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Database: UniProt
Entry: A0A0X3TBS4_9RHOB
LinkDB: A0A0X3TBS4_9RHOB
Original site: A0A0X3TBS4_9RHOB 
ID   A0A0X3TBS4_9RHOB        Unreviewed;       460 AA.
AC   A0A0X3TBS4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cytochrome C oxidase subunit II {ECO:0000313|EMBL:KUJ73265.1};
GN   ORFNames=AVO45_16175 {ECO:0000313|EMBL:KUJ73265.1};
OS   Ruegeria marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ73265.1, ECO:0000313|Proteomes:UP000053791};
RN   [1] {ECO:0000313|EMBL:KUJ73265.1, ECO:0000313|Proteomes:UP000053791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ73265.1,
RC   ECO:0000313|Proteomes:UP000053791};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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:KUJ73265.1}.
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DR   EMBL; LQBQ01000039; KUJ73265.1; -; Genomic_DNA.
DR   RefSeq; WP_068350256.1; NZ_LQBQ01000039.1.
DR   AlphaFoldDB; A0A0X3TBS4; -.
DR   STRING; 1685379.AVO45_16175; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000053791; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053791}.
FT   DOMAIN          308..315
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   460 AA;  48101 MW;  8116FB6A88CE4B9D CRC64;
     MTLTFAAPSD GAIPLHVIDR TGLDAWLESQ SPEIGSWVQA NGFTGALGQT LLIPGRDGAP
     ECALAGYGKA SDRARKRFPL AAAAQALPKG TYRIASGVAQ EALEVEALGW LLTGYAYGRY
     KSQSGAKAQL VAPEGVEAAR IEVLAQAEAL IRDLVNTPAA DMGPGELQAA AEDLAREFGA
     SCETIAGDDL LEANLPMIHA VGRAADRAPR LIEMNWGQSG PKLTLVGKGV CFDTGGLDLK
     PAVAMGLMKK DMGGAANVLG LARMIMALNL PLKLRVLIPA VENSVSGNAF RPGDILTSRK
     GLTVEVNNTD AEGRLVLADA LALADEGAPD LVISMATLTG AARVAVGADL APFYADDDEA
     ALALGRAAAR MVDPIWRMPF HEPYEAMIEP GIADLDNAPS GGFAGSITAA LFLRRFVTQS
     AYVHFDIYSW QRAKEPGRSK GGLGQGPRAI LGALPELLKL
//
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