GCW_01285







Uniprot: A0A0F6CKA4
Description: prolyl-tRNA synthetase
EC number: 6.1.1.15
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). {ECO:0000256|HAMAP-Rule:MF_01571}.
Cofactor: 
Enzyme regulation: 
Function [CC]: 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). {ECO:0000256|HAMAP-Rule:MF_01571}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): proS
Gene names (synonym): 
Mass: 55,465
Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01571}.
Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; proline-tRNA ligase activity [GO:0004827]; prolyl-tRNA aminoacylation [GO:0006433]
Gene ontology IDs: GO:0004827; GO:0005524; GO:0005737; GO:0006433
Chain: 
Signal peptide: 
Domain [CC]: DOMAIN: Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension. {ECO:0000256|HAMAP-Rule:MF_01571}.
Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_01571}.
Protein families: Class-II aminoacyl-tRNA synthetase family, ProS type 3 subfamily
Coiled coil: 
Domain [FT]: DOMAIN 42 281 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:PS50862}.
Motif: 
Region: 
EMBL: CP006916
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: AHB99526
UniPathway: K01881
CDD: 
Gene3D: cd00778
HAMAP: 3.30.110.30;3.40.50.800
InterPro: MF_01571
PANTHER: IPR002314;IPR006195;IPR004154;IPR002316;IPR004499;IPR016061;IPR017449;IPR033721
PIRSF: PTHR11451:SF6
PRINTS: 
PROSITE: PR01046
Pfam: PS50862
ProDom: PF09180;PF00587
SMART: 
SUPFAM: SM00946
TIGRFAMs: SSF52954;SSF64586
304485-305910(+)

>nucleotide sequence
ATGGCTTTTAAAAAAAATCTAGCATCTTCTAAAGATGACAATATTTCAGACTGATATACT
GAAGTAATTAGTAAAGGAAATTTAATCCATTATTCAAACATCAAAGGCTTTATGTCATTT
CTTCCTAACGGTTGAAAAATTTGACAGCTAATAAAAAAAGAGCTAACTAAAGAGTTTGAT
CAACGTGATATTTTAGAACTTTGTTTACCATCATTAATAAGTCAGAACGACTTTTTACTA
GAGAAAAAACACCTAGAAGGATTTGCTCCTGAACTTTTTATAGTTACTAAAACCAGTAAC
GAAACAGAAAAATATATTTTAAGACCCACTTCAGAAATTGCCTTTTGTAATTTATGACGT
GAAACTTTAAGAAATTACCGTCAATTACCTATAAAACACAACCAATGAACTAGTGTTTTT
AGGGTAGAAAAAAACACTCGTCCATTTCTAAGAAACAGTGAGTTCTTTTGACATGAAATT
CACAGTTGTTTTGAAACAGAAGAACAATCTAATGATTTTGCAGTAGATATTTGAAAGTTA
TATCAAAGATTTATTAAGGATATTTTATGCATTCCTTTAGTAGCTGGTGAAAAAACTGAA
GCAGAAAAATTTGCTGGAGCTAAAACTACCTATACTGTTGAAACCATTATGCCAGATGGG
CAAGCGCTACAAAGTGCAACTTCTCATAATCTGTCACAAAATTTTTCTAAAGCTTTTGAT
ATCAGATACCAAACTAAGAATAATGATTATCAAAATGTTTTTAGTATGTCAGCAGGAGTA
TCAACTAGAATCATTGGAGCAATCATCATGACTCACGGGGACAATGACGGGTTGGTTTTC
CCAACTAAAGTTGCGCCTTATCATATTTCATTGAACTGTATTTTTGATGATACTAACCAA
GAATTAAATGCCAAATTAAAAGAACTAGCTAATAAATATTCACAAAAATACCGTGTGCAT
TTAAATCTTAATAAATATTCTACTGTAGAGATTATTAAGAATTCACAATTACGAGGTGAT
TGTTGTGTCTTATTAATGGGTCCAAACGATTTAAAGAAAAACGAAATCGTTTTCATCGAT
CGAATTTCAAAACAAAAGCAATTTATCAACCTTGATCATTTAGATCAAAAGCTTGAAGAA
TTATTTAGTACTTTTGATCAAAAACTTTATCAAAAAGCCAAAGCTGTTTTTGAAACCAAA
GTTGATTTTGCTCAAACGTTTGAAGAGTTTGAACAAAAGATTGCTTCTGGTAAGTTTGTT
AGAGTTTTCTATTGTAATGAAGATCTTTATGAAAAACAGATAAAAGAAAAAACAGGGGCG
TCTTCTCGATGCATTATTAAGCACTTAGATGAACAAACACAAGAGCGTTGTTTTATTTCT
AATAAAAAAGCGAAAGTGGAAATCTATTTTGCGCGTTCTTACTAA


>protein sequence
MAFKKNLASSKDDNISDWYTEVISKGNLIHYSNIKGFMSFLPNGWKIWQLIKKELTKEFD
QRDILELCLPSLISQNDFLLEKKHLEGFAPELFIVTKTSNETEKYILRPTSEIAFCNLWR
ETLRNYRQLPIKHNQWTSVFRVEKNTRPFLRNSEFFWHEIHSCFETEEQSNDFAVDIWKL
YQRFIKDILCIPLVAGEKTEAEKFAGAKTTYTVETIMPDGQALQSATSHNLSQNFSKAFD
IRYQTKNNDYQNVFSMSAGVSTRIIGAIIMTHGDNDGLVFPTKVAPYHISLNCIFDDTNQ
ELNAKLKELANKYSQKYRVHLNLNKYSTVEIIKNSQLRGDCCVLLMGPNDLKKNEIVFID
RISKQKQFINLDHLDQKLEELFSTFDQKLYQKAKAVFETKVDFAQTFEEFEQKIASGKFV
RVFYCNEDLYEKQIKEKTGASSRCIIKHLDEQTQERCFISNKKAKVEIYFARSY






















© Fisunov Lab of Proteomics, 2016.