SPM_001875

Uniprot: A0A037UQF5
Description: proline--tRNA ligase
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: 54,368
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: COILED 300 327 {ECO:0000256|SAM:Coils}.
Domain [FT]: DOMAIN 36 283 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:PS50862}.
Motif:
Region:
EMBL: AGBZ02000001
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: KAI92783
UniPathway:
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: PF03129;PF09180;PF00587
SMART:
SUPFAM: SM00946
TIGRFAMs: SSF52954;SSF64586

340129-341554(-)

>nucleotide sequence
TTAGTAAGCACGAGCAAAATAAACTAAATTAGTTGATGGTTGCCCACAATGAAAACAAGT
TGTTTTTTTGGTTGGAGCATCAAATGGAATACAACGTGATGTTGTTTGTGTTTCAGCTTT
AATTGTATCTTCGCACTCAATGCGACCACAAAATGGCACTAAAAACAAGCCATTCATCTT
TGCTAAAGTTTTTTTATACTCTGAATAATTATCAATTTCTTTTGTTCGTTGATGGCGATT
ATTCAAAGCTTTTTGATATAAATTTGTAGCAATTTGAACTAATAAATCAGAAACTACTTT
TTCAACTTCTGCTAATGAAACAGTAATTTTTTCAAAAGTATCACGACGAGCAATTGTAAC
TTGTTGTTGTGCTAAATCACGAGGTCCAATTTCAATTCGCAATGGAATTCCCTTAATTTC
TGCGTTAGCTGCACGGAATCCAAAGCCTTTATCTGATTGATCAATTTCGCAACGATATTT
CTGTAATTTTTTTTGGAGTTGCTGTGCTGCAGATAATTGCTCGTTACTATCATTATTAAT
TGGTAAAATCATAATTTGAATGGGCGCAATTTGCGGTGGTAACACTAGGCCATTATCATC
ACTATGTGTCATAATAATCCCCCCTATCAAACGTGTTGAAACCCCTCACGATGTTGAATA
AGCATATTCTAAAGTATTTTTTTGATTTGCAAATTTAATGTCAAATGCTTTAGAAAAATT
TTGGCCAAAATAATGACTAGTACCACATTGTAAAGCTTGACCATCATACATTAATGATTC
AATCGTATACGTTTCCTCTGCACCAGCAAATTTTTCACGTTCTGTTTTTTGCCCTTTAAT
AACTGGCAATAATAAAGTTTTTTCTGCAAAAGTAGCATAAATATCTAAAATTTTTAAAGT
AAATTGCTGTGCTTCTTGTTTTGAACTATGAATTGTATGTCCTTCTTGTCATAAAAATTC
ACTTGTTCGTAAAAAAGGACGAGTTGTTTTTTCTCAACGTAAAACATTAACTCATTGATT
ATATAACAATGGTAAATCACGATAACCCTGGATTTCTTTACTAAAAAAGGTTCCAAAAAG
AACTTCTGATGTTGGTCGAATGTATAATTCTTCATCTAAAACTTTATCTCCAACCTTTGT
TACCGTTGCAATTTCTGGTGAAAATCCTTCAATATGTTCTTTTTCTTTATTAAAAAGAGT
TTTTGGAATTAATAAAGGAAAATAAACATTTTTGACACCATTTTTTTTAAATTCAGCATC
TAAAATTTTTTGAATGTTTTCTCAAATTGCATATCCATAAGGTTTAAAAATAGTTGTTCC
CTTGATCGGCCCATAGGCAATTAAATCAGCATTTAAAACAATATCAGTATATCATTGCGC
AAAATCAACTTCACGCAGAGTAATTTTCTCTAACTTTCTTTTCAT

>protein sequence
MKRKLEKITLREVDFAQWYTDIVLNADLIAYGPIKGTTIFKPYGYAIWENIQKILDAEFK
KNGVKNVYFPLLIPKTLFNKEKEHIEGFSPEIATVTKVGDKVLDEELYIRPTSEVLFGTF
FSKEIQGYRDLPLLYNQWVNVLRWEKTTRPFLRTSEFLWQEGHTIHSSKQEAQQFTLKIL
DIYATFAEKTLLLPVIKGQKTEREKFAGAEETYTIESLMYDGQALQCGTSHYFGQNFSKA
FDIKFANQKNTLEYAYSTSWGVSTRLIGGIIMTHSDDNGLVLPPQIAPIQIMILPINNDS
NEQLSAAQQLQKKLQKYRCEIDQSDKGFGFRAANAEIKGIPLRIEIGPRDLAQQQVTIAR
RDTFEKITVSLAEVEKVVSDLLVQIATNLYQKALNNRHQRTKEIDNYSEYKKTLAKMNGL
FLVPFCGRIECEDTIKAETQTTSRCIPFDAPTKKTTCFHCGQPSTNLVYFARAY