ID A0A0X3TNL5_9RHOB Unreviewed; 460 AA.
AC A0A0X3TNL5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cytochrome C oxidase subunit II {ECO:0000313|EMBL:KUJ77348.1};
GN ORFNames=AVO44_17270 {ECO:0000313|EMBL:KUJ77348.1};
OS Ruegeria profundi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ77348.1, ECO:0000313|Proteomes:UP000053690};
RN [1] {ECO:0000313|Proteomes:UP000053690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT108 {ECO:0000313|Proteomes:UP000053690};
RA Zhang G., Stingl U.;
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:KUJ77348.1}.
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DR EMBL; LQBP01000010; KUJ77348.1; -; Genomic_DNA.
DR RefSeq; WP_068339691.1; NZ_LQBP01000010.1.
DR AlphaFoldDB; A0A0X3TNL5; -.
DR STRING; 1685378.AVO44_17270; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000053690; 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}.
FT DOMAIN 308..315
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 460 AA; 48565 MW; 362E00D4C7BD7B40 CRC64;
MTLSFASPSD PSLPLYVIAQ PDLDDWLNDQ PQSLTNWLKS CDFTGRLGQV ALVPGPDGTP
SFAVAGYGKP AIRRRKRFPL AAAAEALPEG NYHIASGVPA NALETECLGW LLTGYAFDTY
AKQSPAKARL VAPDGIDAPR IEILAQSEAL TRDLVNTPTA DMGPDQLQAA VETLAQDFGA
SCKAVRGQAL LDQNLPMIHA VGRAAVQDPR LIEMNWGNSG PKLTLVGKGV CFDTGGLNLK
PGNSMALMKK DMGGAANVLG LAQMIMAMNL PLQLRVLIPA VENSVAGNAF RPGDILTSRK
GLTVEINNTD AEGRLVLADA LTLADEGGPD LVISMATLTG AARVAVGADL APFYTDDETA
AQALMQAGQK AADPVWRMPF HDPYEAMIEP GIADLDNAPS GGFAGSITAA LFLRRFVGNS
RYVHFDIYSW QPRKAPGRSK GGLGQGPRAL LTALPEVLGL
//
