ID A0A022R419_ERYGU Unreviewed; 578 AA.
AC A0A022R419;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
GN ORFNames=MIMGU_mgv1a003554mg {ECO:0000313|EMBL:EYU34348.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU34348.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU34348.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC {ECO:0000256|ARBA:ARBA00011867}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; KI630707; EYU34348.1; -; Genomic_DNA.
DR RefSeq; XP_012841116.1; XM_012985662.1.
DR AlphaFoldDB; A0A022R419; -.
DR STRING; 4155.A0A022R419; -.
DR MEROPS; M17.A03; -.
DR GeneID; 105961431; -.
DR KEGG; egt:105961431; -.
DR eggNOG; KOG2597; Eukaryota.
DR OMA; MPLWKYF; -.
DR OrthoDB; 2899215at2759; -.
DR PhylomeDB; A0A022R419; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT DOMAIN 430..437
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 578 AA; 60538 MW; DFC485C998DF6D4E CRC64;
MAAIRVAFNS LNLLAPTSSS CACHSVLTKL QFRPIWGVSL TFAPLSSRTS NRMAHSIARA
TLGLTQANKI DAQKISFTAK EIDLVQWKGD ILAVGVTEKD MVKDENSKFK NSILQKLDLQ
LGGLLSEASS EEDFTGKSGQ STVLRFPGIG SKRVGLIGLG STSSPTLTYR SLGEAVAAVA
KSARASNVAI ALASSEGISA ESKLSTASAI ATGTVLGTFD DTRFKSESKQ SALKSVDIIG
LGSGPQIEKK LKYAADVCSG IIFGKQLVNA PANVLTPGVL AAEASRIASE HSDVLSAKIL
DVEQCKELKM GSYLAVAEAS ANPAHFIHLC YKPSNGEIKK KIALVGKGLT FDSGGYNIKT
GAGCSIELMK FDMGGSAAVL GAAKALGQIK PSGVEVHFIV AACENMISGT GMRPGDVVTA
SNGKTIEVNN TDAEGRLTLA DALVYACNQG VEKIVDLATL TGACVVALGP SIAGVFTPSD
DLAKEVIGAS EISGEKLWRM PMEDSYWDSM KSGVADMVNT GGRQGGAITA ALFLKQFVDE
KVQWMHIDMA GPVWNDKKKN ATGFGISTLV EWVLKNSS
//
