ID A0A0S3R6M9_PHAAN Unreviewed; 570 AA.
AC A0A0S3R6M9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
GN Name=Vigan.01G414600 {ECO:0000313|EMBL:BAT76177.1};
GN ORFNames=VIGAN_01414600 {ECO:0000313|EMBL:BAT76177.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT76177.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT76177.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015034; BAT76177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R6M9; -.
DR Proteomes; UP000291084; Chromosome 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 419..426
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 570 AA; 59863 MW; 96A59BECFD7EC395 CRC64;
MAAIATIFVC FTSSSSSPFL TRFASRFHFA AFPLRSPARK LMSQTLARAT LGLTHPSNIE
TPKICFTAKD VDVTEWKGDI LAVGVTEKDL ARDEKSRFEN VILSKIDSKL GGILAEVSSE
EDFSGKVGQS TIIRITGHGS KRVSLIGLGQ SPSTPAPFKG LGEAVVAAAK SYQASSVAVV
LASSEGLSAP SKLSTAYAIA SGAVLGLFED NRYKSEAKKP TLQSVDIIGL GTGPELEKKL
KYAGDVSSGI IFGRELVNSP ANVLTPGVLA EEAANIASTY SDVFTAKILN AEQCAELKMG
SYLGVAAASA NPPHFIHLCY KPPSGPVNVK LALVGKGLTF DSGGYNIKTG PGCSIELMKY
DMGGSAAVLG TAKALGQIKP SGVEVHFIVA ACENMISGTG MRPGDVVTAS NGKTIEVNNT
DAEGRLTLAD ALVYACNQGV EKIIDLATLT GACVVALGPS IAGVFTPSDE LAKEIFEASD
VSGEKLWRLP LEESYWESMK SGVADMVNTG GRQGGAIIAA LFLKQFVDEK VQWMHIDMAG
PVWNDKKRSA TGFGIATLVE WVLKNGLNAH
//
