Q6BJ61 (PMIP_DEBHA) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	DEHA2G04928g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces › Debaryomyces hansenii › Debaryomyces hansenii var. hansenii

Protein attributes

Sequence length	794 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: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion Potential
	Chain	40 – 794	755	Mitochondrial intermediate peptidase		PRO_0000338583
Sites
	Active site	582	1	By similarity
	Metal binding	581	1	Zinc; catalytic By similarity
	Metal binding	585	1	Zinc; catalytic By similarity
	Metal binding	588	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BJ61 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: C4E8BCE83A403C84	FASTA	794	90,794
	10 20 30 40 50 60 MRVTSSRLLQ GGSLVSRVLK RRLNNASRTK KGWFSTRTLA DSNEHLRRVF DDQAYFDNFT 70 80 90 100 110 120 KSGAPEGAMN SLFGGNGVGL FRNRALISPQ GLVDFSEESL ERAKMLVSNM MAEVKTSEQG 130 140 150 160 170 180 RLEYIKKLDQ LSDVLCRVID VAEFIRVSHP SQKWVDAAQR THEIMFEYMN QLNTNVELYE 190 200 210 220 230 240 SLRDLLIDPA ITTKLSKEEI EVGEYLRQDF ERSGIHMDPN TRNNFVAITQ EISLLGSHFN 250 260 270 280 290 300 NDIHSLESYW CNISRSEFDK ISDTVVKSEI YGYQSSSPAS QNKDSGNIYI PLAGHIPYTI 310 320 330 340 350 360 LSKCEVESVR RKVWISLHNS PKEQIDTLNA FVKYRALLAK MLGYKSFAHY QLEHKMAKNP 370 380 390 400 410 420 ENVLTLLRNL QQGLISKEYG VCEEVKKLHS FKNGDDAVMT DEEILEDVKP WDREYLLAQL 430 440 450 460 470 480 QSQTLKDEEP LEDISEYFSV GTIVSGLSKL FYSIYNVNLI PEATLKGETW DSNQVRKLNV 490 500 510 520 530 540 FDVTSNKKLG YLYLDFWSPK VLPSHFTIVC SRKLNTDIGS ESRDEMREMV QLDENEQHQL 550 560 570 580 590 600 PVISLVCNLS KPQGTGVGRF TGMDSRKPTL LSLDQVDTIF HEMGHAMHSM IGKTDLHNLS 610 620 630 640 650 660 GTRCVTDFVE LPSVLMESFS KDPRVLCKIA KHYRTKEPLS KETLAKHQSH RVLLEESETF 670 680 690 700 710 720 MQSKMAMLDQ VLHNEDIINC GIKDFDSTAV YHHLESQLKV FADKWSTWHG KFPHLFSYGA 730 740 750 760 770 780 VYYSYLLDRA IAEKIWHGLF KDDPWSREAG QKYKDSILKW GGTRDPWVCL ADALGDERLG 790 KGDSKAMEII GQKV

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382139 Genomic DNA. Translation: CAG90217.2.
RefSeq	XP_461760.2. XM_461760.1.
3D structure databases
ProteinModelPortal	Q6BJ61.
ModBase	Search...
Protein-protein interaction databases
STRING	4959.Q6BJ61.
Protein family/group databases
MEROPS	M03.006.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2904636.
KEGG	dha:DEHA2G04928g.
Phylogenomic databases
eggNOG	COG0339.
HOGENOM	HOG000076521.
KO	K01410.
OMA	TQLQVFY.
OrthoDB	EOG4GJ2XS.
Family and domain databases
Gene3D	1.10.1370.10. 2 hits. 1.20.1050.40. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR024079. MetalloPept_cat_dom. IPR024077. Neurolysin/TOP_dom2. IPR024080. Neurolysin/TOP_N. IPR001567. Pept_M3A_M3B. [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_DEBHA

Accession

Primary (citable) accession number: Q6BJ61

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program