ALAXM_PYRHO
ID ALAXM_PYRHO Reviewed; 216 AA.
AC O57848;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Alanyl-tRNA editing protein AlaX-M;
DE Short=AlaX-M;
DE AltName: Full=Alanyl-tRNA deacylase AlaX-M;
GN Name=alaXM; OrderedLocusNames=PH0108;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION AS TRNA(ALA) EDITING
RP PROTEIN, SUBUNIT, AND COFACTOR.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=17327676; DOI=10.1107/s090744490605640x;
RA Fukunaga R., Yokoyama S.;
RT "Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii.";
RL Acta Crystallogr. D 63:390-400(2007).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC mischarged charged Gly-tRNA(Ala) and Ser-tRNA(Ala).
CC {ECO:0000269|PubMed:17327676}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17327676};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17327676};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17327676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Editing domain AlaX-M subfamily. {ECO:0000305}.
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DR EMBL; BA000001; BAA29177.1; -; Genomic_DNA.
DR PIR; B71231; B71231.
DR PDB; 2E1B; X-ray; 2.70 A; A=1-216.
DR PDBsum; 2E1B; -.
DR AlphaFoldDB; O57848; -.
DR SMR; O57848; -.
DR STRING; 70601.3256494; -.
DR EnsemblBacteria; BAA29177; BAA29177; BAA29177.
DR KEGG; pho:PH0108; -.
DR eggNOG; arCOG01254; Archaea.
DR OMA; LMRLHTA; -.
DR BRENDA; 3.1.1.29; 5244.
DR EvolutionaryTrace; O57848; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
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; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Zinc.
FT CHAIN 1..216
FT /note="Alanyl-tRNA editing protein AlaX-M"
FT /id="PRO_0000391648"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2E1B"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2E1B"
FT HELIX 89..113
FT /evidence="ECO:0007829|PDB:2E1B"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:2E1B"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2E1B"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2E1B"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:2E1B"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:2E1B"
SQ SEQUENCE 216 AA; 25299 MW; 4B4D94685C47EF32 CRC64;
MINMTRKLYY EDAYLKEAKG RVLEIRDNAI LLDQTIFYPT GGGQPHDRGT INGVEVLDVY
KDEEGNVWHV VKEPEKFKVG DEVELKIDWD YRYKLMRIHT GLHLLEHVLN EVLGEGNWQL
VGSGMSVEKG RYDIAYPENL NKYKEQIISL FNKYVDEGGE VKIWWEGDRR YTQIRDFEVI
PCGGTHVKDI KEIGHIKKLK RSSIGRGKQR LEMWLE
