ID A0A2V0PEC0_9CHLO Unreviewed; 605 AA.
AC A0A2V0PEC0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Leucine aminopeptidase-like {ECO:0000313|EMBL:GBF97859.1};
GN ORFNames=Rsub_11209 {ECO:0000313|EMBL:GBF97859.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF97859.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF97859.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF97859.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF97859.1}.
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DR EMBL; BDRX01000109; GBF97859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0PEC0; -.
DR STRING; 307507.A0A2V0PEC0; -.
DR InParanoid; A0A2V0PEC0; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:GBF97859.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT DOMAIN 450..457
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 605 AA; 61269 MW; 3207172F1E1A0976 CRC64;
MLAARGVLRA GSLRRLAARQ CALFEARSAS SAIACAIPAP AGLAARPAHA PPRHARPAGA
RRVATMAAAV VVNPVPAPKA VLFEPESLPA VTVAPGDALE WTGDVLVIAV TEDDLEVKDE
QAAISSAALK GLDASLQGVL AELVASGGFE GKAGQSTRAV RVLGAPAAHV ALAGLGKRDK
LAAVAEWGQS PFQTLGASVA ALCKANKLKA AGLAFAAPPP GSAAAGVQRV VAGALQGAYE
SSRFKSKAPK GARLESLALL GLGSAPGLDA AIKHGAAVAV GGQLTRYLVE APPNVCTPSH
LAAAAKHVAG IAPDRFKLQV LEAEECAALG MGCFLGVAEA SHEPAKFIHL TYSPPGKAAK
KVAIVGKGLT FDSGGYNLKA GAGSMIELMK FDMGGAAATL GAARILADTQ PAGVEVHFVI
ASCENMVSAK GLRPGDILTA ASGKTVEVNN TDAEGRLTLA DALWFVQEKA GVEAVVDIAT
LTGACMIALG GEVAGLFTPS DAMASAVGAA AKEAGEKVWR MPMEANYFEQ LKSSCADMKN
TGGRMGGSIT ASLFLKEFVK EGVEWAHLDI AGPVWSEKEQ LPTGYGAATL AEWATLQGAA
APKAQ
//
