ID A0A6J0MS04_RAPSA Unreviewed; 321 AA. AC A0A6J0MS04; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 13-SEP-2023, entry version 14. 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 Name=LOC108846201 {ECO:0000313|RefSeq:XP_018474929.1}; OS Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus. OX NCBI_TaxID=3726 {ECO:0000313|Proteomes:UP000504610, ECO:0000313|RefSeq:XP_018474929.1}; RN [1] {ECO:0000313|Proteomes:UP000504610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. WK10039 {ECO:0000313|Proteomes:UP000504610}; RX PubMed=22846596; DOI=10.1186/1471-2164-13-352; RA Tanaka Y., Tsuda M., Yasumoto K., Yamagishi H., Terachi T.; RT "A complete mitochondrial genome sequence of Ogura-type male-sterile RT cytoplasm and its comparative analysis with that of normal cytoplasm in RT radish (Raphanus sativus L.)."; RL BMC Genomics 13:352-352(2012). RN [2] {ECO:0000313|RefSeq:XP_018474929.1} RP IDENTIFICATION. RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_018474929.1}; RG RefSeq; RL Submitted (JAN-2023) to UniProtKB. 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_018474929.1; XM_018619427.1. DR AlphaFoldDB; A0A6J0MS04; -. DR GeneID; 108846201; -. DR OrthoDB; 5473250at2759; -. DR Proteomes; UP000504610; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-EC. 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:SF3; METHIONINE AMINOPEPTIDASE 2A; 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|HAMAP-Rule:MF_03175, KW ECO:0000256|RuleBase:RU003653}; KW Protease {ECO:0000256|HAMAP-Rule:MF_03175, ECO:0000256|RuleBase:RU003653}; KW Reference proteome {ECO:0000313|Proteomes:UP000504610}. FT DOMAIN 11..308 FT /note="Peptidase M24" FT /evidence="ECO:0000259|Pfam:PF00557" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175" FT BINDING 94 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 105 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 105 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 174 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 182 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175" FT BINDING 207 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 302 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 302 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 321 AA; 36122 MW; F677FA91730F4285 CRC64; MERLQKPICN SLRQAAEVHR QVRKYMRSIM KPGMLMIDIC ETLEDTVRKL ISENGLRAGI AFPTGCSLNN VAAHWTPNSG DKTVLQYDDV MKLDFGTHID GYIVDSAFTV AFNPIYDPLL AASREATYTG IKEAGVDVRL CDVGAAIQEV MESYEVEING KVYQVKSIRN LNGHSIGRYQ IHAEKSVPNV RGGEQTKMEE GELYAIETFG STGKGYVRDD LECSHYMKNY DVGHVPLRLR RAKQLLATID RNFSTLAFCR RYLDRLGETK YLMALKNLCD SGIIEPCPPV CDVKGSYISQ FEHTILLRPT CKEVISKGDD Y //