ID A0A061SVW7_9RHOB Unreviewed; 460 AA.
AC A0A061SVW7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cytochrome C oxidase subunit II {ECO:0000313|EMBL:KAJ03635.1};
GN ORFNames=PM02_07380 {ECO:0000313|EMBL:KAJ03635.1};
OS Sulfitobacter mediterraneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ03635.1, ECO:0000313|Proteomes:UP000027337};
RN [1] {ECO:0000313|EMBL:KAJ03635.1, ECO:0000313|Proteomes:UP000027337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ03635.1,
RC ECO:0000313|Proteomes:UP000027337};
RX PubMed=24855294;
RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT Mallorca Island (Mediterranean Sea).";
RL Genome Announc. 2:e00350-14(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:KAJ03635.1}.
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DR EMBL; JEMU01000005; KAJ03635.1; -; Genomic_DNA.
DR RefSeq; WP_037906820.1; NZ_JEMU01000005.1.
DR AlphaFoldDB; A0A061SVW7; -.
DR STRING; 83219.PM02_07380; -.
DR eggNOG; COG0260; Bacteria.
DR Proteomes; UP000027337; 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:UP000027337}.
FT DOMAIN 308..315
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 460 AA; 48042 MW; 4FFA9B4E79083DBD CRC64;
MPPRFASDAS SALPLHVIAE DGLDAWLSDQ PEAAQTWIAA QGFTGGLGQA LTIPAADGSV
MMAVAGFGTA AARARGRFHL AAAAAKLPKG IYQIVSGLPD DQKSVEALGW LLSRHSFDRY
KSQSPIAAEL LAPEAVNVAE VEALAAGECM TRDLINTPAS DMGPPDLEQA ARDLAKAHGA
QINVITGDDL LKQNLPMIHT VGRAADRAPR LIDMRWGDSG PTLTLVGKGV CFDTGGLNLK
PGASMGLMKK DMGGAAAVLG LAHMIMATGK QVQLRVLVPA VENAVSGNAF RPQDILTSRK
GLTVEINNTD AEGRLVLADA LALADEEKPD QIISMATLTG AARVAVGPDL APYFSDDAGF
VTALESAAAA QADPVWRLPF HDPYEAMIEP GIADLDNAPK GGFAGCITAA LFLRRFVSDS
PYAHFDIYGW QPAAAPARPK GGVGQATRAL FGALDEILTR
//
