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O42908 (CYM1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mitochondrial presequence protease

EC=3.4.24.-
Gene names
Name:cym1
ORF Names:SPBC119.17
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length882 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the peptidase M16 family. PreP subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 882882Mitochondrial presequence protease
PRO_0000178015

Sites

Active site941Proton acceptor By similarity
Metal binding911Zinc; catalytic By similarity
Metal binding951Zinc; catalytic By similarity
Metal binding1921Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
O42908 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 6F1DA9A346717C60

FASTA88298,971
        10         20         30         40         50         60 
MNYAKLSIAF SKKTIKTHNC RLFQRWLHVG DKVHDFRVVD TKKVPELQLN YTRLKHEPTN 

        70         80         90        100        110        120 
ADMIHLDRED PNSVFSIGFQ TPAENDEGIP HILEHTTLCG SNKYPVRDPF FKMLNRSLAT 

       130        140        150        160        170        180 
FMNAFTASDF TFYPFATVNT TDYKNLRDVY LDATLFPKLR KLDFLQEGWR FEHADVNDKK 

       190        200        210        220        230        240 
SPIIFNGVVY NEMKGQVSDS SYIFYMLFQQ HLFQGTAYGF NSGGDPLAIP DLKYEELVKF 

       250        260        270        280        290        300 
HRSHYHPSNA KILSYGSFPL EDNLSALSET FRPFSKRELN LPNTFLKEFD QEKRVVEYGP 

       310        320        330        340        350        360 
LDPVMAPGRQ VKTSISFLAN DTSNVYETFA LKVLSKLCFD GFSSPFYKAL IESGLGTDFA 

       370        380        390        400        410        420 
PNSGYDSTTK RGIFSVGLEG ASEESLAKIE NLVYSIFNDL ALKGFENEKL EAILHQMEIS 

       430        440        450        460        470        480 
LKHKSAHFGI GLAQSLPFNW FNGADPADWL SFNKQIEWLK QKNSDGKLFQ KLIKKYILEN 

       490        500        510        520        530        540 
KSRFVFTMLP SSTFPQRLQE AEAKKLQERT SKLTDEDIAE IEKTSVKLLE AQSTPADTSC 

       550        560        570        580        590        600 
LPTLSVSDIP ETIDETKLKF LDIAGMKAQW YDLAAGLTYI RLLLPLKNFP ESLIPYLPVY 

       610        620        630        640        650        660 
CDACLNLGTH SESIGDLEHQ IRRYTGGISI SPSAVTNNSD VSKYELGIAI SGYALDKNVG 

       670        680        690        700        710        720 
KLVELINKAF WNTNLSNTDK LAIMLKTSVS GITDGIAEKG HSFAKVSSAS GLTEKTSITE 

       730        740        750        760        770        780 
QLGGLTQVKL LSQLSREESF GPLVEKLTAI REILRGTSGF KAAINASPTQ HEVVEKALQK 

       790        800        810        820        830        840 
FMKSRGVNQQ TQTKSTSKER NGINSIKTYH ELPFQTYFAA KSCLGVPYTH PDGAPLQILS 

       850        860        870        880 
SLLTHKYLHG EIREKGGAYG AGLSYSGIDG VLSFFTYRDS DP 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA17932.3.
PIRT39315.

3D structure databases

ProteinModelPortalO42908.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBC119.17-1.

Protein family/group databases

MEROPSM16.A19.

Proteomic databases

PaxDbO42908.
PRIDEO42908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

PomBaseSPBC119.17.

Phylogenomic databases

eggNOGCOG1026.
HOGENOMHOG000008829.
OrthoDBEOG4QRMC5.

Family and domain databases

Gene3D3.30.830.10. 2 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
IPR013578. Peptidase_M16C_assoc.
[Graphical view]
PfamPF08367. M16C_assoc. 1 hit.
PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. Metalloenz_metal-bd. 4 hits.
PROSITEPS00143. INSULINASE. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801247.

Entry information

Entry nameCYM1_SCHPO
AccessionPrimary (citable) accession number: O42908
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families