ID A0A016S582_9BILA Unreviewed; 296 AA.
AC A0A016S582;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN Name=Acey_s0295.g1670 {ECO:0000313|EMBL:EYB85616.1};
GN Synonyms=Acey-map-1 {ECO:0000313|EMBL:EYB85616.1};
GN ORFNames=Y032_0295g1670 {ECO:0000313|EMBL:EYB85616.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB85616.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB85616.1}.
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DR EMBL; JARK01001631; EYB85616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016S582; -.
DR Proteomes; UP000024635; 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; 6.10.140.2220; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 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 PROSITE; PS00680; MAP_1; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU003653};
KW Hydrolase {ECO:0000256|RuleBase:RU003653};
KW Metal-binding {ECO:0000256|RuleBase:RU003653};
KW Protease {ECO:0000256|RuleBase:RU003653};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 9..53
FT /note="MYND-like zinc finger"
FT /evidence="ECO:0000259|Pfam:PF15801"
FT DOMAIN 120..292
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 296 AA; 33384 MW; 6D46E80FB4EB7689 CRC64;
MMEVEERRCE GFECGKPAKL RCPTCIKLGL KDSFFCDQTC FKANWATHKN QHTDPNAPYN
PWPNYNFTGS LRPAKLTPKR TVPQSIARPD YAFHPEGVSF EERQAKKNRE VKVLDDEEKE
GLRVACRLGR EVLNEAAMAC APGVTTDEID RVVHEACIER NCYPSPLGYH NFPKSCCTSV
NEVICHGIPD LRVLENGDLC NVDVTVFHRG FHGDLNETFL VGDKVDEESR KLVRVTYECL
QQAIAIVRPG VKFREIGNVI QKHANANGFS VVKAYCGHGI HRLFHTAPNI PHYASK
//
