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Database: UniProt
Entry: W9XFM4_9EURO
LinkDB: W9XFM4_9EURO
Original site: W9XFM4_9EURO 
ID   W9XFM4_9EURO            Unreviewed;       883 AA.
AC   W9XFM4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=A1O3_08519 {ECO:0000313|EMBL:EXJ79018.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ79018.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ79018.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ79018.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) 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:EXJ79018.1}.
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DR   EMBL; AMGY01000008; EXJ79018.1; -; Genomic_DNA.
DR   RefSeq; XP_007736806.1; XM_007738616.1.
DR   AlphaFoldDB; W9XFM4; -.
DR   STRING; 1182542.W9XFM4; -.
DR   MEROPS; M01.007; -.
DR   GeneID; 19172606; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_003705_0_1_1; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000019478; 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:UP000019478};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          25..211
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          246..463
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          538..856
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
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         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            404
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   883 AA;  98930 MW;  B511713E45990D5E CRC64;
     MCRFMSDSPG AASTQGRVIL PDDVVPKHYD VTLEVDFDKF TFEGTVIIAL DVARDTSSIA
     LNTLELDIHT TTIHADGALV TSSPTLSYDA ETQTTTIQLG KSITKGQKVQ LKQTYTGQLN
     DKMAGFYRSK RRDGQYLAVT QFEATDARRA LPCFDEPALK AEFTVTLIAD EDKTCLSNMD
     VASTEIVDSK ITGGKRKAVK FNRSPRMSTY LLAFIIAELK SISTDKFRLP IKVWMTPEQN
     DDDGKFALDV AAKTLAFYEK AFQAPYPLPK MDMVAIPDFA AGAMENWGLV TYRVVDLLFD
     QKSAGAATKE RVAEVVQHEL AHQWFGNLVT MDFWDGLWLN EGFATWMSWY SCNEFYPEWK
     VWQTFVIDTL QGALGLDGLR SSHPIEVPVH RAEDINQIFD AISYSKGSAV LRMISKYLGE
     DVFIEGIRKY IKKHAWGNTK TSDLWDALGD ASGKDVAHVM DIWTKYIGYP VVTVTENEKD
     STITVKQNRF LRTGDVKPDE DQVLYPVMLG IRTKEGVDEN LMLTEREQTF KIKGGLEFYK
     LNTDHSAFYR TSYTPDRLMK LGEAAQKGLL SVEDRAGMIA DAGALAASGY GKTSGILSLL
     QAFNTESDFV VWNEILTRIN AVRNTWLFED ESIKDALKAF QLNLCSAKAH ELGWEFSDDE
     DHILGQFKSL MFGSAGLAGD QKVQAAAKEM FAKFLKGDYN AIHPNLRASV LAMALRDGGV
     KEWEAVLARY HSAPTADEKN TCLRSLGRAR SPELIKKTLD LALGGEVKMQ DIYMPIGGLG
     TTSEGVEKRW EWMCKNWETL VEKLPPSMSM LSSVVSICVA GFTKEEQLGK IDEFFRDKDT
     KGFDRSLQQS FDSIRAKSNW LKRDGDDVLG WLKEKGYLEK GRL
//
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