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Protein
Submitted name:

Falcipain 2

Gene
N/A
Organism
Plasmodium falciparum
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15378.
BRENDAi3.4.22.B69. 4889.
SABIO-RKQ9N6S8.

Protein family/group databases

MEROPSiC01.046.

Names & Taxonomyi

Protein namesi
Submitted name:
Falcipain 2Imported
OrganismiPlasmodium falciparumImported
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei36 – 5520HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5800.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi282 ↔ 323Combined sources
Disulfide bondi316 ↔ 357Combined sources
Disulfide bondi342 ↔ 362Combined sources
Disulfide bondi411 ↔ 472Combined sources

Interactioni

Protein-protein interaction databases

DIPiDIP-59137N.
STRINGi5833.PF11_0165.

Chemistry

BindingDBiQ9N6S8.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YVBX-ray2.70A244-484[»]
2GHUX-ray3.10A/B/C/D244-484[»]
3BPFX-ray2.90A/B/C/D244-484[»]
3PNRX-ray2.60A245-484[»]
SMRiQ9N6S8. Positions 244-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini165 – 22258Inhibitor_I29InterPro annotationAdd
BLAST
Domaini261 – 482222Pept_C1InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C1 family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9N6S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYNMDYAPH EVISQQGERF VDKYVDRKIL KNKKSLLVII SLSVLSVVGF
60 70 80 90 100
VLFYFTPNSR KSDLFKNSSV ENNNDDYIIN SLLKSPNGKK FIVSKIDEAL
110 120 130 140 150
SFYDSKKNDI NKYNEGNNNN NADFKGLSLF KENTPSNNFI HNKDYFINFF
160 170 180 190 200
DNKFLMNNAE HINQFYMFIK TNNKQYNSPN EMKERFQVFL QNAHKVNMHN
210 220 230 240 250
NNKNSLYKKE LNRFADLTYH EFKNKYLSLR SSKPLKNSKY LLDQMNYEEV
260 270 280 290 300
IKKYRGEENF DHAAYDWRLH SGVTPVKDQK NCGSCWAFSS IGSVESQYAI
310 320 330 340 350
RKNKLITLSE QELVDCSFKN YGCNGGLINN AFEDMIELGG ICPDGDYPYV
360 370 380 390 400
SDAPNLCNID RCTEKYGIKN YLSVPDNKLK EALRFLGPIS ISVAVSDDFA
410 420 430 440 450
FYKEGIFDGE CGDQLNHAVM LVGFGMKEIV NPLTKKGEKH YYYIIKNSWG
460 470 480
QQWGERGFIN IETDESGLMR KCGLGTDAFI PLIE
Length:484
Mass (Da):55,908
Last modified:October 1, 2000 - v1
Checksum:i092960919F4D43C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239801 mRNA. Translation: AAF63497.1.
AF282975 Genomic DNA. Translation: AAF97805.1.
AF282976 Genomic DNA. Translation: AAF97806.1.
AF282977 Genomic DNA. Translation: AAF97807.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239801 mRNA. Translation: AAF63497.1.
AF282975 Genomic DNA. Translation: AAF97805.1.
AF282976 Genomic DNA. Translation: AAF97806.1.
AF282977 Genomic DNA. Translation: AAF97807.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YVBX-ray2.70A244-484[»]
2GHUX-ray3.10A/B/C/D244-484[»]
3BPFX-ray2.90A/B/C/D244-484[»]
3PNRX-ray2.60A245-484[»]
SMRiQ9N6S8. Positions 244-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59137N.
STRINGi5833.PF11_0165.

Chemistry

BindingDBiQ9N6S8.
ChEMBLiCHEMBL5800.

Protein family/group databases

MEROPSiC01.046.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15378.
BRENDAi3.4.22.B69. 4889.
SABIO-RKQ9N6S8.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum."
    Shenai B.R., Sijwali P.S., Singh A., Rosenthal P.J.
    J. Biol. Chem. 275:29000-29010(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Comparison of efficacies of cysteine protease inhibitors against five strains of Plasmodium falciparum."
    Singh A., Rosenthal P.J.
    Antimicrob. Agents Chemother. 45:949-951(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: D6Imported.
  3. "Structural and functional characterization of Falcipain-2, a hemoglobinase from the malarial parasite Plasmodium falciparum."
    Hogg T., Nagarajan K., Herzberg S., Chen L., Shen X., Jiang H., Wecke M., Blohmke C., Hilgenfeld R., Schmidt C.L.
    J. Biol. Chem. 281:25425-25437(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 244-484, DISULFIDE BONDS.
  4. "Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease."
    Wang S.X., Pandey K.C., Somoza J.R., Sijwali P.S., Kortemme T., Brinen L.S., Fletterick R.J., Rosenthal P.J., McKerrow J.H.
    Proc. Natl. Acad. Sci. U.S.A. 103:11503-11508(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 244-484, DISULFIDE BONDS.
  5. "Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity."
    Kerr I.D., Lee J.H., Pandey K.C., Harrison A., Sajid M., Rosenthal P.J., Brinen L.S.
    J. Med. Chem. 52:852-857(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 244-484, DISULFIDE BONDS.
  6. "Structural basis for the regulation of cysteine-protease activity by a new class of protease inhibitors in Plasmodium."
    Hansen G., Heitmann A., Witt T., Li H., Jiang H., Shen X., Heussler V.T., Rennenberg A., Hilgenfeld R.
    Structure 19:919-929(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 245-484, DISULFIDE BONDS.

Entry informationi

Entry nameiQ9N6S8_PLAFA
AccessioniPrimary (citable) accession number: Q9N6S8
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.