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Database: UniProt
Entry: A0A066UD58_9GAMM
LinkDB: A0A066UD58_9GAMM
Original site: A0A066UD58_9GAMM 
ID   A0A066UD58_9GAMM        Unreviewed;       586 AA.
AC   A0A066UD58;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=M61 glycyl aminopeptidase {ECO:0000313|EMBL:KDN25336.1};
GN   ORFNames=MBO_04614 {ECO:0000313|EMBL:KDN25336.1};
OS   Moraxella bovoculi 237.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN25336.1, ECO:0000313|Proteomes:UP000035860};
RN   [1] {ECO:0000313|EMBL:KDN25336.1, ECO:0000313|Proteomes:UP000035860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=237 {ECO:0000313|EMBL:KDN25336.1,
RC   ECO:0000313|Proteomes:UP000035860};
RX   PubMed=24970830;
RA   Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA   Reilly T.J.;
RT   "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT   Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL   Genome Announc. 2:e00612-14(2014).
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:KDN25336.1}.
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DR   EMBL; AOMT01000021; KDN25336.1; -; Genomic_DNA.
DR   RefSeq; WP_036364356.1; NZ_AOMT01000021.1.
DR   AlphaFoldDB; A0A066UD58; -.
DR   eggNOG; COG3975; Bacteria.
DR   OrthoDB; 9778516at2; -.
DR   Proteomes; UP000035860; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.3650; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR024191; Peptidase_M61.
DR   InterPro; IPR007963; Peptidase_M61_catalytic.
DR   InterPro; IPR040756; Peptidase_M61_N.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF05299; Peptidase_M61; 1.
DR   Pfam; PF17899; Peptidase_M61_N; 1.
DR   PIRSF; PIRSF016493; Glycyl_aminpptds; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:KDN25336.1};
KW   Hydrolase {ECO:0000313|EMBL:KDN25336.1};
KW   Protease {ECO:0000313|EMBL:KDN25336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035860}.
FT   DOMAIN          474..557
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   586 AA;  66415 MW;  095F5B38E77F2FB4 CRC64;
     MKYIVDFTRF NEHLVDIHLN FKARVGAPTL WLPTWIAGSY LIREFSKNIT LVQYDHDDTR
     LDAVKRSKNT YELTHIKAGD VVDVHYEVYC HDLSVRTAFL DNTRLFGNFS SLLVVPTGQE
     SDGANISLHV PNAFYALNPN ATLACGLKHT CADDAFGKTY HLEPVAAFDS YDYPFEISIQ
     DEFAFTITDS DGKDLPHRFF IAGKHHGHLP RLQKDIQRIC QAYLDELGSA PFKDYTFMTM
     VTGSDYGGLE HINSTALVSP RTDLPSTHEG TVPSGDYQRY LGLCSHEYFH AWWVKTVRPD
     VMMDSQLQTE APSPLLWVFE GFTSYIDDLV LLRSGVIDKA SYLKLLAAQI NRYYQTAGRD
     LQSVAESSFD AWIKLYRPDE NSTNQGVSYY NKGALIALLL DLTLLKHSDG KYRLFDVVRA
     FYAKALEQDN RRFGMTHENL GKVVGDMIGY DAWQVFFDNY VIGRQPLPIE EMLAEFGIEI
     TAKAQHRAWG MTTEELPSGI KIKHLIRQSP ASKAGLSAND VIVAIDGLKA SQKLIESTTK
     RQNHDDKPVV VHAFRRDELM TFNVHGGSFE YRQVSLVDNT DSIWLN
//
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