ID   U9VZR2_9CYAN            Unreviewed;       450 AA.
AC   U9VZR2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:ESA37517.1};
GN   ORFNames=N836_36465 {ECO:0000313|EMBL:ESA37517.1};
OS   Leptolyngbya sp. Heron Island J.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA37517.1, ECO:0000313|Proteomes:UP000017515};
RN   [1] {ECO:0000313|EMBL:ESA37517.1, ECO:0000313|Proteomes:UP000017515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Heron Island J {ECO:0000313|EMBL:ESA37517.1,
RC   ECO:0000313|Proteomes:UP000017515};
RX   PubMed=24503993;
RA   Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA   Fromme P.;
RT   "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT   Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL   Genome Announc. 2:e01166-e01113(2014).
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:ESA37517.1}.
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DR   EMBL; AWNH01000023; ESA37517.1; -; Genomic_DNA.
DR   AlphaFoldDB; U9VZR2; -.
DR   STRING; 1385935.N836_36465; -.
DR   PATRIC; fig|1385935.3.peg.1659; -.
DR   eggNOG; COG0260; Bacteria.
DR   Proteomes; UP000017515; 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:ESA37517.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017515}.
FT   DOMAIN          298..305
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   450 AA;  48348 MW;  FBE29DAD775FE300 CRC64;
     MEVPLADAIA IYLVNAEELQ NDHPDSLTWC QASGFSGQVG KSCLVPDAAG KISKVLVGRP
     ESLDTWTLAA LPKTLPTGTY DLAGMFSTHN ATKLYLGWQL GSYNFDRYKL TKVGPVATLQ
     PPENVDLTYV KATTEATYLV RDLITTPSNN MGPDQLEEIT RTLADRYEAQ VAVIAGGDLV
     IENYPMIYAV GKASTRAPRL IDLRWGNPDA PRVTLVGKGV CFDSGGLDVK SATGMRLMKK
     DMGGAAQVLG LAQMIMEVGL PVNLRVLIAA VENSIAGNAL RPLDILTSRK GTTIEVGNTD
     AEGRLVLADA LWEASSEDPD LLIDCATLTG AARVALGTEL PAFFCNNDET TATLLKAGLA
     VDDPLWNLPL HSAYRSMLDS PVADMNNIAS GSYGGSITAA LFLQEFIQTE VPWIHVDFMA
     YNLRSLPGRP EGGEAMGMRA LFQLIKQRLA
//