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 22-FEB-2012, entry version 26. DE RecName: Full=Alanine--tRNA ligase; DE EC=6.1.1.7; DE AltName: Full=Alanyl-tRNA synthetase; 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]. RC STRAIN=ATCC BAA-835; 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 -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a CC two-step reaction: alanine is first activated by ATP to form Ala- CC AMP and then transferred to the acceptor end of tRNA(Ala). Also CC edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its CC editing domain (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + CC diphosphate + L-alanyl-tRNA(Ala). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic CC domain, the editing domain and the C-terminal C-Ala domain. The CC editing domain removes incorrectly charged amino acids, while the CC C-Ala domain, along with tRNA(Ala), serves as a bridge to CC cooperatively bring together the editing and aminoacylation CC centers thus stimulating deacylation of misacylated tRNAs (By CC 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; NC_010655.1. DR ProteinModelPortal; B2UKT4; -. DR STRING; B2UKT4; -. DR GeneID; 6274625; -. DR GenomeReviews; CP001071_GR; Amuc_1383. DR KEGG; amu:Amuc_1383; -. DR PATRIC; 20835640; VBIAkkMuc16855_1557. DR eggNOG; COG0013; -. DR HOGENOM; HBG354397; -. DR KO; K01872; -. DR OMA; VILEMES; -. DR ProtClustDB; PRK00252; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:EC. 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 HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1; -. DR InterPro; IPR002318; Ala-tRNA-synth_IIc. DR InterPro; IPR018162; Ala-tRNA-synth_IIc_anticod-bd. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core. DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR023033; Ala_tRNA_synth_euk/bac. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR012947; tRNA_SAD. DR PANTHER; PTHR11777:SF6; PTHR11777:SF6; 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; SSF101353; Ala-tRNA-synth_IIc_anticod-bd; 1. DR SUPFAM; SSF55186; Thr/Ala-tRNA-synth_IIc_edit; 1. 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; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 942 Alanine--tRNA ligase. FT /FTId=PRO_0000347482. FT METAL 586 586 Zinc (Potential). FT METAL 590 590 Zinc (Potential). FT METAL 695 695 Zinc (Potential). FT METAL 699 699 Zinc (Potential). 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 //