ID A0A3M2JU79_9CELL Unreviewed; 545 AA.
AC A0A3M2JU79;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Leucyl aminopeptidase family protein {ECO:0000313|EMBL:RMI13718.1};
GN ORFNames=EBM89_03090 {ECO:0000313|EMBL:RMI13718.1};
OS Cellulomonas triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2483352 {ECO:0000313|EMBL:RMI13718.1, ECO:0000313|Proteomes:UP000269289};
RN [1] {ECO:0000313|EMBL:RMI13718.1, ECO:0000313|Proteomes:UP000269289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY56 {ECO:0000313|EMBL:RMI13718.1,
RC ECO:0000313|Proteomes:UP000269289};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:RMI13718.1}.
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DR EMBL; RFFI01000010; RMI13718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2JU79; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000269289; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:RMI13718.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000269289}.
FT DOMAIN 390..397
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT REGION 39..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 56092 MW; 1E2178A56A27956C CRC64;
MNPSEVRVGR AVPAVVLAAG TLASSDLLLA PDVDAVAVPV APSTPDEPED TDLQPRRGTA
DAAARYGIDL AELAERARLT GAAGEAWTLL LPRPVGSAGA ALPWAGLPRR LVLVGVGEGT
PQDLRRAGAA LARATRGLRR VLTTVGTEPG ADGPRSVRAL AEGYLLAAYR VQRLGAPAPA
SDAPATELVV VGRDGVRAQA ALDEAVRGAT ATWLVRDLAN TPSSTKDPEW MADRAVELAR
AAGLTTEVLG PRELAAQGFG GILAVGAGSA SPPRLVTVTY DPAALPPADD EDATAAPTSR
RAKHVVVVGK GITYDTGGIS IKPREAMVPM KTDMAGAAVA LATVLGAAAA RVPHRVTAVL
PLAENHFGAS SYRPGDVLRM WGGRTVEIAN TDAEGRIVLG DALAWADATL DPDVLLDVAT
LTGAASLGLG KQHAALYATD ARLSGALEVA GAESGEAVWP MPLVEDYTDA VRSDVADLRH
VPQDGKYGGG SITAALFLRE FVGTRTWAHL DIAGPARATA DKHEVTEGAT GYGARLLLRY
LAALR
//
