ID A0A1X0NMW3_9TRYP Unreviewed; 868 AA.
AC A0A1X0NMW3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=TM35_000301050 {ECO:0000313|EMBL:ORC86065.1};
OS Trypanosoma theileri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC86065.1, ECO:0000313|Proteomes:UP000192257};
RN [1] {ECO:0000313|EMBL:ORC86065.1, ECO:0000313|Proteomes:UP000192257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC86065.1};
RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA Matthews J., Matthews K., Carrington M.;
RT "An alternative strategy for trypanosome survival in the mammalian
RT bloodstream revealed through genome and transcriptome analysis of the
RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL Submitted (MAR-2017) 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:ORC86065.1}.
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DR EMBL; NBCO01000030; ORC86065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0NMW3; -.
DR STRING; 67003.A0A1X0NMW3; -.
DR VEuPathDB; TriTrypDB:TM35_000301050; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000192257; 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:UP000192257};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 13..198
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 243..459
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 533..848
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
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 SITE 400
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 868 AA; 98265 MW; 892CCF3B853642FB CRC64;
MALPRNILPA DPVPHYYTVN ITPDFDTFLF TGHVEIKITA RKPQKSITLN YNELTFVKVS
LKTLDNPSNV EEVPVNAIIL DEGEMKAVFP LKNSFSGEAI LSIDYTGIIN DKLAGFYRSK
YVANRKDSYM GTTQFEAVDA RRAIPCWDEP AVKAVFEMII TAPSNMLVLS NMPHCKKENL
GTQTRWFFEP TPKMSTYLLA WTIAEFDSIQ RTIKKTHKNI NGEVEETLVR VFTPQGKKSQ
ASFALDVACK VLPLYEEFFE SNYILPKVDL LAIPDFAAGA MENWGLITYR EVALLCDESS
SAAHRQYVAI VVAHELAHQW FGNLVTMQWW KELWLNESFA TYMEYWSIDK LFPEWHVFTQ
FVHDEITRAF KLDSLRSSHP VEVEVKNAKE IDDIFDAISY SKGGSIVRMT VNFIGEEAFQ
KGMSAYLKHF AYGNATTEDL WNFLGKAAGK PLTPILEYWT GKQGYPFLTV TLSDNKESLH
VTQNRFLATG DITEDENKTV WKIPLLVTRP ENQILKTIIE EKESTLSIPH SSWVKVNTDQ
SAFCRVLYGS QELLHSLLPA IAGKYISNID RLSIVSDYHA FARAGYCSAV EVLKLLSSYI
NEDDYTVWCS IVDFETDLRM VVSTQGGDVL NAYNAFCRRL YSGAMKKIGF TPKPGDKHSV
TQLRGILFNR LAVAEDEDTI AHAEKLYGER QTTPIPADLY YTVFAVYVKK NGDTALEEVK
MLASTATEAM ERSYYLRALA SSRVNGVVSE LFKFALSDKV RSQDVIYLLG ALASNTEKIK
LYAEELRRVW STLGEKLPGL ILGRALKYLE YGADVTVADE MDSFWNSLDE KAKMGMSRSF
EQGIEGLRNN VAWVTRDAKN VVQFLTSK
//
