ID A0A091V4C7_PHORB Unreviewed; 347 AA.
AC A0A091V4C7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
DE Flags: Fragment;
GN ORFNames=N337_09720 {ECO:0000313|EMBL:KFQ84608.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ84608.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ84608.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ84608.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|RuleBase:RU003653};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU003653};
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.
CC {ECO:0000256|RuleBase:RU003653};
CC -!- SIMILARITY: Belongs to the peptidase M24A family.
CC {ECO:0000256|RuleBase:RU003653}.
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DR EMBL; KK413293; KFQ84608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091V4C7; -.
DR Proteomes; UP000053700; Unassembled WGS sequence.
DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 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 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 PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU003653,
KW ECO:0000313|EMBL:KFQ84608.1};
KW Hydrolase {ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:KFQ84608.1};
KW Metal-binding {ECO:0000256|RuleBase:RU003653};
KW Protease {ECO:0000256|RuleBase:RU003653};
KW Reference proteome {ECO:0000313|Proteomes:UP000053700}.
FT DOMAIN 99..327
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ84608.1"
FT NON_TER 347
FT /evidence="ECO:0000313|EMBL:KFQ84608.1"
SQ SEQUENCE 347 AA; 39128 MW; 495832D3D694A686 CRC64;
ECFKGSWATH KLLHKKAKDE KAKREVSSWT LEGDVNTNPW SGYRYTGKLR PHYPLTPTRP
VPSYIQRPDY ADHPLGMSES EQALKGTSQI KILSSEDIEG MRVVCRLARE VLDVAAMMVK
AGVTTEEIDH AVHLACIARN CYPSPLNYYN FPKSCCTSVN EVICHGIPDR RPLQEGDIVN
VDITVYRNGY HGDLNETFYV GEVDEGARRL VQTTYECLMQ AIDAVKPGVR YRELGNIIQK
HAQANGFSVV RSYCGHGIHK LFHTAPNVPH YAKNKAVGVM KPGHVFTIEP MICEGGWQDE
TWPDGWTAVT RDGKRSAQFE HTLLVTDTGC EILTRRLDSI RPHFMSQ
//
