ID A0A1X2HET1_SYNRA Unreviewed; 558 AA.
AC A0A1X2HET1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal domain-containing protein {ECO:0000259|SMART:SM01263};
GN ORFNames=BCR43DRAFT_530580 {ECO:0000313|EMBL:ORY97412.1};
OS Syncephalastrum racemosum (Filamentous fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX NCBI_TaxID=13706 {ECO:0000313|EMBL:ORY97412.1, ECO:0000313|Proteomes:UP000242180};
RN [1] {ECO:0000313|EMBL:ORY97412.1, ECO:0000313|Proteomes:UP000242180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORY97412.1,
RC ECO:0000313|Proteomes:UP000242180};
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:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:ORY97412.1}.
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DR EMBL; MCGN01000004; ORY97412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2HET1; -.
DR STRING; 13706.A0A1X2HET1; -.
DR InParanoid; A0A1X2HET1; -.
DR OMA; CTALQWM; -.
DR OrthoDB; 443480at2759; -.
DR Proteomes; UP000242180; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 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; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634015-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000242180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 410..555
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 94..96
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 207..212
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 511..513
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ SEQUENCE 558 AA; 63204 MW; EE8BA9C0B3D72A01 CRC64;
MVTRVDNVAK IVLDTSYIDV KSATLAGQAL KFTIAERHPH LGSALTLDLP EPIATAGTEL
QIKIDYATTE KCTAIQFLEP EQTVGQKYPY LFSQCQAIHA RSFVPCQDSP SVKLTYSAAV
TSPLRVLMSA LETKSVENAS NSTTTYHFEQ RTTIPSYLIA IASGNLAGRE IGPRSTDTES
FIKTGEDLLT PYEWGRYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDRSA VDVVAHEISH
SWMGNLVTTR NWEHFWLNEG WTVFVERKIA GRLHGEAERQ FSAIIGWKAL KESVELFGEN
SPATVLKPDL SSGVDPDDYF SSVPYEKGFN LLYHIEKTVG GPEVFEPFMK AHVEKFASES
VTTEQWKAFL YEFMEKHHGQ AVVDKLNTID FDLWINGTGM PPVDPEFDTT LADICYKLAD
RWDKARDSQD FTGFSPEDIK DMKADQKIVF LERLTDTKPM PHSLLAKMDE LYHFTPIRNA
DIRFRWQQLC VMASYEPIYP HVVKFVTEQG RMKFVRPLYR LLHRATNGKE LAEKTYLEHK
KFYHPIAAQL IEKDMGLN
//
