ID I0JKU0_HALH3 Unreviewed; 395 AA.
AC I0JKU0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Alanyl-transfer RNA synthetases family profile domain-containing protein {ECO:0000259|PROSITE:PS50860};
GN OrderedLocusNames=HBHAL_2415 {ECO:0000313|EMBL:CCG44760.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44760.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG44760.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; HE717023; CCG44760.1; -; Genomic_DNA.
DR AlphaFoldDB; I0JKU0; -.
DR STRING; 866895.HBHAL_2415; -.
DR KEGG; hhd:HBHAL_2415; -.
DR PATRIC; fig|866895.3.peg.1423; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_7_2_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
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 PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT DOMAIN 1..238
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 395 AA; 44734 MW; 3F6DDC96A7D29E24 CRC64;
MMTRKLYYED PYQLEFDSTV TKSDRDEHGP YVVLEATAFY PTGGGQPHDT GTLNSIKVID
VEEADGEVRH YIEEEFPQNG EDVHGSVDPK RRIDHMQQHS GQHIISAVFD DHYGIPTTSF
HLGSDTVTID LDTNQLSEEL LQKAEEQVNN IIRRNIPVEA RWMTADEANE YPLRKPLAVE
GEVRLVIIPY VDYNGCGGTH PASTGEVMAV KFLGWTKSKK QVRLEFVCGS RVLEKLDQKH
RILTDMKQLV PRPEEQLVEE VSEMIQAGKE KDKRITELEE QLLHYEARHI ISETKGEPVI
QRVFKDRPIK SLQSLGKTMI EEASDTYLIL VSEQEEQLQF VLAHGASIDR NMNDIAKQAM
PLIDGKGGGK PHFVQGGGKK LMDGTDFSNR VKELL
//
