ID   A0A3L9Y1I0_9RHOB        Unreviewed;       461 AA.
AC   A0A3L9Y1I0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Leucyl aminopeptidase family protein {ECO:0000313|EMBL:RMA42694.1};
GN   ORFNames=D9R08_07835 {ECO:0000313|EMBL:RMA42694.1};
OS   Rhodophyticola porphyridii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodophyticola.
OX   NCBI_TaxID=1852017 {ECO:0000313|EMBL:RMA42694.1, ECO:0000313|Proteomes:UP000281343};
RN   [1] {ECO:0000313|EMBL:RMA42694.1, ECO:0000313|Proteomes:UP000281343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MA-7-27 {ECO:0000313|EMBL:RMA42694.1,
RC   ECO:0000313|Proteomes:UP000281343};
RA   Jung H.S., Jeon C.O.;
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:RMA42694.1}.
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DR   EMBL; RCNT01000003; RMA42694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L9Y1I0; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000281343; 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; 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:RMA42694.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281343}.
FT   DOMAIN          308..315
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   461 AA;  47761 MW;  56D0AC5AC729CFE4 CRC64;
     MSARFAEESA EAIPLHLLAP DDIPDELPSL TAAQRAWVTH LGFSGKAGEA VSLADTEGAP
     AMVLVGLGTA RDRARERFAA GAAIAGLPKG TYRIAATPGG AAGHEIALGY LLACYRFDRY
     RTQPGPEAAL VAPDGCDANR LEQIAAAEFL TRDLINTPAE DMGPDALEAA LRGLAGRYGG
     EVNSTEGAAL IAANLPLIHT VGRAAARAPR LLDMTWGENG PALTLVGKGV CFDTGGLNLK
     PSASMGLMKK DMGGAATVLG LARMIMAANM PLRLRVLIPA VENAISGNAF RPGDILTARN
     GLTVEINNTD AEGRLVLADA LALASETPPD LLVSMATLTG AARVAVGPDL APFYTDDEAL
     AAALATAAGA VADPVWRMPF HEPYETMIEP GIADLDNAPK GGFAGSITAA LFLRRFVADT
     PRYAHFDIYG WQPSAAPARP KGGVGQGARC LFEALPKVLG L
//