ID A0A1Y2ET11_9BASI Unreviewed; 837 AA.
AC A0A1Y2ET11;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=BCR35DRAFT_281272 {ECO:0000313|EMBL:ORY74296.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY74296.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY74296.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY74296.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY74296.1}.
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DR EMBL; MCGR01000042; ORY74296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2ET11; -.
DR STRING; 106004.A0A1Y2ET11; -.
DR InParanoid; A0A1Y2ET11; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000193467; 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; 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 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|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3,
KW ECO:0000256|RuleBase:RU364040};
KW Metalloprotease {ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW Zinc {ECO:0000256|PIRSR:PIRSR634016-3, ECO:0000256|RuleBase:RU364040}.
FT DOMAIN 3..104
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 200..419
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 492..811
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 360
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 837 AA; 91729 MW; C3A6677F531F1D0D CRC64;
MKELTTLSFE KELAAGDAVL GFRWEGSLDA GSMLGYYRIP GPPSEEEGTE PEYYAVTQMQ
PTMARRAFPC FDHPAKKAVF AVSLISPKGL VSLSNTPEVS RSASKGNFPS SDLLSTAFLA
EDEGKLADAS SSAGADGVEW ELVTFEPTPI MTSYLVAWAV GRFSSISSSY VSPLTQRTVP
LNVYAASSFE HIERGQGQLA LDTLAKVMPV YEKLFDIPYE LGKLDILVCD AFDAGGMENW
GLITGKTMNL LHDAERSGMQ GERMVVSTVS HEAAHMWFGN LVSMAWWDDL WLNEGFATLM
GEVIALHEIE PSWNVHASFL KYHRTSALEL DALRSSHPVQ MVCEDDSEDA VTQSFDAISY
EKGSAVLKML SQVIGEEAFI RGTSTYLKAH AHSCSTSGDL WRAMSEASGI DVAALMDSWI
SKIGFPVVSV EETAEGLKLR QNRFLSTGDP KPEEDETIWT IPLDLKLVGS DAPVEKILMS
TRELVLPLPQ GLYKLNSETS GTFRVSYPPA HLSKLAEEAS KPRSGLSLAD RLGLVQDVIL
LSEAGYTPTS SALDLMKQMV SEPEHLVWVE IAQAFQRLVD AWWEQPEEII DGVRAFARSL
FGPLVEKVGF SHQPEEDAEA RQFRVLAIAA AAAAEEPSFL AWIQQAFGLL ASGHTDETLA
DLAPIIVTTT VKHGGAMEYN IALAIYNNPP TPQHQLAAIG GLTSTRDSAL IQQAAGMLMG
GQVAEQNMTM FLHGLAANPL SRRLVWQFVA GAWPMLEMQF QGSFHLGKIA QFSFQSLSTE
EDAAQVEAFF ADKETSQFIQ PLQQGLDTVR AKARWLNRAA EDVKQWLEKN EFLSSDA
//
