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Database: UniProt
Entry: A0A1E3QU47_9ASCO
LinkDB: A0A1E3QU47_9ASCO
Original site: A0A1E3QU47_9ASCO 
ID   A0A1E3QU47_9ASCO        Unreviewed;       882 AA.
AC   A0A1E3QU47;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=BABINDRAFT_33484 {ECO:0000313|EMBL:ODQ81228.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ81228.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-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}.
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DR   EMBL; KV454428; ODQ81228.1; -; Genomic_DNA.
DR   RefSeq; XP_018986556.1; XM_019131637.1.
DR   AlphaFoldDB; A0A1E3QU47; -.
DR   STRING; 984486.A0A1E3QU47; -.
DR   GeneID; 30149490; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000094336; 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:UP000094336};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          18..218
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          258..475
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          546..858
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        331
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            416
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   882 AA;  97625 MW;  4A5F7BEA8D9D24DE CRC64;
     MCSSQVEKQV EVLPKNLKPS NYDIQIFDID AVANTFSGRV AITMEILQNT SEVVLNVRDL
     EVASAKVQLT VTKTEQEIPV VEITSDKKQE TVTLKLAEPL KAAPSASLVV TLNYTGLIQT
     NMAGFYRSRY TNAEGQDAVM LSTQFEATDA RRAFPCFDEP NLKATFDVAI VLRADWTVLS
     NMPELESRTL DSGKKGPGAD QELKLVRFET TPIVSTYLVA WAMGDFECIE TTTAELYNGK
     PLPVRVFTTK GIVEQGRFAL EMTAKTLDFF SQKFEIPYAL PKVDLIAVHE FSHGAMENWG
     LITFRSTAIL YDPAKSDPKY QKNVAYVVAH ELAHQWFGNL VTMNWWDELW LNEGFATYAG
     FMAVDNFYPD WKVFDAYVSE SLQSALNLDA LRGSHPIEVP VYSALDIDQV FDAISYLKGS
     STIRMLATTI GVDTFFRGVA KYLNRHKYSN ATTANLWAAV GEVSGVDVAQ IMESWIQKIG
     FPVLSVSETE DHKLKITQDR FLLSGDVKPE ENETKWWIPL NIASDDTDVV KALEAKELVI
     DKPANFIKLN KDSVGVYRVS YTPELFSNIT ANIETLNAKD KVGLIADAAS CAKAGLSATS
     TLLKLAKALS GESEFVVWSE LINRVGEITS TWYQQPEPVQ KALNKFAREL YGPASAKIGY
     EVAETDGFLT LQLRAKLMLA AGLAGVPEVV AFARKTFDSY ARGEKIHPSL RIAVFSTVLA
     ADTVTAADFD LVLKEVLTPS SLDGREIALQ SLGCTNTAVL GNKAVTLLSD VPTMDAHYLS
     VSLAANTDAR HLLWDYFAAN YDALYKAMST NMVVLDRFVK VSLGSFADIK EEEKIRAFFE
     GKDTNGFQRS LSQILNKISG NAIWVNKDAG DVEAWLKAEH YL
//
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