Skip Header

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

Endothiapepsin

Gene

EAPA

Organism
Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241
Active sitei288 – 2881

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.22. 2077.

Protein family/group databases

MEROPSiA01.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothiapepsin (EC:3.4.23.22)
Alternative name(s):
Aspartate protease
Gene namesi
Name:EAPA
Synonyms:EPN-1
OrganismiCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifieri5116 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Pathology & Biotechi

Protein family/group databases

Allergomei3881. Cry p AP.

Chemistry

ChEMBLiCHEMBL1075067.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 8969Activation peptide1 PublicationPRO_0000025879Add
BLAST
Chaini90 – 419330EndothiapepsinPRO_0000025880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi344 ↔ 379

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Chemistry

BindingDBiP11838.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 1009Combined sources
Beta strandi106 – 1127Combined sources
Turni113 – 1164Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi130 – 1323Combined sources
Helixi139 – 1413Combined sources
Helixi150 – 1523Combined sources
Beta strandi157 – 16711Combined sources
Beta strandi173 – 18513Combined sources
Beta strandi188 – 20114Combined sources
Helixi203 – 2075Combined sources
Beta strandi213 – 2164Combined sources
Helixi220 – 2223Combined sources
Beta strandi226 – 2283Combined sources
Helixi233 – 2375Combined sources
Turni238 – 2403Combined sources
Beta strandi241 – 2499Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi256 – 2616Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi285 – 2939Combined sources
Beta strandi299 – 3079Combined sources
Beta strandi313 – 3164Combined sources
Helixi318 – 3258Combined sources
Beta strandi332 – 3343Combined sources
Turni335 – 3384Combined sources
Beta strandi339 – 3435Combined sources
Beta strandi351 – 3555Combined sources
Beta strandi358 – 3625Combined sources
Helixi364 – 3674Combined sources
Beta strandi368 – 3736Combined sources
Beta strandi377 – 38610Combined sources
Turni387 – 3893Combined sources
Beta strandi390 – 3945Combined sources
Helixi396 – 3994Combined sources
Beta strandi402 – 4076Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi413 – 4186Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5OX-ray2.05E90-419[»]
1E80X-ray2.05E90-419[»]
1E81X-ray2.05E90-419[»]
1E82X-ray2.05E90-419[»]
1EEDX-ray2.00P90-419[»]
1ENTX-ray1.90E90-419[»]
1EPLX-ray2.00E90-419[»]
1EPMX-ray1.60E90-419[»]
1EPNX-ray1.60E90-419[»]
1EPOX-ray2.00E90-419[»]
1EPPX-ray1.90E90-419[»]
1EPQX-ray1.90E90-419[»]
1EPRX-ray2.30E90-419[»]
1ER8X-ray2.00E90-419[»]
1GKTneutron diffraction2.10A90-419[»]
1GVTX-ray0.98A90-419[»]
1GVUX-ray0.94A90-419[»]
1GVVX-ray1.05A90-419[»]
1GVWX-ray1.00A90-419[»]
1GVXX-ray1.00A90-419[»]
1OD1X-ray1.37A90-419[»]
1OEWX-ray0.90A90-419[»]
1OEXX-ray1.10A90-419[»]
