Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

C1A138

- AMPA_RHOE4

UniProt

C1A138 - AMPA_RHOE4

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Probable cytosol aminopeptidase

Gene

pepA

Organism
Rhodococcus erythropolis (strain PR4 / NBRC 100887)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.UniRule annotation

Catalytic activityi

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.UniRule annotation
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.UniRule annotation

Cofactori

Mn2+UniRule annotationNote: Binds 2 manganese ions per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi269 – 2691Manganese 2UniRule annotation
Metal bindingi274 – 2741Manganese 1UniRule annotation
Metal bindingi274 – 2741Manganese 2UniRule annotation
Active sitei281 – 2811UniRule annotation
Metal bindingi292 – 2921Manganese 2UniRule annotation
Metal bindingi351 – 3511Manganese 1UniRule annotation
Metal bindingi353 – 3531Manganese 1UniRule annotation
Metal bindingi353 – 3531Manganese 2UniRule annotation
Active sitei355 – 3551UniRule annotation

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-HAMAP
  2. manganese ion binding Source: UniProtKB-HAMAP
  3. metalloexopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciRERY234621:GHDE-3657-MONOMER.

Protein family/group databases

MEROPSiM17.950.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cytosol aminopeptidaseUniRule annotation (EC:3.4.11.1UniRule annotation)
Alternative name(s):
Leucine aminopeptidaseUniRule annotation (EC:3.4.11.10UniRule annotation)
Short name:
LAPUniRule annotation
Leucyl aminopeptidaseUniRule annotation
Gene namesi
Name:pepAUniRule annotation
Ordered Locus Names:RER_36150
OrganismiRhodococcus erythropolis (strain PR4 / NBRC 100887)
Taxonomic identifieri234621 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
ProteomesiUP000002204: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Probable cytosol aminopeptidasePRO_1000203838Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi234621.RER_36150.

Structurei

3D structure databases

ProteinModelPortaliC1A138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0260.
HOGENOMiHOG000243129.
KOiK01255.
OMAiGMENMTS.
OrthoDBiEOG6FV8B3.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C1A138-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTRTARSLG PDLVLAGTVA KRAEILVVGL TSGPDGPEIA LSEGIVAEDV
60 70 80 90 100
LAEILDSLIA VGATGKPEQL TRVPAPSALS VTSVLAVGLG SADKLDSEQI
110 120 130 140 150
RKSAGAAARS LSGIDTVATT LSILDLGAAA EGFALGAYSF TEFKSSMTAP
160 170 180 190 200
GPDSQPLARV ELLVPSPRTK ETKATLARSA AIAEAVATAR EFVNTPPSHL
210 220 230 240 250
YPAEFAARAK ALGVEAGLTV QVLDEKALEK GGYGGIIGVG KGSSRQPRLV
260 270 280 290 300
RLEYASKKRG ARKVALVGKG ITFDTGGISI KPAAGMENMT SDMGGAAAVI
310 320 330 340 350
STVVLAAKLG LPVNVVAYVP MAENMPSATA QRPGDVLTQY GGITIEVVNT
360 370 380 390 400
DAEGRLILAD AMVRAGEDNP DYMIDTATLT GAQMVALGNR TPGVMGTDEF
410 420 430 440 450
RDRVASISQS VGENGWAMPL PEELRGDLDS KVADMANVTP HRWGGMLVAA
460 470 480 490 500
HYLKEFVPEG VQWAHIDVAG PAYNTSGPWG YTGKGGTGVP VRTMISVLED

IAVNG
Length:505
Mass (Da):52,012
Last modified:May 26, 2009 - v1
Checksum:i437D2EFC0C97E40A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008957 Genomic DNA. Translation: BAH34323.1.
RefSeqiYP_002767062.1. NC_012490.1.

Genome annotation databases

EnsemblBacteriaiBAH34323; BAH34323; RER_36150.
GeneIDi7715119.
KEGGirer:RER_36150.
PATRICi23193706. VBIRhoEry66701_4131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008957 Genomic DNA. Translation: BAH34323.1 .
RefSeqi YP_002767062.1. NC_012490.1.

3D structure databases

ProteinModelPortali C1A138.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 234621.RER_36150.

Protein family/group databases

MEROPSi M17.950.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH34323 ; BAH34323 ; RER_36150 .
GeneIDi 7715119.
KEGGi rer:RER_36150.
PATRICi 23193706. VBIRhoEry66701_4131.

Phylogenomic databases

eggNOGi COG0260.
HOGENOMi HOG000243129.
KOi K01255.
OMAi GMENMTS.
OrthoDBi EOG6FV8B3.

Enzyme and pathway databases

BioCyci RERY234621:GHDE-3657-MONOMER.

Family and domain databases

HAMAPi MF_00181. Cytosol_peptidase_M17.
InterProi IPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view ]
Pfami PF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view ]
PRINTSi PR00481. LAMNOPPTDASE.
PROSITEi PS00631. CYTOSOL_AP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
    Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PR4 / NBRC 100887.

Entry informationi

Entry nameiAMPA_RHOE4
AccessioniPrimary (citable) accession number: C1A138
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: November 26, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3