(data stored in ACNUC8465 zone)

SWISSPROT: C1E1Q7_MICCC

ID   C1E1Q7_MICCC            Unreviewed;       311 AA.
AC   C1E1Q7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE            EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN   ORFNames=MICPUN_97151 {ECO:0000313|EMBL:ACO61782.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61782.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61782.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins.
CC       The N-terminal methionine is often cleaved when the second residue
CC       in the primary sequence is small and uncharged (Met-Ala-, Cys,
CC       Gly, Pro, Ser, Thr, or Val). {ECO:0000256|RuleBase:RU003653}.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC       {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653}.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-
CC       affinity and a low affinity metal-binding site. The true nature of
CC       the physiological cofactor is under debate. The enzyme is active
CC       with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC       methionine aminopeptidases function as mononuclear Fe(2+)-
CC       metalloproteases under physiological conditions, and the
CC       catalytically relevant metal-binding site has been assigned to the
CC       histidine-containing high-affinity site. {ECO:0000256|HAMAP-
CC       Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03174}.
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DR   EMBL; CP001324; ACO61782.1; -; Genomic_DNA.
DR   RefSeq; XP_002500524.1; XM_002500478.1.
DR   ProteinModelPortal; C1E1Q7; -.
DR   MEROPS; M24.001; -.
DR   GeneID; 8241715; -.
DR   KEGG; mis:MICPUN_97151; -.
DR   HOGENOM; HOG000030427; -.
DR   InParanoid; C1E1Q7; -.
DR   KO; K01265; -.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP.
DR   CDD; cd01086; MetAP1; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E1Q7.
DR   SWISS-2DPAGE; C1E1Q7.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174,
KW   ECO:0000256|RuleBase:RU003653};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
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,
KW   ECO:0000256|RuleBase:RU003653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN       60    294       Peptidase_M24. {ECO:0000259|Pfam:
FT                                PF00557}.
FT   METAL       143    143       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_03174}.
FT   METAL       154    154       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_03174}.
FT   METAL       154    154       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03174}.
FT   METAL       223    223       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03174}.
FT   METAL       256    256       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03174}.
FT   METAL       287    287       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_03174}.
FT   METAL       287    287       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03174}.
FT   BINDING     126    126       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03174}.
FT   BINDING     230    230       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03174}.
SQ   SEQUENCE   311 AA;  33965 MW;  388ECC42D0F45F1F CRC64;
     MPEFKWTGPL RPMKVSPKRS VPKIGWLCPL PDYARTGWPE AEFASSLQHK LEVKTPEQLA
     KMRAACSLGR AVMDAVAAAI KPGVTTDQLD RICHAMTLMN GAYPSPRNYM GFPKSLCTSV
     NEVVCHGIPD ARPLEDGDIV NLDITVCLDG YHGDLNETYF VGTGSSDPER AERAKALMKC
     ALECLELAMA RCTPGARFRD LGEAIQTHAN GRGYGVVKDF CGHGIGALFH CAPNVPHYAK
     NKAVGVMKPG MTFTIEPMVN EGTHRTKHWP DGWTAVTADG GRSAQYEHTM AVTETGLDVL
     TKRTANSRPF Y
//

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