ID A0A369SMG1_9METZ Unreviewed; 947 AA.
AC A0A369SMG1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=TrispH2_000850 {ECO:0000313|EMBL:RDD47632.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD47632.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD47632.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD47632.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD47632.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:RDD47632.1}.
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DR EMBL; NOWV01000002; RDD47632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369SMG1; -.
DR STRING; 287889.A0A369SMG1; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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|RuleBase:RU364040,
KW ECO:0000313|EMBL:RDD47632.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {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:UP000253843};
KW Transmembrane {ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 75..263
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 299..517
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 608..924
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 456
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 947 AA; 107032 MW; CE986E459BA9F476 CRC64;
MAQGSGTPEN EDKYFISKSR ALIFLIVVCL LAVVVGLIAG LSANSGSQDN IQTTNAPPVQ
DGKPWMTLRL PTDVVPDHYN LMLFPLVDGS TFTGKVSITI NVTKATRHIL VHIRDLAITD
KSVSTIGGSP RKLSIVQSFF YKPNEFYVIE VGENLEAGKQ YNVTYDFNGN FPKVLFGLYK
STYKTPQGTT RNMVTSDFEP LDARMALPCF DEPTLKATFT TTLVRPTTGY IALSNMPEAR
SYQYQAGYTA VEYQKTVKMS TYLLAFIICD FKYNETTVNN GVKIRIYSPP HLLNNTGFAT
YTTKAQMEYF NTQTALPYDL PKSDLIAIPD FNSGAMENWG LITFRETLLL YDPLKSSIFE
KQRIAVVISH ELVHQWFGNL VTLAWWDDLW LNEGFASYLE YQGVHAVYPD WKIMDQFLSG
DFFRIMARDA LISSRPISAL SDTPAAIKQM FDAITYSKGA VAVRMVEFIL GDTGFKNGYR
AYLKKYQYSN ANTMQLWNSL SEANNNRINM VEVMDPWVRQ KNFPVITITN QGAQGTASQK
RFLIDDSAAT GTGSDFSTYG VMLSLRWFSG SYKWYVPLNY ITSADTNTPI SAWLNKTSVN
FNYPVNGWMK ANVGQYGFYI VNYPETNWNR LQAALESDVN TLKSGDRAGL INDAFMLARS
GTIKQSLALG MTKYLSKEKE YVPWTTALGS LGYFDTILSM RPSYGDFKTY MINLIRGRYN
DLGWTDSGSH LDRYARSDIL LWVTRLNYNT AIQAAKKIYN NWMVNGTSIH PNIRTRVLRA
GIAAGGLKEW DFAWNKFLTT ESASEKTALM YALAFSRTPW ILNRYLQRSM NTSLVRSQDT
LSVIRYVSGT TLGRPIAWSF FQANWNTLYD RYSQVTFGLA RAAESLTSAF ATDYQLQEVQ
NFFNTAKDTN AISSSKKTIL ENIKSNIDWL KKNEADVADW LAKNKNI
//
