ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q7SDD5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PMIP_NEUCR
Primary accession number Q7SDD5
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on December 15, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 33)
Name and origin of the protein
Protein name Mitochondrial intermediate peptidase [Precursor]
Synonyms MIP
EC 3.4.24.59
Octapeptidyl aminopeptidase
Gene name
Name: oct-1
ORFNames: NCU02063
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
Comments
  • FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
  • CATALYTIC ACTIVITY: Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.
  • COFACTOR: Binds 1 zinc ion (By similarity).
  • SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
  • SIMILARITY: Belongs to the peptidase M3 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AABX02000003; EAA34783.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_964019.1; -.
3D structure databases
ModBase Q7SDD5.
Protein family/group databases
MEROPS M03.006; -.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001567; Pept_M3A_M3B.
IPR006025; Pept_M_Zn_BS.
Graphical view of domain structure.
Pfam PF01432; Peptidase_M3; 1.
Pfam graphical view of domain structure.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS Q7SDD5.
ProtoNet Q7SDD5.
Genome annotation databases
GeneID 3880168; -.
KEGG ncr:NCU02063; -.
NMPDR fig|5141.1.peg.7186; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease; Transit peptide; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    25  25     Mitochondrion (Potential). 
CHAIN   26   805  780     Mitochondrial intermediate peptidase. PRO_0000338590
ACT_SITE   579   579        By similarity. 
METAL   578   578        Zinc; catalytic (By similarity). 
METAL   582   582        Zinc; catalytic (By similarity). 
METAL   585   585        Zinc; catalytic (By similarity). 
Sequence information
Length: 805 AA [This is the length of the unprocessed precursor] Molecular weight: 91095 Da [This is the MW of the unprocessed precursor] CRC64: 8F2F597AB9BD2130 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIQPLVKASR PRLWVCSDCL LRRTLSPLLR QQRRRFTGFT AHAPKTLTGT IPVTHKNGDT 

        70         80         90        100        110        120 
KHDDSLLRSI FDSPETWKQF SGDKHGRNVG LFRNAYLTSP HGFLDFAHVS LGKARALVDK 

       130        140        150        160        170        180 
VLNAQSLDEY RAIVRHLDRL SDILCRVLDM ADFVRVTHPD QQIQRTASMA WDMMYEYMNQ 

       190        200        210        220        230        240 
LNTMTGLYDQ LVQAMDNPQV STTWSEEERM VAEVLKLDFA KSAVHLPKDA RDKFVHLSSA 

       250        260        270        280        290        300 
ISQTGTNFIQ HMEPKIPYTT VEKSRMMGMD PVEVKRMASM GKVYVQTLSP QASIALRTVR 

       310        320        330        340        350        360 
DDHARHQLFM ASRTASRRTV HTLEELMLLR GESAKLSGFE SYGHLVLHDR MMASTPESVR 

       370        380        390        400        410        420 
QFLQALSENT RPQAQQEVAD LTAAKRAHKG GDATLEPWDK DFYAESIRQA IKSRQKREDL 

       430        440        450        460        470        480 
SSYFSLGTVM QGLSRIFTRL YGIRFVPREP MPGETWHPDV RRLDVVSDVE GHVAVLYCDL 

       490        500        510        520        530        540 
FYRPLKSPNP AHFTLRCSRE LSPHEIAETA HTQAENPHVL IPSFESAEFA ANDGMAYSRS 

       550        560        570        580        590        600 
QDGAIKQLPT IALVCDFPQQ SHNRPALLSF FQLETLFHEM GHAIHSILAR TSFQNVSGTR 

       610        620        630        640        650        660 
CATDLAELPS TLMEYFAADP SVLALFARHY ETDNPLPYEW VDNKIREARR FEALDTENQI 

       670        680        690        700        710        720 
ILAMLDQELH SSKAVQGHID STEIFHSLQR QFSTAPPDPQ GTAWQGFFGH LVGYGSTYYS 

       730        740        750        760        770        780 
YLFDRVLAQR VWNVVFNSGQ GGAALQRENG ERLKENLLKW GGSKDPWKCL AGALKDERLE 

       790        800 
GGGEKAMKLV GSWGGQRGTK SDQAV
Q7SDD5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!