIR QMFLDFFQEK NHRVEPSAPL VPHDDPSLLW INSGVATLKK YFDGRVIPEN
     PRITNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGEYF KKEAIHWAWE FLTDEKWMAF
     EADKLSVTIH PEDDEAFEIW NKEVGLPEER IIRLEGNFWD IGEGPSGPNT EIFYDRGESY
     GNDANDPELY PGGENERYLE IWNLVFSEFN HNPDGTYTPL PKKNIDTGMG LERMASVVQE
     VPTNFDTDLF MPIIEATEVI SGEKYRESVE KDVAFKVVAD HIRTVAFAIG DGALPSNEGR
     GYVLRRLLRR AVRYAKQIHI NRPFMFELVP VVGEIMKDFY PEVSAKTEFI QKVIKNEEER
     FHETLHEGLA ILSSMIETAK SKGSNVIAGE DVFRLYDTYG FPVELTEEYA EEEGMKVDHE
     GFDKEMENQR ERARAARQDV DSMQVQGGVL GDITVASQFS GYDQLTVETT VAVVIANGEI
     VESATAGEEV QFILDETPFY AESGGQIADK GVLEADGLRV VIQDVKKAPN GQHVQQALVE
     QGTLKTGQKV TARVDEASRG KIIKNHTATH LLHQALKDVL GTHVNQAGSL VGPDRLRFDF
     SHFGQVQPEE LEQIETIVNE KIWRSLVVNI ANKSLDEAKA MGAMALFGEK YGDVVRVVSV
     GDYSLELCGG CHVPNTSVIG LFKIVSESGI GAGTRRIEAV TGEAAYQLLN QQVTLLKEAA
     NKLKANPKDI VTKVESLQAE MKELQRENES LLHKLSNIEA GSLLDNVKEV NGVKFLAARV
     QATDMNNLRT MADELKQKLD SGIIVLAAPS EDKVNIIAGV TKDLVDKGYH AGKLVKEVAS
     RCGGSGGGRP DMAQAGAKDP SKTEEALQFV EEWVKSV
//
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