ID A0A498I253_MALDO Unreviewed; 971 AA.
AC A0A498I253;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Puromycin-sensitive aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DVH24_019917 {ECO:0000313|EMBL:RXH77029.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH77029.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH77029.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH77029.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RXH77029.1}.
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DR EMBL; RDQH01000340; RXH77029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498I253; -.
DR STRING; 3750.A0A498I253; -.
DR Proteomes; UP000290289; Chromosome 14.
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 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:UP000290289};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..285
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 326..523
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 531..645
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 648..970
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 971 AA; 109259 MW; 992C0B3281FE37A9 CRC64;
MARLVLPCKS SALVRTSILG LISSTPLQCT SRVRLLGNSA KRLTRYRRFL TSEVACSRNY
RIPYTALPRD KQGSRRLICS VATESLPDQV DESKMAAPKE IFLKDYKMPD YYFDSVDLNF
SLGEEKTIVS SKISVFPRVE GSSSPLVLDG TDLKLLSNIS IDSSLFLNEE DYNLDSCHLT
LKSLPSGAFT LEILTEMYPQ KNTSLEGLYK SSGNFCTQCE AEGFRKITFY QDRPDIMAKY
RCCIEADKSL YPVLLSNGNL TEQGDLEGNR HYALWEDPFK KPCYLFALVA GQLESRDDTF
TTRSGRKVAL RIWTPAQDVP KTAHAMYSLK AAMKWDEDVF GLEYDLDLFN IVAVPDFNMG
AMENKSLNIF NSRLVLASPE TASDADYAAI LGVIGHEYFH NWTGNRVTCR DWFQLSLKEG
LTVFRDQEFS SDMGSRPVKR ISDVSKLRNY QFPQDAGPMA HPVRPHSYIK GAEVVRMYKT
LLGSQGFRNG MDLYFKRHDG QAVTCEDFYA AMRDANNADF ANFLLWYSQA GTPIVKVASS
YNAEARTFSL KFSQEVPPTP GQPIKEPMFI PMAVGLLDST GKELPLSSVH HDGTVQSIAN
NGQPVYTTVL RVTKKEEEFV FSDVSERPIP SLLRGYSAPI RLETDLTDSD LFLLLAYDSD
EFNRWEAGQV LARKLMLDLV ANFQQNKPLV LNPKFVIGLR RILSDLSLDK EFVAKAITLP
GEGEIMDMME VADPDAVHAV RTFIRKQLAH ELKAELLNTV ENNRSSEEYV FDHPNLSRRA
LKNIALAYLA SLEDSKCTEL VLNEYKTATN MTEQFAALAA IAQNPGKTRD DILADFYSKW
QEDYLVVNKW FALQAMSDVP GNVENVRNLL SHPAFDLRNP NKVYSLIGGF CGSPVNFHAK
DGSGYKFLGE IVMQLDKINP QVASRMVSAF SRWRRYDETR QNLAKAQLEK ILSTNGLSEN
VFEIASKSLA A
//
