aspS:Gene Product(s) - EcoliWiki
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aspS:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

AspS

Synonyms

aspartyl-tRNA synthetase[1], B1866[2][1], Tls[2][1], AspS[2][1]

Product description

aspartyl-tRNA synthetase[2][3];

Component of ; aspartyl-tRNA synthetase[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0003676

nucleic acid binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004365

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR004115
InterPro:IPR004364
InterPro:IPR006195
SP_KW:KW-0030

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006418

tRNA aminoacylation for protein translation

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004364
InterPro:IPR006195

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0000166

nucleotide binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR002312
InterPro:IPR004364
InterPro:IPR004524
InterPro:IPR006195
SP_KW:KW-0547

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006412

translation

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR002312
InterPro:IPR004115
InterPro:IPR004364
InterPro:IPR004524
InterPro:IPR006195
SP_KW:KW-0648

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0004815

aspartate-tRNA ligase activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR002312
InterPro:IPR004524
EC:6.1.1.12
HAMAP:MF_00044

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR002312
InterPro:IPR004115
InterPro:IPR004364
InterPro:IPR004524
InterPro:IPR006195
SP_KW:KW-0067
HAMAP:MF_00044

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR002312
InterPro:IPR004115
InterPro:IPR004364
InterPro:IPR004524
InterPro:IPR006195
SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0006422

aspartyl-tRNA aminoacylation

GO_REF:0000002
GO_REF:0000002
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR002312
InterPro:IPR004524
HAMAP:MF_00044

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016874

ligase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0436

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0004815

aspartate-tRNA ligase activity

PMID:9171418[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006422

aspartyl-tRNA aminoacylation

PMID:9171418[5]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc 12.5 [4]

complete

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Interactions

Partner TypePartnerNotesReferences

Protein

Subunits of aspartyl-tRNA synthetase

could be indirect


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Notes

Localization

CompartmentDescriptionEvidenceNotes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD PDRADALKLA
SELRNEFCIQ VTGTVRARDE KNINRDMATG EIEVLASSLT IINRADVLPL DSNHVNTEEA
RLKYRYLDLR RPEMAQRLKT RAKITSLVRR FMDDHGFLDI ETPMLTKATP EGARDYLVPS
RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT
APQVREVMEA LVRHLWLEVK GVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELTDVADLLK
SVEFAVFAGP ANDPKGRVAA LRVPGGASLT RKQIDEYGNF VKIYGAKGLA YIKVNERAKG
LEGINSPVAK FLNAEIIEDI LDRTAAQDGD MIFFGADNKK IVADAMGALR LKVGKDLGLT
DESKWAPLWV IDFPMFEDDG EGGLTAMHHP FTSPKDMTAA ELKAAPENAV ANAYDMVING
YEVGGGSVRI HNGDMQQTVF GILGINEEEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM
LLTGTDNIRD VIAFPKTTAA ACLMTEAPSF ANPTALAELS IQVVKKAENN
Mol. Wt

65.91 kDa (calc) [2]

pI
Extinction coefficient

42860 - 43485 (calc based on 14 Y, 4 W, and 5 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes
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Structure

Structures
  • Representative Escherichia coli structure:
    1C0A|A
    1-585 of 590 residues (E-value: 3.2e-315) (Percent Identity: 100.00)
  • Representative homolog:
    1EOV|A (Saccharomyces cerevisiae)
    84-288 of 590 residues (E-value: 1.7e-20) (Percent Identity: 30.95)
  • View all other structures.
Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:ASPS-MONOMER

UniProt (EcoliWiki Page)

UniProt:P21889

PFAM (EcoliWiki Page)

PFAM:PF01336

RefSeq (EcoliWiki Page)

RefSeq:NP_416380

ModBase (EcoliWiki Page)

ModBase:P21889

PDB (EcoliWiki Page)

PDB:1IL2


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Notes

Links

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NameURLComments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. 5.0 5.1 Martin F et al. (1997) Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant. J Bacteriol 179: 3691-6 PubMed EcoliWiki page


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