ID SYA_AKKM8 Reviewed; 942 AA. AC B2UKT4; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 24-MAR-2009, entry version 7. DE RecName: Full=Alanyl-tRNA synthetase; DE EC=6.1.1.7; DE AltName: Full=Alanine--tRNA ligase; DE Short=AlaRS; GN Name=alaS; OrderedLocusNames=Amuc_1383; OS Akkermansia muciniphila (strain ATCC BAA-835). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., RA de Vos W.M., Richardson P.; RT "Complete sequence of Akkermansia muciniphila ATCC BAA-835."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + CC diphosphate + L-alanyl-tRNA(Ala). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001071; ACD05207.1; -; Genomic_DNA. DR RefSeq; YP_001877988.1; -. DR GeneID; 6274625; -. DR GenomeReviews; CP001071_GR; Amuc_1383. DR KEGG; amu:Amuc_1383; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00036; -; 1. DR InterPro; IPR002318; Ala-tRNA-synth_IIc. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_cons-reg. DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR003156; Pesterase_DHHA1. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF02272; DHHA1; 1. DR Pfam; PF01411; tRNA-synt_2c; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR00980; TRNASYNTHALA. DR TIGRFAMs; TIGR00344; alaS; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 942 Alanyl-tRNA synthetase. FT /FTId=PRO_0000347482. SQ SEQUENCE 942 AA; 103645 MW; ED53F46EB999D0D9 CRC64; MMTATEIRQS FLDFFREKQH TVVPSASLMP QSPGLLFTNA GMNQFVPYFL GVWTPPWTPA RATDTQKCIR AGGKHNDLED VGYDSYHHTF FEMLGNWSFG DYFKREAIRW AWELVVERWG FPAERLYATV YAPDKSKGDP GEFDREAWDF WAELFRSRGL DPDVHIVHGN VKDNFWMMGE TGPCGPCSEL HVDLTPEGNT KGSLVNKDSD QCIEIWNLVF IQYNAESDGS MRNLPACHVD TGMGFERACS IMQCTNGFKD FSRKPSNYAT DVFRPLFDRL EVLSGRKYAD VYPAPGSKRV DAEDGTLQEA IAFRVIADHL RTLSFSIADG ILPGNNGRNY VLRRILRRAV RYGRRLGFTQ PFLAELVDTL VESFGQVFPE LAARATTVKE VLNREEASFN ETLDRGLELF DAETASAGKV SGEFAFKLYD TYGFPIDLTA LLAEERGLDI DMERFNRLME EQRERARAAR KSEVVRALDL KTDAVTEFTG YDVDECAATV LEVSRQGDSL FIITDKTPFY AEMGGQVSDA GLIEIGGESY HVMAVQQIGN ARAHVVEARP GLEVKPGDRV HLSIDAERRR RIEAHHTATH LLHCALHQVV SPDAAQQGSF VSEDRLRFDF NSSAVSPDQL RLIEEKVNGW IEESLPVHCT ERAYADVKGN AAIAQFFGDK YGDVVRVVQV GGCRDGLDGV SMEFCGGTHI ANTKNIGLFK IKSEGAIASG VRRIEAMTGD AALEMIRQHV VAKSLEIAKA VEKIKEVNYE LADMGLEQVP VPTIEGKPGL TALGASDIRT VNDSLARFDA SVEHFKQTAL DAEKKLKKAR AGQSAAKADA LLNEWLSDAP SSLIQVAEGA GELLQELLNG LKKRQYAGAA FLLCVDSSSL LLGAYCGKDA IADGLSAGDM IREVAALAGG KGGGRADQAR GSAPQDADPQ ALAAAARNII NG //