2ER0X-ray3.00E90-419[»]
2ER6X-ray2.00E90-419[»]
2ER7X-ray1.60E90-419[»]
2ER9X-ray2.20E90-419[»]
2JJIX-ray1.57A90-419[»]
2JJJX-ray1.00A90-419[»]
2V00X-ray1.55A90-419[»]
2VS2neutron diffraction2.00A90-419[»]
3ER3X-ray2.00E90-419[»]
3ER5X-ray1.80E90-419[»]
3LZYX-ray1.80A90-419[»]
3PB5X-ray1.90A90-419[»]
3PBDX-ray1.70A90-419[»]
3PBZX-ray1.48A90-419[»]
3PCWX-ray1.25A90-419[»]
3PCZX-ray1.50A90-419[»]
3PGIX-ray1.90A90-419[»]
3PI0X-ray1.64A90-419[»]
3PLDX-ray1.40A90-419[»]
3PLLX-ray1.73A90-419[»]
3PM4X-ray1.68A90-419[»]
3PMUX-ray1.43A90-419[»]
3PMYX-ray1.38A90-419[»]
3PRSX-ray1.38A90-419[»]
3PSYX-ray1.43A90-419[»]
3PWWX-ray1.22A90-419[»]
3Q6YX-ray1.35A90-419[»]
3T6IX-ray1.32A90-419[»]
3T7PX-ray1.35A90-419[»]
3T7QX-ray1.30A90-419[»]
3T7XX-ray1.27A90-419[»]
3URIX-ray2.10A90-419[»]
3URJX-ray1.90A90-419[»]
3URLX-ray2.00A90-419[»]
3WZ6X-ray1.40A90-419[»]
3WZ7X-ray1.90A90-419[»]
3WZ8X-ray1.45A90-419[»]
4APEX-ray2.10A90-419[»]
4ER1X-ray2.00E90-419[»]
4ER2X-ray2.00E90-419[»]
4ER4X-ray2.10E90-419[»]
4KUPX-ray1.31A90-419[»]
4L6BX-ray1.37A90-419[»]
4LAPX-ray1.12A90-419[»]
4LBTX-ray1.25A90-419[»]
4LHHX-ray1.73A90-419[»]
4LP9X-ray1.35A90-419[»]
4Y35X-ray1.46A90-419[»]
4Y36X-ray1.59A90-419[»]
4Y37X-ray1.69A90-419[»]
4Y38X-ray1.10A90-419[»]
4Y39X-ray1.20A90-419[»]
4Y3AX-ray1.17A90-419[»]
4Y3DX-ray1.48A90-419[»]
4Y3EX-ray1.25A90-419[»]
4Y3FX-ray1.40A90-419[»]
4Y3GX-ray1.13A90-419[»]
4Y3HX-ray1.23A90-419[»]
4Y3JX-ray1.31A90-419[»]
4Y3LX-ray1.16A90-419[»]
4Y3MX-ray1.55A90-419[»]
4Y3NX-ray1.34A90-419[»]
4Y3PX-ray1.55A90-419[»]
4Y3QX-ray1.17A90-419[»]
4Y3RX-ray1.13A90-419[»]
4Y3SX-ray1.10A90-419[»]
4Y3TX-ray1.42A90-419[»]
4Y3WX-ray1.58A90-419[»]
4Y3XX-ray1.25A90-419[»]
4Y3YX-ray1.35A90-419[»]
4Y3ZX-ray1.12A90-419[»]
4Y41X-ray1.40A90-419[»]
4Y43X-ray1.48A90-419[»]
4Y44X-ray1.24A90-419[»]
4Y45X-ray1.06A90-419[»]
4Y47X-ray1.19A90-419[»]
4Y48X-ray1.25A90-419[»]
4Y4AX-ray1.28A90-419[»]
4Y4BX-ray1.11A90-419[»]
4Y4CX-ray1.24A90-419[»]
4Y4DX-ray1.27A90-419[»]
4Y4EX-ray1.30A90-419[»]
4Y4GX-ray1.44A90-419[»]
4Y4JX-ray1.03A90-419[»]
4Y4TX-ray1.30A90-419[»]
4Y4UX-ray1.75A90-419[»]
4Y4WX-ray1.45A90-419[»]
4Y4XX-ray1.67A90-419[»]
4Y4ZX-ray1.48A90-419[»]
4Y50X-ray1.32A90-419[»]
4Y51X-ray1.60A90-419[»]
4Y53X-ray1.62A90-419[»]
4Y54X-ray1.61A90-419[»]
4Y56X-ray1.63A90-419[»]
4Y57X-ray1.49A90-419[»]
4Y58X-ray1.17A90-419[»]
4Y5AX-ray1.45A90-419[»]
4Y5BX-ray1.24A90-419[»]
4Y5CX-ray1.19A90-419[»]
4Y5EX-ray1.12A90-419[»]
4Y5GX-ray1.47A90-419[»]
4Y5KX-ray1.44A90-419[»]
4Y5LX-ray0.99A90-419[»]
4Y5MX-ray1.28A90-419[»]
4Y5NX-ray1.29A90-419[»]
4Y5PX-ray1.23A90-419[»]
4YCKX-ray1.07A90-419[»]
4YCTX-ray1.13A90-419[»]
4YCYX-ray1.70A90-419[»]
4YD3X-ray1.25A90-419[»]
4YD4X-ray1.27A90-419[»]
4YD5X-ray1.21A90-419[»]
4YD6X-ray1.30A90-419[»]
4YD7X-ray1.42A90-419[»]
5ER1X-ray2.00E90-419[»]
5ER2X-ray1.80E90-419[»]
ProteinModelPortaliP11838.
SMRiP11838. Positions 90-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 417312Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

