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Q7ZWV9

- MAP1_XENLA

UniProt

Q7ZWV9 - MAP1_XENLA

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Protein

Methionine aminopeptidase 1

Gene

metap1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Cotranslationally 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).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 Fe(2+)-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 sitei203 – 2031SubstrateUniRule annotation
Metal bindingi220 – 2201Divalent metal cation 1UniRule annotation
Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
Metal bindingi231 – 2311Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei301 – 3011SubstrateUniRule annotation
Metal bindingi327 – 3271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi358 – 3581Divalent metal cation 1UniRule annotation
Metal bindingi358 – 3581Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1UniRule annotation
Short name:
MetAP 1UniRule annotation
Alternative name(s):
Peptidase M 1UniRule annotation
Gene namesi
Name:metap1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254194. metap1.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosolic ribosome Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Methionine aminopeptidase 1PRO_0000323738Add
BLAST

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ7ZWV9.
SMRiQ7ZWV9. Positions 81-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 5244Zinc finger-like; important for proper ribosome associationUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG067178.

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.

Q7ZWV9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVESRVCE TEGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL
60 70 80 90 100
LHKKAKDDKI KPEVSPWTMD GEVNTDPWPG YRYTGKLRPH YPLTPMRPVP
110 120 130 140 150
SYIQRPDYAD HPLGMSESEQ TLKGTSQIKT LSPEDIEGMR VVCRLAREVL
160 170 180 190 200
GVAAMMVKSG ITTEEIDHAV HLACISRNCY PSPLNYYNFP KSCCTSVNEV
210 220 230 240 250
ICHGIPDRRP LQDGDIVNVD ITVYRDGYHG DLNETFYVGD VDEGAKRLVE
260 270 280 290 300
TTYECLMQAI DEVKPGVRYR ELGNIIQKHA QANGFSIVRS YCGHGIHKLF
310 320 330 340 350
HTAPNVPHYG KNKAVGVMKP GHVFTIEPMI CEGGWQDETW PDGWTAITRD
360 370 380
GKRSAQFEHT LLVTETGCEI LTCRLEENGR PYFIS
Length:385
Mass (Da):43,196
Last modified:March 18, 2008 - v2
Checksum:iE3CCA9B269376EEF
GO

Sequence cautioni

The sequence AAH46685.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC046685 mRNA. Translation: AAH46685.1. Different initiation.
BC070567 mRNA. Translation: AAH70567.1.
UniGeneiXl.76058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC046685 mRNA. Translation: AAH46685.1 . Different initiation.
BC070567 mRNA. Translation: AAH70567.1 .
UniGenei Xl.76058.

3D structure databases

ProteinModelPortali Q7ZWV9.
SMRi Q7ZWV9. Positions 81-385.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M24.017.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Xenbasei XB-GENE-6254194. metap1.

Phylogenomic databases

HOVERGENi HBG067178.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiMAP1_XENLA
AccessioniPrimary (citable) accession number: Q7ZWV9
Secondary accession number(s): Q6NRY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 26, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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