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Database: UniProt
Entry: A0A0E3Z248_9GAMM
LinkDB: A0A0E3Z248_9GAMM
Original site: A0A0E3Z248_9GAMM 
ID   A0A0E3Z248_9GAMM        Unreviewed;       455 AA.
AC   A0A0E3Z248;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Cytochrome C oxidase subunit II {ECO:0000313|EMBL:AKC87063.1};
GN   ORFNames=WQ53_10205 {ECO:0000313|EMBL:AKC87063.1};
OS   Pseudoxanthomonas suwonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC87063.1, ECO:0000313|Proteomes:UP000033067};
RN   [1] {ECO:0000313|EMBL:AKC87063.1, ECO:0000313|Proteomes:UP000033067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J1 {ECO:0000313|EMBL:AKC87063.1,
RC   ECO:0000313|Proteomes:UP000033067};
RX   PubMed=26067962;
RA   Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT   "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT   Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL   Genome Announc. 3:e00614-15(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP011144; AKC87063.1; -; Genomic_DNA.
DR   RefSeq; WP_052632058.1; NZ_CP011144.1.
DR   AlphaFoldDB; A0A0E3Z248; -.
DR   KEGG; psuw:WQ53_10205; -.
DR   PATRIC; fig|314722.6.peg.2194; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000033067; 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; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF20; PEPTIDASE B; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033067}.
FT   DOMAIN          304..311
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   455 AA;  48428 MW;  77DF78C8D38672CB CRC64;
     MNHQSHYADT GSHALPLHLL DRDGYGAWRS AQPAAVSAWL DAQEFQPAPG SVALLPGEDG
     LLGAVVGIGD PLDPCSYAHA PTALPPGAWV PAAELPAGQQ AALQLGWGLG SYRFDRYKNP
     PRTPARLRLA TLDGEALDLL HATMRVRDWV NTPTQDMGPQ QLEAIARELA AEHGAHIEVV
     AGESLLAHNF PAIHAVGRAS HRAPRLIELR WGEQTHPHVV LVGKGVCFDT GGLDIKPADG
     MRNMKKDMGG AAHALALAGL VMAQKLPVRL SVLVPAVENA IGPDAFRPGE VIATRAGVSV
     EIDNTDAEGR VVLCDALTYA GEQKPALIVD FATLTGAARI ALGPDLPALF ANDDALAASW
     IAAGEQTRDP VWRLPLWRPY LRYLTSHVAD LANAGSRMAG AVTAALYLER FVPGGTPWAH
     LDTYAWNDSS RPGRPVGGEA LGLRSAWAML KARYL
//
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