OMAiICKASIA.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPLKNALV TAMLAGGALS SPTKQHVGIP VNASPEVGPG KYSFKQVRNP
60 70 80 90 100
NYKFNGPLSV KKTYLKYGVP IPAWLEDAVQ NSTSGLAERS TGSATTTPID
110 120 130 140 150
SLDDAYITPV QIGTPAQTLN LDFDTGSSDL WVFSSETTAS EVDGQTIYTP
160 170 180 190 200
SKSTTAKLLS GATWSISYGD GSSSSGDVYT DTVSVGGLTV TGQAVESAKK
210 220 230 240 250
VSSSFTEDST IDGLLGLAFS TLNTVSPTQQ KTFFDNAKAS LDSPVFTADL
260 270 280 290 300
GYHAPGTYNF GFIDTTAYTG SITYTAVSTK QGFWEWTSTG YAVGSGTFKS
310 320 330 340 350
TSIDGIADTG TTLLYLPATV VSAYWAQVSG AKSSSSVGGY VFPCSATLPS
360 370 380 390 400
FTFGVGSARI VIPGDYIDFG PISTGSSSCF GGIQSSAGIG INIFGDVALK
410
AAFVVFNGAT TPTLGFASK
Length:419
Mass (Da):43,255
Last modified:October 1, 1993 - v2
Checksum:i262D13F1D2F13296
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63351 Genomic DNA. Translation: CAA44952.1.
X53997 Genomic DNA. Translation: CAA37944.1.
PIRiS22136.

