ID   I9ND57_RHILT            Unreviewed;       463 AA.
AC   I9ND57;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:EJB04672.1};
GN   ORFNames=Rleg9DRAFT_3529 {ECO:0000313|EMBL:EJB04672.1};
OS   Rhizobium leguminosarum bv. trifolii WSM597.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=754764 {ECO:0000313|EMBL:EJB04672.1, ECO:0000313|Proteomes:UP000005092};
RN   [1] {ECO:0000313|EMBL:EJB04672.1, ECO:0000313|Proteomes:UP000005092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM597 {ECO:0000313|EMBL:EJB04672.1,
RC   ECO:0000313|Proteomes:UP000005092};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R.,
RA   O'Hara G., Rui T., Howieson J., Reeve W., Woyke T.;
RT   "Improved High-Quality Draft Sequence of Rhizobium leguminosarum bv.
RT   trifolii WSM597.";
RL   Submitted (FEB-2012) 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; JH719381; EJB04672.1; -; Genomic_DNA.
DR   RefSeq; WP_003589209.1; NZ_JH719381.1.
DR   AlphaFoldDB; I9ND57; -.
DR   HOGENOM; CLU_013734_2_1_5; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000005092; 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:EJB04672.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          311..318
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   463 AA;  49951 MW;  7E6EDA35EB569508 CRC64;
     MAPYQFTERP TPFNAKGGST LPIFAVTPAH IETGTIDPIA LDWAQRAGYK AESGSLLLIP
     TADGHLGGAL FGLGTNPSEQ PYITGRLARA LPAGDWHIET APLTANRLAL GFGLGSYRFD
     RYKSEKSPAA TLMIPRDADS ADIKRQLAGV FLARDLINTP TNDMGPNQLE TVFRGLAAHY
     KADVSVITGD ELLEQNFPLV HTVGRASADA PRLLELRWGK KGHRKVTLVG KGVCFDTGGL
     DIKPAASMLL MKKDMGGAAN VMGLALMIMD AKLKVDLRVI VPVVENAISS NAFRPGDIYK
     SRKGLTVQID NTDAEGRLIL ADALAYADEE EPDLLIDMAT LTGAARVALG PDLPPFFTDD
     ANLAHDLTEA SLETDDPIWR LPLYSGYEKD IRTKFADLTN APAGGMAGAI TAALFLKRFV
     GKTKSWAHFD IYGWAQSERP HSPGGGEAQA IRALFHHIRE SLR
//