ID A0A1Z5TIK5_HORWE Unreviewed; 883 AA.
AC A0A1Z5TIK5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-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=BTJ68_06604 {ECO:0000313|EMBL:OTA35751.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA35751.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA35751.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA35751.1,
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:OTA35751.1}.
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DR EMBL; MUNK01000040; OTA35751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TIK5; -.
DR STRING; 1157616.A0A1Z5TIK5; -.
DR VEuPathDB; FungiDB:BTJ68_06604; -.
DR InParanoid; A0A1Z5TIK5; -.
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; 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:UP000194280};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 28..217
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 252..469
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 543..860
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 410
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 883 AA; 99267 MW; D26B7A13A67105F0 CRC64;
MCRHDAETAD ANMDISKGRE VLPKNVRPVH YDLTLEPNFE TFKYEGTVVV DLDVTEDTKS
ISLNTYEIDV QETKVTAAGT LISSSPRLSY NEDSQTTTAE FDQTIPAGQK AQLTMKFTGT
LNDNMAGFYR SSYKDASGND KWMATTQMEP TDARRAFPCW DEPALKASYT VTLIADHDQT
CLSNMDVASE KDVDSTMAGK KRKAVTFNKT PLMSTYLLAF IVGELKVYES KSFRLPVRVF
CTPDKDPEQG RFSAELGART LAFYEKEFAS EFPLPKMDMV AIPDFSAGAM ENWGLVTYRV
VDVLLDEKTA SASTKQRVAE VVQHELAHQW FGNLVTMDFW DGLWLNEGFA TWMSWYSCNA
FYPEWKVWQG YVTDNLQSAL GLDSLRSSHP IEVPVKRADE VNQIFDAISY SKGSCVIRMV
SKHLGEDVFM EGIRRYLKKH AYGNTTTSDL WAALSDASGQ DVERIADIWT KEVGFPVVTV
SEKPKENEIH LQQNRFLRTA DVKPEEDKTL YPVFLGLRTK NGVDENLTLN DREGNFKVPD
MDFYKLNADH SGIYRTNYPP ERLQKLGQNA KDGLLTVEDR AGMIADAGAL TAAGYQKTSG
LLSLLKGFDT ESDFIVWDEI TARVGAVRAA WIFEDEKTKD ALKAFQRDLV SGKSHKLGWE
FADNDGHIEQ QFKALLFGSA ASSGDEKAKA AAFDMFEKFI GGDRSAIHPN LRGGVYATVL
SYGGEKEYNA IVKEYETAKN ADERNTALRA IGRAKDPKLI QRTLAYSLSK EVKDQDIYLP
LSGLRAHKEG VVAFWSWMKE NWETLIKKLP PSLSMMGSVV TMGTSSFTKE HQLKDVEAFF
KEKGTKGFER NLAQSKDAIS AKIGWLERDA KDVETWLKEN KYL
//
