ID A0A0V0W4N6_9BILA Unreviewed; 873 AA.
AC A0A0V0W4N6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
DE Flags: Fragment;
GN Name=Npepps {ECO:0000313|EMBL:KRX70780.1};
GN ORFNames=T06_12973 {ECO:0000313|EMBL:KRX70780.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX70780.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX70780.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX70780.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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:KRX70780.1}.
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DR EMBL; JYDK01000267; KRX70780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0W4N6; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_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:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 15..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 228..442
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 534..851
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 386
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX70780.1"
SQ SEQUENCE 873 AA; 100262 MW; 9F65C348A428399C CRC64;
LENMAAYERL PPSVKPKHYD LWLKIFETNF TAKVSIDIEI FSSVNNITLN SSELVITDAT
LVLQKKTYEK LDVSYDEHFG TAKMALPETI APQLGKLHLT YNGIIKDTLK GLYKCTVEDE
KPSTLLVTQF ESRYARCVLP CWDEPVYKAT FTVALTVPEQ LTAISNMPVE KVTENEPGWK
MFEFQKSPVM STYLLAFVIG KLEFVEKTVG NTVCRVYTVP GKSNQGLFAL DVMISALKFY
ENIFQVPYTL PKLDLVGIPN FEAGAMENWG LVTYRESCLL LKSGVTSARV RQNIALTVAH
EIAHMWFGNL VTIEWWTILF LTEGFATLME NICVDHIFPE FGIWGQFVTD HISYAMAMDA
LRSSHAIEVE ISDPEEIDSI FDAVSYSKAA CVIKMWKDYM GEEQFYKGLQ LYLRKYSYQC
ATMENLIQML ESVSKGKCLM KMAFNWTQTT GFPMVEVSME KVNGTRRLLF SQKRFLADGS
EGKLLFLINK HENNSLWQIP ISISDSGKAI HYYLLKERSG CFEMGEQIND ANQFIKINHN
YSGFYRVKYS DEMLRMLLPA VEAKVLDEAD RFSLCADSFA FVTAGYTTVY QYLNMLDSFK
NETDYNVWME IDRAVIFMDN CLQRTPLYGR FKAAMIPLYE QVFNRLGVVG SSDEAHTTKL
LRPIIIRRMG EYGHQGVVKM AIQEVDDFLR DGVWRNADLR QMFFMLIAQF GGEPGFQKLR
LIYESSSSSE IREQCLMAMG QSPELNLVKQ VLELTLTDKV LLQDMYRVYF GVRRFAKNNA
VAWDFFKDNV QNIVHKCGYT SSCLFIYIID SLFSRQCCMV KAKEMEDFCR GVNLITVGSE
LRFKQALECV EVNAKFLERN LPSVERWLME KGF
//
