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Database: UniProt
Entry: A0A256YNE8_9ARCH
LinkDB: A0A256YNE8_9ARCH
Original site: A0A256YNE8_9ARCH 
ID   A0A256YNE8_9ARCH        Unreviewed;       769 AA.
AC   A0A256YNE8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00017959};
DE            EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN   Name=alaS {ECO:0000313|EMBL:OYT42006.1};
GN   ORFNames=B6U78_02345 {ECO:0000313|EMBL:OYT42006.1};
OS   Candidatus Aenigmarchaeota archaeon ex4484_224.
OC   Archaea; Candidatus Aenigmarchaeota.
OX   NCBI_TaxID=2012503 {ECO:0000313|EMBL:OYT42006.1, ECO:0000313|Proteomes:UP000217063};
RN   [1] {ECO:0000313|Proteomes:UP000217063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (JUN-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:OYT42006.1}.
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DR   EMBL; NJEA01000017; OYT42006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256YNE8; -.
DR   Proteomes; UP000217063; 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:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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; 2.40.30.130; -; 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; IPR022429; Ala-tRNA_lgiase_arc.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   NCBIfam; TIGR03683; A-tRNA_syn_arch; 1.
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   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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OYT42006.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          71..729
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
SQ   SEQUENCE   769 AA;  89973 MW;  F6A544E82F27F369 CRC64;
     MDIKQEILKI FQKNPEKYWK VEVFDREGYK RCVCKKCGTG FWSIEEREYC PNPSCGEEYG
     FIGNPISKKK LDYIQTWKLL EKFFVKKGHE SIPRYPVVAR WREDIYFNIA SIVDFQRFDN
     GVMTFDYPAN PLIVPQVCLR FNDLKNVGIT GRHYTSFVMP GQHAFNYPKE GYWKDKTIEL
     NFEFFTKELG IPKEKLIYVE ELWHMPDFSA LGPYIETYSL GLEMVNSGFM EFSWKNGKLE
     KLPMKVVDVG WGLERLVWFI NGTPTSYDVV FGKALENFKK KVDLEYDEKL FLQYAKIAGS
     LDLTEIDEKI GRKRIAKILN VSLEELERKV LPIQSIYAIL DHSRTALFAI ADGVLPSNIG
     AGYFIRVVIR RALGLLNKFN WEVKLEDLVR WHIDYLSKMF PELKEREDEV ITIVNVEEKK
     WKKSRENAKR IIEKLKKEEI TEEKLVKIYE TYGITPEDLG IEASSFFYKK LEKKPKIEKK
     KIEFDISNLS KTKILFYDDI FEFKAKVLKV FDGNWIVLDK TAFYPKSGGQ DHDKGYIDGK
     EVLEVIKIGN VILHKVSEKI EEGKEVNCKV DEERRKILTQ HHDAVHIVNG IVKKVIGSWC
     NQYGAEKTVE KARLDITHFE NLSEEQIEKI EEEANKAIEK DLPINKFFMN RLEAERKYGF
     RIYQGGYVPS KVIRIVEIPS IDIEACSGTH GNSTKEVELI KILRTRRIAD GLIRIELVAG
     KRAKELLEER KKLLEEIKEK IGKEDIVEGG KEIFERWKKL RKEIKKLKK
//
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