Tag | Content |
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CPLM ID | CPLM-005370 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Asparagine--tRNA ligase, mitochondrial |
Protein Synonyms/Alias | Asparaginyl-tRNA synthetase; AsnRS |
Gene Name | SLM5 |
Gene Synonyms/Alias | YCR024C; YCR242; YCR24C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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101 | WQSTPNRKQPFELQI | ubiquitination | [1] | 109 | QPFELQIKNPVKSIK | ubiquitination | [1] |
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Reference | [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae. Starita LM, Lo RS, Eng JK, von Haller PD, Fields S. Proteomics. 2012 Jan;12(2):236-40. [ PMID: 22106047] |
Functional Description | |
Sequence Annotation | |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 492 AA |
Protein Sequence | MFHAFTFLKG GRFYSSLTVK SLYEQVHHTS HDPISINGWI KSIRLLKRIA FLDLQDGTSV 60 NPLRIVIPLT NTDEVQFLKI LKTGQTLSIS NATWQSTPNR KQPFELQIKN PVKSIKLVGP 120 VSENYPLQKK YQTLRYLRSL PTLKYRTAYL SAILRLRSFV EFQFMLYFQK NHFTKVSPPI 180 LTSNDCEGAG ELFQVSTNTS PTASSYFGKP TYLTVSTQLH LEILALSLSR CWTLSPCFRA 240 EKSDTPRHLS EFWMLEVEMC FVNSVNELTS FVETTIKHII KACIDNQQEL LPKQFISSQE 300 NNASSELSIN QETQQIKTRW EDLINEKWHN ITYTNAIEIL KKRHNEVSHF KYEPKWGQPL 360 QTEHEKFLAG EYFKSPVFVT DYPRLCKPFY MKQNSTPDDT VGCFDLLVPG MGEIIGGSLR 420 EDDYDKLCRE MKARGMNRSG ELDWYVSLRK EGSAPHGGFG LGFERFISYL YGNHNIKDAI 480 PFYRTSAESI DF 492 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:SGD. GO:0004816; F:asparagine-tRNA ligase activity; ISS:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0003676; F:nucleic acid binding; IEA:InterPro. GO:0070145; P:mitochondrial asparaginyl-tRNA aminoacylation; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |