| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Proline--tRNA ligase |
Protein Synonyms/Alias | ProRS |
Gene Name | proS |
Gene Synonyms/Alias | SYNPCC7002_A1656 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | | 591 | DLDAVVATLKNWVEA | T | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys- tRNA(Pro) is not edited by ProRS (By similarity) |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Nucleotide-binding; Proteinbiosynthesis |
Protein Sequence | MRLSQSLFVT LREDPADAEI PSHKLLLRAG YIRRIGRGIY AYLPLMWRVL QKVSQIVREE 60
MNATGAQETL LPQLQPAEIW QESGRWDTYT QAEGIMFSLR DRLDGELGLG PTHEEVITTI 120
AKDMIRSYRQ LPQHLYQIQT KFRDEIRPRF GLMRGREFIM KDGYSFHASE ECLKKTYADM 180
DQAYRNMLRR CGLQFRAVEA DSGAIGGSGS QEFMILADAG EDEILYTEDE KYAANTEKAV 240
SLPVEAIASP FNSFEKRETP NTATIESLCK FLNCSPTCVV KNVLYQVVYN NGKTVLALIS 300
IRGDQDVNEV KLQNELTKLA PNYDAKTVIS LTVPDADAQQ KWAAKSLPLG YISPALADDC 360
IAKNKAVSGE FLRLVDPTAA TLENFVTGAD ETNYHVLGAN WGTEFKLPPL QVDVRLAKAG 420
DRAVHDPTQI LQTARGIEAG HIFQLGTKYS EAMGATFTDE NGKEHPLVMG CYGVGVSRLA 480
QAAVEQSYDE NGIIWPVAIA PYHAVVVVPN VKSEEQMAAA EKLYADLNAA GVETILDDRN 540
ERAGVKFKDA ELIGIPFRVV TGKSLKDGKV EVVRRKEGDR QDLDLDAVVA TLKNWVEAAG 600
Q 601 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0002161 F:aminoacyl-tRNA editing activity IEA:InterPro GO:0005524 F:ATP binding IEA:UniProtKB-KW GO:0004827 F:proline-tRNA ligase activity IEA:UniProtKB-EC GO:0006433 P:prolyl-tRNA aminoacylation IEA:InterPro |
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