ID A0A212R1X0_RHOAC Unreviewed; 463 AA.
AC A0A212R1X0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:SNB65995.1};
GN ORFNames=SAMN06265338_102367 {ECO:0000313|EMBL:SNB65995.1};
OS Rhodoblastus acidophilus (Rhodopseudomonas acidophila).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Rhodoblastus.
OX NCBI_TaxID=1074 {ECO:0000313|EMBL:SNB65995.1, ECO:0000313|Proteomes:UP000198418};
RN [1] {ECO:0000313|Proteomes:UP000198418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 137 {ECO:0000313|Proteomes:UP000198418};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FYDG01000002; SNB65995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212R1X0; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000198418; 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; 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:SNB65995.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000198418}.
FT DOMAIN 306..313
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 463 AA; 48611 MW; E13871134C129CB1 CRC64;
MPDLPELKFA DDGEAIPVWC APVAAIKAAL DGAAHALPAE ALSLAKASGF APGAGKSLAF
VQAGGAPGVL FCLDEDGDVF QFGALAGLPE GVYRLAEAPE HPDVAGLGFL LGAYRFTRYK
AAKPGARLIA PQGADRAEVE TVASAVALAR DLINTPANDL GPDELEGFAR ALAEKFGAAV
RVIQGAELER ECPLIHAVGK GSPRVPRLVE LRWKPERAKK LALVGKGVCF DSGGLNIKPD
SAMALMKKDM GGAAAALAAS AMIMAGDLDL SLRLLLPIVE NSVSGEAFRP GDVYRSRKGL
TVEIGNTDAE GRLILADALA LADEEAPDLL VDFATLTGAA RVALGPDLPP FYTDDDKLAE
MIARNGFACN DPVWRLPLWK AYEPKLDSKI ADLNNAPAGG MAGSIMAALF LKRFVTPGRA
WAHFDIYGWT PAAKPGRPEG GEAQAARLIY NLAREKFNVA KLS
//