ID A0A2H9LGE6_9ARCH Unreviewed; 580 AA.
AC A0A2H9LGE6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=COT14_01885 {ECO:0000313|EMBL:PIU22320.1};
OS Candidatus Diapherotrites archaeon CG08_land_8_20_14_0_20_30_16.
OC Archaea; Candidatus Diapherotrites.
OX NCBI_TaxID=1974403 {ECO:0000313|EMBL:PIU22320.1, ECO:0000313|Proteomes:UP000230520};
RN [1] {ECO:0000313|EMBL:PIU22320.1, ECO:0000313|Proteomes:UP000230520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG08_land_8_20_14_0_20_30_16 {ECO:0000313|EMBL:PIU22320.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PIU22320.1}.
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DR EMBL; PEXK01000030; PIU22320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9LGE6; -.
DR Proteomes; UP000230520; 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 CDD; cd00673; AlaRS_core; 1.
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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:PIU22320.1};
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..580
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 482..509
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 580 AA; 66134 MW; AFF843B6CCAE2C47 CRC64;
MDAKTLKKKY IDFFKSKGHI EIPSASLVPE NDPTVLFTTA GMHPLVPYLI GQKHPLGKRL
VNVQRCIRTA DIDEVGDTYH HTFFEMLGNW SLGGYFKKEA IELIFEFHTK ILGISPKRYA
VTVFSGNKTS PKDIESENTW LSLGVPKERI AFLEDNWWWP PGSTGPCGPD TEMFYWKPND
IPGPKKFDPS DARWVEIGNN VLMQYIKTDK GQLLEAKQKN IDFGGGVERT VTVLSGLEDD
YLSDTFLPII KKIENLSNKK YIGNEKAMRI IADHIKASVF IIGDGVVPSN NERGYVLRRL
IRRAIRFGVE LGLKQFTKSI GTAVFKIYSD SNYDFLQKNK HHILTELEKE ENKFTQTLQQ
GIKEFNKIVD KWKDINGEDA FLLYQSYGFP IEMTIELAKE KNIKVDLNGF NEEYKKHQEL
SRTLSAGQFK SGLQDNSDIT KRLHTATHLL NEALRRVVSK DIKQKGSNIT PERLRFDFNH
HNALTQDEIK AVEDEVNKII QQKLTVKKED LPLKEALKSG CQAEFSIKYP DKVTVYSIGS
YSKEICMGPH VDNTSQLGCF KIIKEESSAS GIRRIKAVLE
//
