ID A0A3F3Q515_9EURO Unreviewed; 854 AA.
AC A0A3F3Q515;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=BDQ94DRAFT_159074 {ECO:0000313|EMBL:RDH34185.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH34185.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH34185.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH34185.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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). {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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000256|ARBA:ARBA00006146}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase eukaryotic type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03175}.
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DR EMBL; KZ852044; RDH34185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q515; -.
DR STRING; 1341132.A0A3F3Q515; -.
DR OrthoDB; 5485164at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0042284; F:sphingolipid delta-4 desaturase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
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; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
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; IPR013866; Sphingolipid_d4-desaturase_N.
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:SF2; METHIONINE AMINOPEPTIDASE 2; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF08557; Lipid_DES; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SMART; SM01269; Lipid_DES; 1.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03175};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03175};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03175};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03175};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 475..513
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 219
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 230
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 230
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 299
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 307
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT BINDING 332
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 427
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 427
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
SQ SEQUENCE 854 AA; 94109 MW; F7621C43D546DF07 CRC64;
MAAQASEKLQ KLDLNGQSGD AKADAPAAGQ AQAGEAEDDS DDDEVEDGNA AGEGAASGAA
KKKKKRKSKK KKKGGAKVQS SPPRVPLSTL FAGKEYPEGE IVEYQNENSY RTTNEEKRYL
DRMKNDFLQE YRQAAEVHRQ VRQYAQKTIK PGQTLTEIAE GIEESVRALT GHQGLEEGDN
LKGGMGFPCG LSINHCAAHY TPNAGNKMVL QQGDVMKVDF GAHINGRIVD SAFTVAFDPV
YDPLLAAVKD ATNTGIREAG IDVRMSDIGA AIQEAMESYE VEINGTMYPV KCIRNLNGHN
IDQHIIHGGK SVPIVKGGDQ TKMEEGEVFA IETFGSTGKG YVREDMETSH YALIPDHSQV
PLRLSSAKNL LNVINKNFGT LPFCRRYLDR LGQDKYLLGL NNLVSSGIVQ DYPPLCDIKG
SYTAQYEHRT GIGPSVDPGS PTWKASAPKL TFQAPQTTSD KTEPSTRIDP PEASAVDDHF
FWTYTEEPHR SRRQAIIKAH PEVTKLCGPE PLTKYVVLGV VSLQILCAYL LRNTSMFDWK
FLATAYVIGA TSNQNLFLAI HEISHNLAFR SAMANRLLAI FANIPIGLPY SAAFRPYHLT
HHKSLGVAGL DTDLPTAVEA FLLDSLLGKA FFCTFQIFFY AVRPMFIYSP PFTSIHVLNL
ITQLTFDYAL TKFCGGSLQP LLYLLLSSFL AGSLHPCAGH FIAEHYFFSR VDHGTESIQE
QKNNQKKSHP LDSLPPPETY SYYGPLNFFT YNVGLHNEHH DFPAIPWTRL HELHRIASEF
YEPLPCHHSW VWVIWTFILD KNVGMWCRVK RAQGGRLVGG GGGGSGRAGE SISASSAGPE
GESGDGWKES EIQN
//
