ID A0A158Q9F5_ENTVE Unreviewed; 1705 AA.
AC A0A158Q9F5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminopeptidase {ECO:0000313|WBParaSite:EVEC_0000186901-mRNA-1};
GN ORFNames=EVEC_LOCUS1577 {ECO:0000313|EMBL:VDD86434.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000186901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000186901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD86434.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; UXUI01007231; VDD86434.1; -; Genomic_DNA.
DR STRING; 51028.A0A158Q9F5; -.
DR WBParaSite; EVEC_0000186901-mRNA-1; EVEC_0000186901-mRNA-1; EVEC_0000186901.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
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; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 2.
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:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 2.
DR Pfam; PF01433; Peptidase_M1; 2.
DR Pfam; PF17900; Peptidase_M1_N; 2.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 2.
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 ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 1..173
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 208..431
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 449..760
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 798..998
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 1037..1240
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 1330..1677
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 361
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1705 AA; 194820 MW; DB1D676F9D911C6E CRC64;
MTFDGMTTFR FTVKQKINVF TLHTYELSYS DIQLLNDEGT VMQIQNYSLD LNLQHLVITP
TLKPKVGSTY ILQFKYTGRI RPYNEGGLYY TYYDDVFAKR HWMVSTHMEN GVQARAVFPC
IDQPSAKARF HLTLIYPENL IALGNGMETM PQKFRNGWNV ARFRPSLKMS TYLVALAIGP
FVSKSVVNDA GTLVRIWGWT GQDEYLEFAA NISAKCLYQM GLYTNFTYPM SKSDQIGLPE
FRAGAMENWG LVIYKYQYIA FNPNLHTTYV KQAAAKVMCH ELAHQWFGDL VTAFWWSDLF
LNEGFAAFFE IESLKLAIPE QNAFLEGKFL VETEQKGLTA DASASSHPIY FNDVIFDAIT
YNKAPSVLRM TQLVLGKEVF QEGLREYLSA YQFQNTKHEM LFEKLTNAAR KHGVTDWCGK
PINVSEFLNP WILQKCDGKR VFSSSDVPWT MTNVESSSFV RVDYDDIGYD RLLSHLQAEG
TNGFSMADKI VLIGDQIALI TKRKSTGQAF SYKRLLQFLV AILPNYPHFS VFELSDPVLT
ELEKFYMEDI DQKLFQAYIA RYYILFESAK HDILSATYHL SNMFDKFKEL CFDTTTGIEN
CSQGIDPDIH RGMFCAATIY DRSNSSGFLL ELYHQQITYG LYFYQEYYAM LEGVGCTTDN
SVLQILIKEL LSARKNFAYV PSYSYITRNP LGTQAMYDYL ISNTSDVVNS VPIDEYLDAL
TSTWYSNKRL QQLINLNSTL QTVLNSSEAA RVLERQIKTI NSQISFAENH LPEITRFLYD
NYVADKLDTT MLVPKDCKPL SYTLHLKPYF SGPAKYPWYK NMTFEGTVTI RFTVIAPISQ
VVIAANKLII NPEQVKLSCD ALGNVAIAKH EKDYDFGILQ LNLPERLMLP DNTNCTLNMK
YKGFINDRPT KGVSTHSSYF EFNNQKTWIF ATDFLNARGI RSLVPCFDEP YFKAPWQITL
EHPSDMVPLS NAISNGTILG NNGWATTTFA YTQRMSSYAL SLFLGHFDAQ ESVSPEAKVL
SRVWAWSGME IYANRALKVL TSAVDAVSKL LQTRPPISKI DLVALPQCLY TNVTFNGFGV
ISGDYNKILE DPYYATTADH MLISQIIAQA TANQWFGNLV TPETLSYAGL TDGLSMFIAT
KLVAKLEPQQ ANLKSFLEFI MFETSFTFNS NGRFAVLPGD NSALSNEANC KGAAAFAMLE
NIVGEDIVIE ALQALLSDYS YDVVNDVLLW KALEKVVSNR TSTFEESAHM SLTNFMEPYM
WQRSYPIFKV STDGENMTYS MEAYDEETVL FYQPLWVLPV YTADSTGANF WYYGSELQDS
FLNQTFDEKW RIYNVARRAP FRVWYDDQTW SPIYQQLVKD KTVFDEVTRA QLIADTAALR
ERGSLEWPRL LDLGLLLVKD TSFLPLYSFT STLENLMNRF YNTKYYDAVK SYARDVVADA
YDKIAWRNTD DWIQKLETVL DFSTFVQLLE NSIIKKLCLS TLSSSITELA CKAGYEKCLL
DASQRFQNFT ERCAHSLVGT GRCNLVHSDY RGTQYCYGLS SSPSSLEMVL KVYQWFEKES
KYFKRDQENL LYGIGCGKPD SFKRFISDAV HGTMSTKVLT FIGQTVEGAE QLWDYLQKNI
EEVLYGAVQF SFYVSSLTKT WNNDAYVKRI GSFLNSTISS RLPKNAREVL ERSVETILSR
NDWLLKNAGE NSTLVSWLKN HSYYL
//
