ID C4WUS7_ACYPI Unreviewed; 378 AA.
AC C4WUS7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN Name=ACYPI008785 {ECO:0000313|EMBL:BAH71647.1};
GN Synonyms=100168049 {ECO:0000313|EnsemblMetazoa:NP_001155775.1};
OS Acyrthosiphon pisum (Pea aphid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH71647.1};
RN [1] {ECO:0000313|EMBL:BAH71647.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LSR1 {ECO:0000313|EMBL:BAH71647.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:BAH71647.1};
RA Shigenobu S., Nakabachi A., Richards S.;
RT "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA Weinstock G., Gibbs R.A.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001155775.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
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; AK341197; BAH71647.1; -; mRNA.
DR RefSeq; NP_001155775.1; NM_001162303.2.
DR AlphaFoldDB; C4WUS7; -.
DR STRING; 7029.C4WUS7; -.
DR MEROPS; M24.017; -.
DR EnsemblMetazoa; NM_001162303.2; NP_001155775.1; LOC100168049.
DR GeneID; 100168049; -.
DR KEGG; api:100168049; -.
DR eggNOG; KOG2738; Eukaryota.
DR HOGENOM; CLU_015857_2_1_1; -.
DR InParanoid; C4WUS7; -.
DR OMA; FYGDHAY; -.
DR OrthoDB; 5475502at2759; -.
DR Proteomes; UP000007819; Unassembled WGS sequence.
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; 6.10.140.2220; -; 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 2: Evidence at transcript level;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174,
KW ECO:0000256|RuleBase:RU003653};
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:UP000007819};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 10..54
FT /note="MYND-like zinc finger"
FT /evidence="ECO:0000259|Pfam:PF15801"
FT DOMAIN 127..355
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT REGION 83..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 210
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 221
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 221
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 284
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 291
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 317
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 348
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 348
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 378 AA; 41961 MW; 392F3EB6232E746F CRC64;
MSASLANRTC ETAGCGSKAN LQCPTCIKLD IPGSYFCSQE CFKGNWSTHK ALHKAGQNSN
GIIEPFNPWP DYVFTGPLRP HRTSPARTVP GHIQKPDYAE HPDGTPLSEQ SVKLSSHIKV
LNDEEQEQMR IACKLGREVL DEVALMIDVG ITTDEIDRVV HEACIEKECY PSPLNYYKYP
KSCCTSINEV ICHGIPDMRA LINGDICNVD VTVCHRGYHG DLNETFFIGN VSKAAEKLVN
VTWECLEKAI KAVTPGEKYR ELGNIIHKHA QSNGFSVVRS YCGHGIHQLF HTSPGVPHYA
KNKAVGVMKP GHTFTIEPMI SQGSWRDKCW PDNWTAVTVD GLLSAQFEQT LLVTDTGVDI
LTKRLGNNGK PYFMDKKS
//
