ID E3M5M9_CAERE Unreviewed; 371 AA.
AC E3M5M9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN Name=Cre-map-1 {ECO:0000313|EMBL:EFO92356.1};
GN ORFNames=CRE_10941 {ECO:0000313|EMBL:EFO92356.1}, GCK72_015023
GN {ECO:0000313|EMBL:KAF1758564.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFO92356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFO92356.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF1758564.1, ECO:0000313|Proteomes:UP000483820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX506 {ECO:0000313|EMBL:KAF1758564.1,
RC ECO:0000313|Proteomes:UP000483820};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KAF1758564.1};
RA Teterina A.A., Willis J.H., Phillips P.C.;
RT "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when the
CC second residue in the primary sequence is small and uncharged (Met-
CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
CC {ECO:0000256|RuleBase:RU003653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
CC ECO:0000256|RuleBase:RU003653};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000256|HAMAP-Rule:MF_03174};
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03174}.
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DR EMBL; DS268425; EFO92356.1; -; Genomic_DNA.
DR EMBL; WUAV01000004; KAF1758564.1; -; Genomic_DNA.
DR RefSeq; XP_003108664.1; XM_003108616.1.
DR AlphaFoldDB; E3M5M9; -.
DR STRING; 31234.E3M5M9; -.
DR MEROPS; M24.017; -.
DR EnsemblMetazoa; CRE10941.1; CRE10941.1; WBGene00074144.
DR GeneID; 9799446; -.
DR KEGG; crq:GCK72_015023; -.
DR CTD; 9799446; -.
DR eggNOG; KOG2738; Eukaryota.
DR HOGENOM; CLU_015857_2_1_1; -.
DR InParanoid; E3M5M9; -.
DR OMA; FYGDHAY; -.
DR OrthoDB; 5475502at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000483820; Chromosome iv.
DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR HAMAP; MF_01974; MetAP_1; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR InterPro; IPR031615; Zfn-C6H2.
DR NCBIfam; TIGR00500; met_pdase_I; 1.
DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43330:SF7; METHIONINE AMINOPEPTIDASE 1; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF15801; zf-C6H2; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174,
KW ECO:0000256|RuleBase:RU003653};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03174};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03174,
KW ECO:0000256|RuleBase:RU003653};
KW Protease {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 10..51
FT /note="MYND-like zinc finger"
FT /evidence="ECO:0000259|Pfam:PF15801"
FT DOMAIN 119..347
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 309
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
SQ SEQUENCE 371 AA; 41808 MW; 02052E965FDB504D CRC64;
MESLEGKKCI GCQKPAKLRC PTCIKMSLPD AYFCDQTCFK AFWPIHKISH TDVSGAYNPW
PCYSFTGALR PARVTDRRTV PDHIPRPDYA LHPQGVSLEE RQSKSERIIK VLTDEEKEGL
KVACKLGREC LNEAGRACEP GVTTDELDRV VHEAAIERDC YPSPLGYYKF PKSCCTSVNE
VICHGIPDMR VLENGDLCNV DVTVYHRGFH GDLNETFLVG DKVDEESRKL VQTTWECLQQ
AIAIVKPGVK FREIGNVIQK HANANGFSVV KGYCGHGIHR LFHTAPNVPH YAKNNATGVM
KAGNSFTIEP MINAGTFHDD KWPDDWTAVT RDGRRSAQFE QTLLVTDTGC EILTKRDQNR
PWFMDQIAQK Y
//
