ID A0A1S3USH5_VIGRR Unreviewed; 970 AA.
AC A0A1S3USH5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Puromycin-sensitive aminopeptidase isoform X3 {ECO:0000313|RefSeq:XP_014508854.1};
GN Name=LOC106768302 {ECO:0000313|RefSeq:XP_014508854.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014508854.1};
RN [1] {ECO:0000313|RefSeq:XP_014508854.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014508854.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR RefSeq; XP_014508854.1; XM_014653368.2.
DR AlphaFoldDB; A0A1S3USH5; -.
DR GeneID; 106768302; -.
DR OrthoDB; 745at2759; -.
DR Proteomes; UP000087766; Chromosome 7.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|RefSeq:XP_014508854.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..272
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 313..522
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 530..643
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 647..969
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 970 AA; 109517 MW; 3FD57CED51197AD1 CRC64;
MARLVLPSKR LCLSRNTLLG LISPAPNTAK RSIRYKHCVA SEVNFQKKYS PLYTSLTRVK
QGSKRLICAV ATEDLPKQVE ESNMETPKEI FLKDYKMPDY YFDNVDLEFS LGEEKTIVSS
KISVYPRIEG SSPPLVLDGQ DVSLVSVQLN GKALKEEDYH LDARHLTILS PPSGKYDLEI
VTEICPQKNT SLEGLYKSSG NFCTQCEAEG FRKITFYQDR PDIMAKYTVR IEADKSLYPV
LLSNGNLVEH GDLEDGRHYT VWVDPFKKPC YLFALVAGQL ESRDDIFTTR SGRNVVLRIW
TPKEDVPKTA HAMYSLKAAM KWDEDVFGLE YDLDLFNVVA VPDFNMGAME NKSLNIFNSK
LVLASPETAT DADYAAILGV IGHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQEFSSDM
GSRTVKRIAD VSNLRNYQFP QDAGPMAHPV RPHSYIKMDN FYTVTVYEKG AEVVRMYKTL
LGSQGFRKGM DLYFKRHDGH AVTCEDFFSA MVDANGADFA NFSLWYSQAG TPVVKVSTSY
NSEGHTFSLK ISQEIPPTPG QAVKEPMFVP VAVGLLDSTG KDIPLSNLYH NGTLQSVSNN
DQPVFTTVLR VTKKEEEFIF TDIFEKPVPS LLRGYSAPVR LESDLSDSDL FFLLANDSDE
FNRWEAGQVL ARKLMLKLVD DFQHNKPLVL NPNFVDGFKR ILSDPSLDKE FVAKAITLPG
VGEIMDMMEV ADPDAVHAVR TFIRKQLASE LRSEFRTTVL YNRSSEHYVF DHPNMARRAL
KNIALAYLGC LEDQELTELA IEEYKTATNM TEQFAALVAI AQTPGKTRDD FLADFYGKWE
HDFLVVNKWF ALQSSSDIPG NVENVRKLLD HPAFDLRNPN KVYSLIGGFC GSPVNFHAKD
GSGYEFLGEI VLLLDKLNPQ VASRMVSAFS RWKRYDESRQ KLAKAQLEKI VSCNGLSENV
YEIASKSLAV
//
