ID A0A1Y2HL96_9FUNG Unreviewed; 891 AA.
AC A0A1Y2HL96;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=BCR44DRAFT_119150 {ECO:0000313|EMBL:ORZ34473.1};
OS Catenaria anguillulae PL171.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ34473.1, ECO:0000313|Proteomes:UP000193411};
RN [1] {ECO:0000313|EMBL:ORZ34473.1, ECO:0000313|Proteomes:UP000193411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL171 {ECO:0000313|EMBL:ORZ34473.1,
RC ECO:0000313|Proteomes:UP000193411};
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:ORZ34473.1}.
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DR EMBL; MCFL01000028; ORZ34473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2HL96; -.
DR STRING; 765915.A0A1Y2HL96; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000193411; 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:UP000193411};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 13..203
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 247..462
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 546..868
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 403
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 891 AA; 99100 MW; B6C9EA0D20FE60DC CRC64;
MSEEREILPT NVVPTHYNVE LTPDLESFTF EGSVDIQVKI VEATSVVKVN VKELELHAAR
ISLSHNKAEK TLLAASITDD SHTEQATITF PEELPAGAQA TLSITFKGIH NDKMAGFYRS
GYKDNEGKQK HMVVTQFEAT DARRAFPCWD EPALKATFDV TLNVRKELTA LSNMNVVSEE
AHASKATHKS VKFARTPIMS TYLLAFAVGE LEYIESKTSP SCKALPNPVT VRVYTTKGES
GKGKFGLGCA VRILEYFSEV FGEPYPLPKM DMIAVPDFSA GAMENWGLVT YRTIYLLFDE
KTSSAKTKEG VAYVVAHELA HQWFGNLVTM EWWNELWLNE GFATWVGWLA TDALFPDWNI
WTSFVSNDMN RAFGLDGMRS SHPIQVPVSS AREISQIFDA ISYSKGASVI RMLSSWLSQE
VFLAGIRKYI QRHKYGNAST NDLWTALSEA SGLNVNDFMN LWTSKIGYPV LSAERKGDKV
HVSQARFLST GDVKAEEDET LWWCPLNMYT GDDEATKRTA QSTILKTREG VFQLPARPAG
SAIDMYKLNR HQANFYRVKY APADLEKLGE AISSGSGVLN TSDRVGLVGD VFALAAAGYT
STVDALTLLK HFNKEDEYIA LNIVAEKLAH LKTVWTTEPE EVTERLNALA RSIFAPTARK
VGWEFHDGEG QLDVLLRTLA ISVAGMNSDK DVVAQAKTRF ARFIQGDDAA IHPNLRGAVY
NIVLKHAAAG SRAEFDQIKA IWENETLATD QRLAALAALG RHPDLALSSE LLEYTLNSGK
VRDQDFMYPL RSVAANHKAR VLAWQFVQNN WATLESKFKS SLSLLSHCVS IAADWADAEF
GNEVKVFFED KDTKAVDRAL GQTLEKISAQ SAWLNRDRDA VAQWLKENVQ A
//
