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Protein

Methionine aminopeptidase 1D, mitochondrial

Gene

metap1d

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei164 – 1641SubstrateUniRule annotation
Metal bindingi181 – 1811Divalent metal cation 1UniRule annotation
Metal bindingi192 – 1921Divalent metal cation 1UniRule annotation
Metal bindingi192 – 1921Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi255 – 2551Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Metal bindingi287 – 2871Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi318 – 3181Divalent metal cation 1UniRule annotation
Metal bindingi318 – 3181Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.028.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1D, mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1DUniRule annotation
Short name:
MetAP 1DUniRule annotation
Alternative name(s):
Methionyl aminopeptidase type 1D, mitochondrial
Peptidase M 1DUniRule annotation
Gene namesi
Name:metap1d
Synonyms:map1d
ORF Names:zgc:110461
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-050522-71. metap1d.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747MitochondrionUniRule annotationAdd
BLAST
Chaini48 – 338291Methionine aminopeptidase 1D, mitochondrialPRO_0000314128Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000010471.

Structurei

3D structure databases

ProteinModelPortaliQ4VBS4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
HOVERGENiHBG067178.
InParanoidiQ4VBS4.
KOiK01265.
PhylomeDBiQ4VBS4.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q4VBS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPCAAQCL YRTGGLRLLQ RISRLPHCHK DASLAHQCQF HRSFFWRKPK
60 70 80 90 100
TSHSVVRPAI VRPAYPVPKH IQRPDYVSSS KVPEWPDYIE IKDEEQIQGL
110 120 130 140 150
RRACQLARHI LLLTGNSLKV GMTTDEIDFI VHQEAIRHNG YPSPLHYGGF
160 170 180 190 200
PKSVCTSVNN VVCHGIPDSR PLQDGDIINI DVTVYLEGYH GDTSETFLIG
210 220 230 240 250
SVNDQGRKLV DVARQCRDQA IAACGPGQPL CVIGNIISNI ANSNGFRVCP
260 270 280 290 300
YFIGHGIGEY FHGHPEIWHH ANDNDLKMEE GMSFTIEPIL MEGTSGFRIL
310 320 330
SDKWTAVSVD DKRSAQFEHT VVITSDGVEI LTKLPEED
Length:338
Mass (Da):37,785
Last modified:July 5, 2005 - v1
Checksum:i4FB31183518AD263
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC095283 mRNA. Translation: AAH95283.1.
RefSeqiNP_001019563.1. NM_001024392.1.
UniGeneiDr.42917.

Genome annotation databases

GeneIDi554090.
KEGGidre:554090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC095283 mRNA. Translation: AAH95283.1.
RefSeqiNP_001019563.1. NM_001024392.1.
UniGeneiDr.42917.

3D structure databases

ProteinModelPortaliQ4VBS4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000010471.

Protein family/group databases

MEROPSiM24.028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi554090.
KEGGidre:554090.

Organism-specific databases

CTDi254042.
ZFINiZDB-GENE-050522-71. metap1d.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
HOVERGENiHBG067178.
InParanoidiQ4VBS4.
KOiK01265.
PhylomeDBiQ4VBS4.

Miscellaneous databases

NextBioi20880657.
PROiQ4VBS4.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.

Entry informationi

Entry nameiMAP12_DANRE
AccessioniPrimary (citable) accession number: Q4VBS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2005
Last modified: June 24, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.