ID A0A498JP24_MALDO Unreviewed; 979 AA.
AC A0A498JP24;
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=Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DVH24_008083 {ECO:0000313|EMBL:RXH95583.1};
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:RXH95583.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH95583.1, 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:RXH95583.1};
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:RXH95583.1}.
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DR EMBL; RDQH01000332; RXH95583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498JP24; -.
DR STRING; 3750.A0A498JP24; -.
DR Proteomes; UP000290289; Chromosome 6.
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 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; 2.
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; 2.
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 132..230
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 271..423
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 477..531
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 539..653
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 656..978
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 979 AA; 110647 MW; 169C813C4DAD1429 CRC64;
MARLVLPCKS SAFVRISLLG LISSAPCTSR VRLLGNSAKR LSRYKHFLTL EATCSRNYRI
PYTALPRDKQ GSRRLICSVT TESLPDQVDE SKMAAPKEIF LKDYKMPDYY FDSEEDYNLD
SRHLTLKSLP SGVFTLEILT EMYPQKNTSL EGLYKSSGNF CTQCEAEGFR KITFYQDRPD
IMAKYTCRIE ADKSLYPVLL SNGNLTEQGD LEGNRHYALW EDPFKKPCYL FALVAGQLES
RDDTFITRSG RKVALRIWTP AQDVAKTAHA MYSLKAAMKW DEDVFGLEYD LDLFNIVAVP
DFNMGAMENK SLNIFNSRLV LASPETASDA DYAAILGVIG HEYFHNWTGN RVTCRDWFQL
SLKEGLTVFR DQEFSSDMGS RPVKRISDVS RLRNSQFPQD AGPMAHPVRP HSYIKMDNFY
TVIWVKPLLF VIGICALNFD MFWVSCAITL YLIVILDCHQ HLLAVTSQWH NLTVQLYQGA
EVVRMYKTLL GSQGFRNGMD LYFKRHDGQA VTCEDFYAAM RDANNADFAN FLLWYSQAGT
PIVKVASSYN AEARTFSLKF SQEVPPTPGQ PIKEPMFIPV AVGLLDSTGK EVPLSSVHHD
GIVQSIANNG QPVYTTVLRV TKKEEEFIFS DVSERPIPSL LRGYSAPIRL ETDLTDSDLF
LLLAYDSNEF NRWEAGQVLA RKLMLNLVAD FQQNKPLVLN PKFVLGLRSI LSDLSLDKEF
VAKAITLPGE GEIMDMMEVA DPDAVHAVRS FIRKQLAHEL KAELLSTVEN NTSSEEYVFD
HPNLSRRALK NIALAYLASL EDSKCTELVL NEYKTATNMT EQFAALAALA QNPGKTRDDI
LADFYNKWKK DYLVVNKWFQ LQAMSNIPGN VENVRNLLSH PAFDLRNPNK VYSLIGGFCG
SPVNFHAKDG SGYKFLGEIV MQLDKINPQV ASRMVSAFSR WRRYDETRQN LAKAQLEKIL
AANGLSENVF EIASKSLAA
//
