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
//