Reviewed, UniProtKB/Swiss-Prot A1DMR2 (PMIP_NEOFI)

Names and origin

Protein names

Recommended name:
    Mitochondrial intermediate peptidase
      Short name=MIP
    EC=3.4.24.59
Alternative name(s):
    Octapeptidyl aminopeptidase

Gene names

Name:	oct1
ORF Names:	NFIA_054290

Organism

Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]

Taxonomic identifier

331117 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya

Protein attributes

Sequence length	801 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (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.
Sequence similarities	Belongs to the peptidase M3 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Mitochondrion Potential
	Chain	43 – 801	759	Mitochondrial intermediate peptidase		PRO_0000338589
Sites
	Active site	566	1	By similarity
	Metal binding	565	1	Zinc; catalytic By similarity
	Metal binding	569	1	Zinc; catalytic By similarity
	Metal binding	572	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1DMR2-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 906514456D11365F	FASTA	801	89,774
	10 20 30 40 50 60 MKDQLLVPLR RRPWTCRKCL QRLQLLPQHQ TRRSFETAAS PFPRQLDSLP ADYSRTKTVD 70 80 90 100 110 120 DDTLRRVFDS QQFWREFSQQ RSAQPKPTGL VQNQYLTSPD GFRTFANVSL QKCQAIVSKV 130 140 150 160 170 180 LAASTLEEYR TMARDLDRLS DLLCRVIDLS DFIRVIHPDP QVQEAATQAY ALMFEYMNVL 190 200 210 220 230 240 NTTTGLNDQL KKAAANPEVT SQWSDEEKIV AQILIKDFSN SAIHMPPHER QRFVNLSNDI 250 260 270 280 290 300 SQLGSSFVNG AEPAKSHVSV ATNNLRGLDP ILVQQIKRWN RTAAVPTTGM IPRLALRSVH 310 320 330 340 350 360 DENVRREVYL ASRTSSKRQL HRLEELLLKR AELAKLSGYE SFAHMTLSDK MAKSPEAVSN 370 380 390 400 410 420 FLTALVDSNR KLVREELSQL QAMKGAPLQP WDHAYYVHQR VMQYSQARRS RELSAVPEFF 430 440 450 460 470 480 SLGTVMQGLS RLFDRLYGVR LVPQEPAPGE TWNPDVRRLD VVDESGRHIA VIYCDLFSRP 490 500 510 520 530 540 NKHPNPAHFT LRCSREISTE EVAECASLDQ SSHPNDGMAT AVDPVTKTLR QLPTIALVCD 550 560 570 580 590 600 FSEPGTNGGG RPSLLSEHSV RTLFHEMGHA VHSILGQTRL QSISGTRCAT DFAELPSVLM 610 620 630 640 650 660 EHFATAPSVL ALYARHWRTD EPLSEGMIRS MERDRTAHGS IYGAVENEAQ ILMALVDQAY 670 680 690 700 710 720 HSRPADGGRI DSTALYQQVS QQHSSLPEPA DVTPPTSWQG FFGHLYGYGA TYYSYIFDRA 730 740 750 760 770 780 IANKLWVDVF GAGRQAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE 790 800 GGDEAMREVG RWGLGRDGVS G

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DS027698 Genomic DNA. Translation: EAW16083.1.
RefSeq	XP_001257980.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M03.006.
Genome annotation databases
GeneID	4584495.
KEGG	nfi:NFIA_054290.
Family and domain databases
InterPro	IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view]
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PMIP_NEOFI

Accession

Primary (citable) accession number: A1DMR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)