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Database: UniProt
Entry: A0A0E1RWP9_COCIM
LinkDB: A0A0E1RWP9_COCIM
Original site: A0A0E1RWP9_COCIM 
ID   A0A0E1RWP9_COCIM        Unreviewed;       375 AA.
AC   A0A0E1RWP9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE            EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN   ORFNames=CIMG_08020 {ECO:0000313|EMBL:EAS29274.1};
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS29274.1, ECO:0000313|Proteomes:UP000001261};
RN   [1] {ECO:0000313|Proteomes:UP000001261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2] {ECO:0000313|Proteomes:UP000001261}
RP   GENOME REANNOTATION.
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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|HAMAP-Rule:MF_03174,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
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_03174};
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03174}.
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DR   EMBL; GG704913; EAS29274.1; -; Genomic_DNA.
DR   RefSeq; XP_001240857.1; XM_001240856.2.
DR   AlphaFoldDB; A0A0E1RWP9; -.
DR   STRING; 246410.A0A0E1RWP9; -.
DR   MEROPS; M24.017; -.
DR   GeneID; 4559383; -.
DR   KEGG; cim:CIMG_08020; -.
DR   VEuPathDB; FungiDB:CIMG_08020; -.
DR   InParanoid; A0A0E1RWP9; -.
DR   OMA; YGDHAYT; -.
DR   OrthoDB; 5475502at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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   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|HAMAP-Rule:MF_03174,
KW   ECO:0000256|RuleBase:RU003653}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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, ECO:0000256|RuleBase:RU003653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001261};
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          119..349
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   BINDING         201
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   BINDING         212
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   BINDING         212
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_03174"
FT   BINDING         278
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_03174"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   BINDING         311
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_03174"
FT   BINDING         342
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_03174"
FT   BINDING         342
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
SQ   SEQUENCE   375 AA;  41747 MW;  672312AFC8900BB6 CRC64;
     MGEVDAKNCI GLDCRNPAGS LRCPTCLKIG IESYFCSQDC FKRSWAEHKA IHKSKSTYDP
     FPTYPYTGKL RPVYPLSPQN KVPPNVVQPD YAIDGIPRSE QKLFGRNNIR ILTEKEQDGM
     RKVCRMGREV LDIAAREIKV GVTTDHIDKV VYQACMERKA YPSPLNYMNF PKSVCTSVNE
     VICHGIPDQR PLEDGDIINI DISIYHGGFH ADLNETYYVG DKSLADPDTV RVVETARECL
     DKAIEIVKPG MLFREPGNVI EKHAKSRDCS VVRTYCGHGV NQLFHTAPSI PHYAKSKTVG
     SAKPGMCFTI EPMINLGSYR DKTWPDNWTS VTIDGKKSAQ FEHTLLVTET GVEILTARQS
     DSPGGPVSMP SISGD
//
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