ID B3RHX4_TRIAD Unreviewed; 893 AA.
AC B3RHX4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=TRIADDRAFT_20166 {ECO:0000313|EMBL:EDV29668.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV29668.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV29668.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29668.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS985241; EDV29668.1; -; Genomic_DNA.
DR RefSeq; XP_002108870.1; XM_002108834.1.
DR AlphaFoldDB; B3RHX4; -.
DR STRING; 10228.B3RHX4; -.
DR MEROPS; M01.010; -.
DR EnsemblMetazoa; TriadT20166; TriadP20166; TriadG20166.
DR GeneID; 6749352; -.
DR KEGG; tad:TRIADDRAFT_20166; -.
DR CTD; 6749352; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_2_0_1; -.
DR InParanoid; B3RHX4; -.
DR OrthoDB; 3085317at2759; -.
DR PhylomeDB; B3RHX4; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 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:UP000009022};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 40..230
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 270..484
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 569..873
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 423
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 893 AA; 101848 MW; 73FB363E5D278208 CRC64;
MTQSSGSTTT RTVATVKPTA PKPTSRYPAV NNIRLPKNIV PIQYWFSLDV DMIGLQFTGQ
NDIEISVTSQ TNIIIVHMKQ MTLVGSPVVS STRNFGNPLT ISEHNAFALN DYYYIVLASP
LNPGIYYVRF NFRAALSTAL NGLYKSTYTK LDGRVINIAA SQCQPTDARK IIPLFDEPEL
KANFTATIIT QSNYTSVLWN MPIQRNVTIP NRPGFRRYDY NTSVRMSSYL LAFVLADFTY
IEMMTKNRVP IRVWATTDTI NQGNFALIGG VNITDYFEDF FGIPFPLPKQ DMVAVPDFAA
GAMENWGLIL YRETALLYDP NVSAANNQQR VAYVVAHELA HMWFGNLVTM KWWDDLWLNE
GFASFMEYLG TDHYQPTWEM LDQFVPIDVQ RAFSLDAFVT SHPVQVTVYH PDEINEVFDT
ISYAKGASII RMMRDMMGNL DFKNGISRYL KKFEYRNAVT RDLWQTLSEA ISYRINVTDV
MDTWTLQMGF PVVTITNTGS QARLSQKRFL LDPNNKNPEV DPATSKFRSP YGYKWNIPLK
YILGNSPNTI RSAMVNMSSS KLPWPAGTWL KANKDAYGYY RVNYPVSNWN LLIQEMQKTQ
PALSKRDFSN LLDDAFNLAS LQVLDIAFGT TKYLTKERSY VPWRTANSVL GAIGSIISYR
SSYGYFSVSV NDRYPSNLIR LLRMSALTIG CGFGYKPCLD NATLLFRRFM ADPTNNAVKP
NLKAVVYRFG IANGGIAEWD FLYNYFYKTN VASEKRTILD ALSYSKEPWI LNRYLRWSID
PAKVRSQDST VVIGYIANNL VGRPLAWDFV RANWAYIRKT YGGSFFSFGS LIRNTAGRFA
SQFRLKQANF FRQNPDVGTG ANAVKQSVES IKNRISWINS YERVAEDWLK RNV
//