Genome annotation databases

KEGGiag:CAA44952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63351 Genomic DNA. Translation: CAA44952.1.
X53997 Genomic DNA. Translation: CAA37944.1.
PIRiS22136.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5OX-ray2.05E90-419[»]
1E80X-ray2.05E90-419[»]
1E81X-ray2.05E90-419[»]
1E82X-ray2.05E90-419[»]
1EEDX-ray2.00P90-419[»]
1ENTX-ray1.90E90-419[»]
1EPLX-ray2.00E90-419[»]
1EPMX-ray1.60E90-419[»]
1EPNX-ray1.60E90-419[»]
1EPOX-ray2.00E90-419[»]
1EPPX-ray1.90E90-419[»]
1EPQX-ray1.90E90-419[»]
1EPRX-ray2.30E90-419[»]
1ER8X-ray2.00E90-419[»]
1GKTneutron diffraction2.10A90-419[»]
1GVTX-ray0.98A90-419[»]
1GVUX-ray0.94A90-419[»]
1GVVX-ray1.05A90-419[»]
1GVWX-ray1.00A90-419[»]
1GVXX-ray1.00A90-419[»]
1OD1X-ray1.37A90-419[»]
1OEWX-ray0.90A90-419[»]
1OEXX-ray1.10A90-419[»]
2ER0X-ray3.00E90-419[»]
2ER6X-ray2.00E90-419[»]
2ER7X-ray1.60E90-419[»]
2ER9X-ray2.20E90-419[»]
2JJIX-ray1.57A90-419[»]
2JJJX-ray1.00A90-419[»]
2V00X-ray1.55A90-419[»]
2VS2neutron diffraction2.00A90-419[»]
3ER3X-ray2.00E90-419[»]
3ER5X-ray1.80E90-419[»]
3LZYX-ray1.80A90-419[»]
3PB5X-ray1.90A90-419[»]
3PBDX-ray1.70A90-419[»]
3PBZX-ray1.48A90-419[»]
3PCWX-ray1.25A90-419[»]
3PCZX-ray1.50A90-419[»]
3PGIX-ray1.90A90-419[»]
3PI0X-ray1.64A90-419[»]
3PLDX-ray1.40A90-419[»]
3PLLX-ray1.73A90-419[»]
3PM4X-ray1.68A90-419[»]
3PMUX-ray1.43A90-419[»]
3PMYX-ray1.38A90-419[»]
3PRSX-ray1.38A90-419[»]
3PSYX-ray1.43A90-419[»]
3PWWX-ray1.22A90-419[»]
3Q6YX-ray1.35A90-419[»]
3T6IX-ray1.32A90-419[»]
3T7PX-ray1.35A90-419[»]
3T7QX-ray1.30A90-419[»]
3T7XX-ray1.27A90-419[»]
3URIX-ray2.10A90-419[»]
3URJX-ray1.90A90-419[»]
3URLX-ray2.00A90-419[»]
3WZ6X-ray1.40A90-419[»]
3WZ7X-ray1.90A90-419[»]
3WZ8X-ray1.45A90-419[»]
4APEX-ray2.10A90-419[»]
4ER1X-ray2.00E90-419[»]
4ER2X-ray2.00E90-419[»]
4ER4X-ray2.10E90-419[»]
4KUPX-ray1.31A90-419[»]
4L6BX-ray1.37A90-419[»]
4LAPX-ray1.12A90-419[»]
4LBTX-ray1.25A90-419[»]
4LHHX-ray1.73A90-419[»]
4LP9X-ray1.35A90-419[»]
4Y35X-ray1.46A90-419[»]
4Y36X-ray1.59A90-419[»]
4Y37X-ray1.69A90-419[»]
4Y38X-ray1.10A90-419[»]
4Y39X-ray1.20A90-419[»]
4Y3AX-ray1.17A90-419[»]
4Y3DX-ray1.48A90-419[»]
4Y3EX-ray1.25A90-419[»]
4Y3FX-ray1.40A90-419[»]
4Y3GX-ray1.13A90-419[»]
4Y3HX-ray1.23A90-419[»]
4Y3JX-ray1.31A90-419[»]
4Y3LX-ray1.16A90-419[»]
4Y3MX-ray1.55A90-419[»]
4Y3NX-ray1.34A90-419[»]
4Y3PX-ray1.55A90-419[»]
4Y3QX-ray1.17A90-419[»]
4Y3RX-ray1.13A90-419[»]
4Y3SX-ray1.10A90-419[»]
4Y3TX-ray1.42A90-419[»]
4Y3WX-ray1.58A90-419[»]
4Y3XX-ray1.25A90-419[»]
4Y3YX-ray1.35A90-419[»]
4Y3ZX-ray1.12A90-419[»]
4Y41X-ray1.40A90-419[»]
4Y43X-ray1.48A90-419[»]
4Y44X-ray1.24A90-419[»]
4Y45X-ray1.06A90-419[»]
4Y47X-ray1.19A90-419[»]
4Y48X-ray1.25A90-419[»]
4Y4AX-ray1.28A90-419[»]
4Y4BX-ray1.11A90-419[»]
4Y4CX-ray1.24A90-419[»]
4Y4DX-ray1.27A90-419[»]
4Y4EX-ray1.30A90-419[»]
4Y4GX-ray1.44A90-419[»]
4Y4JX-ray1.03A90-419[»]
4Y4TX-ray1.30A90-419[»]
4Y4UX-ray1.75A90-419[»]
4Y4WX-ray1.45A90-419[»]
4Y4XX-ray1.67A90-419[»]
4Y4ZX-ray1.48A90-419[»]
4Y50X-ray1.32A90-419[»]
4Y51X-ray1.60A90-419[»]
4Y53X-ray1.62A90-419[»]
4Y54X-ray1.61A90-419[»]
4Y56X-ray1.63A90-419[»]
4Y57X-ray1.49A90-419[»]
4Y58X-ray1.17A90-419[»]
4Y5AX-ray1.45A90-419[»]
4Y5BX-ray1.24A90-419[»]
4Y5CX-ray1.19A90-419[»]
4Y5EX-ray1.12A90-419[»]
4Y5GX-ray1.47A90-419[»]
4Y5KX-ray1.44A90-419[»]
4Y5LX-ray0.99A90-419[»]
4Y5MX-ray1.28A90-419[»]
4Y5NX-ray1.29A90-419[»]
4Y5PX-ray1.23A90-419[»]
4YCKX-ray1.07A90-419[»]
4YCTX-ray1.13A90-419[»]
4YCYX-ray1.70A90-419[»]
4YD3X-ray1.25A90-419[»]
4YD4X-ray1.27A90-419[»]
4YD5X-ray1.21A90-419[»]
4YD6X-ray1.30A90-419[»]
4YD7X-ray1.42A90-419[»]
5ER1X-ray2.00E90-419[»]
5ER2X-ray1.80E90-419[»]
ProteinModelPortaliP11838.
SMRiP11838. Positions 90-419.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP11838.
ChEMBLiCHEMBL1075067.

