ID A0A1Z5TC00_HORWE Unreviewed; 976 AA.
AC A0A1Z5TC00;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=BTJ68_05219 {ECO:0000313|EMBL:OTA33585.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA33585.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA33585.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA33585.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-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:OTA33585.1}.
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; MUNK01000073; OTA33585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TC00; -.
DR STRING; 1157616.A0A1Z5TC00; -.
DR VEuPathDB; FungiDB:BTJ68_05219; -.
DR InParanoid; A0A1Z5TC00; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000194280; 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:SF171; 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:UP000194280};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 108..306
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 347..563
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 637..951
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 504
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 976 AA; 109939 MW; BBF1CCD514D37E4F CRC64;
MAASFGRWHR LLPLAGPCRG VQASKLHEQT PRFVSFPLIQ PKARAQRFSS ISLLYTERPK
SRARPDPRQP RLSAARTCID RRHCSSSASS TLVKMASDRD ILPADVKPTN YAISLHDLQS
GEPWTYQGTV NIDLQVKKST KTVTLNTHEL KVHSVEVFTE AGKTASSVKA ADISYDAKNQ
RCTFSFDQAL PQSQKAVISI AFEGTMNNVM AGFYRSKYTP TTTPAKGVAK DSEHHYMFST
QFESSDARRA FPCFDEPNLK ASFDFEIEIP EDLTALSNMP EKETKKGKAG TKVVSFERTP
IQSTYLLAWA FGDFEYVEDF TRRKYNGKNL PVRVWTTRGL KEQGKLALES AHQIVDYFSE
IFRIDYPLPK VDLLAVHEFS HGAMENWGLI TYRTTAVLFD PESSDQKYRN RVVYVVAHEL
AHQWFGNLVT MDWWNELWLN EGFATWVGWY AVDHLHPDWN VWGQFVTEGM QMAFNLDSLR
TSHPIEVPVR NALEVDQIFD HISYLKGSSV IRMLASYLGV ETFLKGVSDY LKAHMYSNAK
TNDLWDALSK ASGQDVTTFM DPWIRKIGFP VVTIAEEPGQ ISVKQNRFIS AGDVKPEEDQ
TTWWIPLNLK TGQTMSDAKR EALTEKSDTY RDIDTTFYKP NADQTGFYRT NLPPEHLIQL
SKALDKLSVQ DKIGLVGDAA AMAVAGEGTT AGLLSFVEGF ATETNYLVWS EVLSSLGKIR
RIFSSDEKVA AGLREFTLKL VSPATDKIGW EFAPSDDYLT GQLRSLLIST AGLMGHEKVV
AEAQKRFKAF MNGDKKAIHP SLRGPVFRIA VKNGGADAYK AVQNEFLTTT SIDGREIALQ
SMGQVQSQEL AKEYLQFGFS GKVATQDLHT VGASLAMNSK VRENVWQFVK SEWPMIRERL
GANMVVLERF LRMCLDKFAD AEVEKDVQAF FSDKDNTGYD RGLAVAMDTI KSNARYRERD
AELVKEWLSA HGYLKA
//
