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Database: UniProt
Entry: A0A345WSN8_9SPHN
LinkDB: A0A345WSN8_9SPHN
Original site: A0A345WSN8_9SPHN 
ID   A0A345WSN8_9SPHN        Unreviewed;       462 AA.
AC   A0A345WSN8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Leucyl aminopeptidase family protein {ECO:0000313|EMBL:AXJ96690.1};
GN   ORFNames=DM480_15560 {ECO:0000313|EMBL:AXJ96690.1};
OS   Sphingomonas sp. FARSPH.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2219696 {ECO:0000313|EMBL:AXJ96690.1, ECO:0000313|Proteomes:UP000254856};
RN   [1] {ECO:0000313|EMBL:AXJ96690.1, ECO:0000313|Proteomes:UP000254856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FARSPH {ECO:0000313|EMBL:AXJ96690.1,
RC   ECO:0000313|Proteomes:UP000254856};
RA   Bendezu Eguis J., Morales Ruiz S., Montesinos R., Quispe Conislla J.,
RA   Tataje-Lavanda L., Fernandez-Sanchez M., Fernandez-Diaz M.;
RT   "Cell Culture Contaminant.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP029985; AXJ96690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345WSN8; -.
DR   KEGG; sphf:DM480_15560; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000254856; Chromosome.
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; IPR048816; Peptidase_M17_N_1.
DR   PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF21337; Peptidase_M17_N_1; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
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:AXJ96690.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254856}.
FT   DOMAIN          308..315
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   462 AA;  48888 MW;  C4549E0C74E537E0 CRC64;
     MTDFAALLQA DRGQPARTIH VVHPDDFTAW LVAQPPRTRT AIAAHALSGK AGDRAVLPGE
     AADDWSMLLV CNEAKSSPWR IASLAATLPA GTYRLADGDV GAAGLGWLLA QHRFDLYRKG
     DPVAPRILLT REPAAIDETV RLAAATALVR DLVNTGASDL GPAELEAAAA RLAGAHHATL
     TVTRGDALAS GYPMIHAVGQ AATKERAPRL VELTWGDPAH PRIAIVGKGV VFDTGGLDIK
     PSAGMRLMKK DMGGAAHALA LADLVMAARL PVRLHLLIPA VENAIAGNAF RPGDVLRSRA
     GITVENTNTD AEGRLILGDA LTRAAEEQPA LILDFATLTG AARVALGPDL PPLFTDDEAL
     AADLLAAGDT LHDPLWRMPL WNGYDEMLKS DIADMVNAPD GGFAGAITAA LFLRRFVPKD
     TPWAHMDVFA WRPAAKPGRP KGGDAFGLRA CYQLLRTRYA AR
//
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