Protein family/group databases

Allergomei3881. Cry p AP.
MEROPSiA01.017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA44952.

Phylogenomic databases

OMAiICKASIA.

Enzyme and pathway databases

BRENDAi3.4.23.22. 2077.

Miscellaneous databases

EvolutionaryTraceiP11838.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and mutation of the gene encoding endothiapepsin from Cryphonectria parasitica."
    Razanamparany V., Jara P., Legoux R., Delmas P., Msayeh F., Kaghad M., Loison G.
    Curr. Genet. 21:455-461(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular analysis and overexpression of the gene encoding endothiapepsin, an aspartic protease from Cryphonectria parasitica."
    Choi G.H., Pawlyk D.M., Rae B., Shapira R., Nuss D.L.
    Gene 125:135-141(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 38755 / EP155.
  3. "Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica."
    Barkholt V.
    Eur. J. Biochem. 167:327-338(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 90-419.
  4. "Homology among acid proteases: comparison of crystal structures at 3-A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica."
    Subramanian E., Swan I.D.A., Liu M., Davies D.R., Jenkins J.A., Tickle I.J., Blundell T.L.
    Proc. Natl. Acad. Sci. U.S.A. 74:556-559(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 90-419.
  5. "X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1-A resolution of endothiapepsin."
    Blundell T.L., Jenkins J.A., Sewell B.T., Pearl L.H., Cooper J.B., Tickle I.J., Veerapandian B., Wood S.P.
    J. Mol. Biol. 211:919-941(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 90-419.
  6. "High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme."
    Sali A., Veerapandian B., Cooper J.B., Foundling S.I., Hoover D.J., Blundell T.L.
    EMBO J. 8:2179-2188(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 90-419.
  7. "Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism."
    Coates L., Erskine P.T., Crump M.P., Wood S.P., Cooper J.B.
    J. Mol. Biol. 318:1405-1415(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS) OF 90-419.

Entry informationi

Entry nameiCARP_CRYPA
AccessioniPrimary (citable) accession number: P11838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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.