ID W4IW17_PLAFP Unreviewed; 640 AA.
AC W4IW17;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Methionine aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE Short=MAP 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE Short=MetAP 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_03175};
DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_03175};
GN ORFNames=PFUGPA_03862 {ECO:0000313|EMBL:ETW53989.1};
OS Plasmodium falciparum (isolate Palo Alto / Uganda).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW53989.1, ECO:0000313|Proteomes:UP000019103};
RN [1] {ECO:0000313|EMBL:ETW53989.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW53989.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW53989.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW53989.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) 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). {ECO:0000256|HAMAP-
CC Rule:MF_03175, 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|ARBA:ARBA00000294, ECO:0000256|HAMAP-
CC Rule:MF_03175, ECO:0000256|RuleBase:RU003653};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03175};
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_03175};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase eukaryotic type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03175}.
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DR EMBL; KI927384; ETW53989.1; -; Genomic_DNA.
DR AlphaFoldDB; W4IW17; -.
DR EnsemblProtists; ETW53989; ETW53989; PFUGPA_03862.
DR OMA; WQDYRRS; -.
DR Proteomes; UP000019103; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd01088; MetAP2; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_03175; MetAP_2_euk; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002468; Pept_M24A_MAP2.
DR InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00501; met_pdase_II; 1.
DR PANTHER; PTHR45777; METHIONINE AMINOPEPTIDASE 2; 1.
DR PANTHER; PTHR45777:SF2; METHIONINE AMINOPEPTIDASE 2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS01202; MAP_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_03175}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03175};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03175};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03175};
KW Reference proteome {ECO:0000313|Proteomes:UP000019103}.
FT DOMAIN 329..540
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 412
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 423
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 423
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_03175"
FT BINDING 492
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_03175"
FT BINDING 500
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 526
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_03175"
FT BINDING 621
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 621
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_03175"
SQ SEQUENCE 640 AA; 73113 MW; 590B7FFD4A51E025 CRC64;
MNKNNNKGSV KKNNNSKKKT STNINNVNNL SSIKNIKNEQ NVKNGDVNDE IATTTSSNHV
NMVLNGNDEG IKDVKVVNNL NIDNKREDNN VRINVQGEET LNNDSKNKEA ENKSNIKNNK
SNQSNQSNKK TKNNNNKNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNKNS TSNKKNSKNK
KKVDKLDLIL NEFKNDIKNE KGENNQNDNK LLNGAIETNN NNNNNNNNSG NNRIHFDKEE
IKEIKKKIIL KEHVLEEQDN SSIRLLKNWP QLEKTYQTNP PCIPIDMIYG KDGKYPVGEI
LEYNNYNLSG QSLVEKKERE KLSIDYYEDL RKAAECHRQV RKHMQAFIKP GKKMIDIAQE
TERKTKELIL AEKLKCGWGF PTGCSLNHCA AHYTPNYGDE TVLKYDDVCK LDFGVHVNGY
IIDCAFTIAF NEKYDNLIKA TQDGTNTGIK EAGIDARMCD IGEAIQEAIE SYEIELNQKI
YPIKAISNLR GHSINKYIIH GGKCVPIVRQ KEKNEIMEEG ELFAIETFAS TGKGYVNHEN
ECSHYMRNPE KQFVPIRLNS AKTLLKVIND NFDTLPFCNR WLDDLGQTRH FMALKTLIDL
NIVEPYPPLC DIKNSFTSQM EHTILLRPTC KEVLSRGPDF
//
