ID F4NUU2_BATDJ Unreviewed; 1020 AA.
AC F4NUU2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BATDEDRAFT_34313 {ECO:0000313|EMBL:EGF83642.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF83642.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF83642.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; GL882879; EGF83642.1; -; Genomic_DNA.
DR RefSeq; XP_006675823.1; XM_006675760.1.
DR AlphaFoldDB; F4NUU2; -.
DR STRING; 684364.F4NUU2; -.
DR MEROPS; M01.A25; -.
DR GeneID; 18240395; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; F4NUU2; -.
DR OMA; MEYLCVE; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF300; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..293
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 328..549
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 660..969
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 486
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1020 AA; 114787 MW; B83A768207A1A33B CRC64;
MQQYSSNMER KSELEPLLAN EDAFKVVHAY KTRKSCSSRV FPIMGALALV LTAILAVSLI
WQPALHSTDA GANEIYKEIS KVESVRLPAG IAPSRYNLDI VTKLSTATFS GSVAIDIHVD
TPTQFIAIHQ LELSIGAITL DALTAAPDLT KPFDPKTLST DTKYEVDHIA NITQFQYLEI
YFKQTIEPGY YNLKVDFAGK LQDTLEGFYR SSYTNKHTGK KEYLATTQME PVHARKAFPC
FDEPEFKAIF VISITTESEY HAISNMPATS VKTLPSGLVK YNFAPTLRMS SYLIAYIVSN
FESIEAKTKN GVIVRVFTQR QSTDLGKYAL EVAVKVMEYF QATYAIPFPL PKCDLIAIPD
FQAGAMENWG LITFRDTALL YDPKVSSQGN KQGVASTIAH ELAHQWFGNL VTMKWWSDLW
LNEGFAEFMT YKGTHAAEPE WKMLEQFLPG ELMRAENADE SIFTHPIAIP VKNPEEIQEI
FDDISYGKGS AVLRMLEGYL ETKFGQNYFF THLTSYLNSH SYGNADTSQL WQALQNPGSP
DIAAFMSTWT DQPGFPLVTV SFPSTDDSTK KSSFQVTQKR YIFSGLVDPL STVPEKLIPP
VLNVPKDPST QTWAIPLTFA LFSNHTGKVK RVSDPTVFEF FTHGPIQVDL ATQIPKDTIV
LANYGKSGVY RVQYDERTLH YLLEWLRADI NVFSAVERAG LLSDVFSFTY SGQLSDVTIA
LEFMKLMEHE ESTIVWGTAI REFRTLKKAF AHHPSYGLIQ QFEQNVIHKM VKSIGWVETS
KDTSQHHMRA LLRGLLLQEA VRSGHKKTIA TALDYFKLLM EGKKDKVDVT ADALTAILVA
GVMYGDEANY EWVLQQHLNS TFAPEKSRYL FALASSPVSY LQMRTLDLTL TDKIRKQDIT
SLVENVASST PVGHLTAWIF LMDNWAAIAK WKDYNMTGLG AIIQDIIGKF TNSYLVSEAQ
RLFVDRKDPD LIVPDNIMVA VFKGLETSRQ LVKWQGMVKA DVAAWLRKEL DIFDASAQKE
//
