ID A0A1F6KHS7_9BACT Unreviewed; 619 AA.
AC A0A1F6KHS7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
DE Flags: Fragment;
GN ORFNames=A3B47_04405 {ECO:0000313|EMBL:OGH46687.1};
OS Candidatus Levybacteria bacterium RIFCSPLOWO2_01_FULL_39_24.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798623 {ECO:0000313|EMBL:OGH46687.1, ECO:0000313|Proteomes:UP000178241};
RN [1] {ECO:0000313|EMBL:OGH46687.1, ECO:0000313|Proteomes:UP000178241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:OGH46687.1}.
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DR EMBL; MFOW01000002; OGH46687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6KHS7; -.
DR Proteomes; UP000178241; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.54.20; -; 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01411; tRNA-synt_2c; 2.
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 PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 1..619
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGH46687.1"
SQ SEQUENCE 619 AA; 71001 MW; B90BF91710DF5122 CRC64;
PLVPYLLGEP HPMGKKLVNV QNCFRAVDIE EVGDNRHTTF FRMLGNWSLG DYFKKKQLPW
MWEFVTKELG IPANKLYVTV FKGYKRILKD EETEKIWTEI LTKEGLSPKE RIFFYDTKNW
WSRAGEPDKM PVGEPGGPDS EIFFDFETPH TTEYGKYCHP NCECGRFMEI VNSVFMEYSS
FASAFVKTSA DKKATDGQSK NTFIKLPQRN VDHGAGVERL LAAVENQQDI FQTSLFKPIV
NAIEQILKSD YKINSRAIRI ITDHLIASTF IAANGIIPSN KEQGYILRRL LRRAIRYGKQ
LGVDKIFTSD IASVIIKNYS DTDSDLTEKE KLIKDLFNEE EKKFAQVIQE GLRRSEKIFE
IKTPIKTGLY SKLMQISDKK ELFRNIYRNK IPKNILIPIG EIKLATISGE EAFNLYQSFG
FPIEMIIELV QEKGLLVDIE AFEKEIEKHQ KISKVGAEKK FKGGLADTSE KTIMGHTATH
LLHKALRDLL GENVHQTGSN ITSERIRFDF NYDKNLAPEQ IKKIEEVVKE KIRENLPVHF
EMLSLAKAKE IGAIGLFDEK YGQTVKVYFV GPKTKDQRPY SIEFCGGPHV AFTSEIKSFR
IIKQENIGKG NRRIYAKVG
//
