ID A0A0F4RIS8_9RHOB Unreviewed; 459 AA.
AC A0A0F4RIS8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cytochrome c oxidase subunit II {ECO:0000313|EMBL:KJZ19475.1};
GN ORFNames=TW80_09700 {ECO:0000313|EMBL:KJZ19475.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ19475.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ19475.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ19475.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ19475.1}.
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DR EMBL; JXYE01000003; KJZ19475.1; -; Genomic_DNA.
DR RefSeq; WP_045997618.1; NZ_JXYE01000003.1.
DR AlphaFoldDB; A0A0F4RIS8; -.
DR STRING; 579483.TW80_09700; -.
DR PATRIC; fig|579483.3.peg.1992; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000033741; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741}.
FT DOMAIN 308..315
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 459 AA; 48048 MW; 2DE736BEE9EE428A CRC64;
MLLTFAANSE NAIPLYVVET DGLDAVLSNF SDRGRKWVVG QGFTGALGQV VSIPGEDGSV
DAVLAGYGSA KARARGRFHM GVIAAKLPQG IYRIADGLSG ADLEEAALAW LLAQYKFDRY
APATAAVAQL VAPDGVDADR IATIATGEAL TRDLINTPAS DMGPQELEDA ARALANEHGA
NVTVTKGDDL VEAGFPMVHA VGRASTRAPR LIDMRWGNAG PQLTLVGKGV CFDTGGLNIK
PGASMGLMKK DMGGSATVLG LAHMIMGLGL PLRLRVLIPA VENSIDGNAF RPQDILTSRK
GLTVEINNTD AEGRLVLADA LTLSDEDNPD LVISMATLTG AARVAVGPDL SPFYTDNDDH
AAAIASAARA VADPVWRMPF HEPYEAMIEP GVADLDNAPK GGMAGSITAA LFLRRFIESP
YIHFDIYGWQ PNAAPSRPKG GVGMGARAVL DALPEMLGL
//