ID W7J899_9PSEU Unreviewed; 1010 AA.
AC W7J899;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Aminopeptidase Y (Arg, Lys, Leu preference) {ECO:0000313|EMBL:EWC62239.1};
DE EC=3.4.11.15 {ECO:0000313|EMBL:EWC62239.1};
GN ORFNames=UO65_2488 {ECO:0000313|EMBL:EWC62239.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC62239.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC62239.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC62239.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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:EWC62239.1}.
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DR EMBL; AYXG01000084; EWC62239.1; -; Genomic_DNA.
DR AlphaFoldDB; W7J899; -.
DR STRING; 909613.UO65_2488; -.
DR PATRIC; fig|909613.9.peg.2492; -.
DR eggNOG; COG2234; Bacteria.
DR eggNOG; COG3227; Bacteria.
DR eggNOG; COG4934; Bacteria.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03876; M28_SGAP_like; 1.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EWC62239.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EWC62239.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 103..135
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 226..362
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 375..536
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 642..847
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 444
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 1010 AA; 104049 MW; DF343B0FDA39975D CRC64;
MLTRAVPGAD ARGARLGRVP ARPGRATLPR GASMTRRTVT AGLALVVLAG SAVGTPASAA
PVVPDVPDAQ TRALGAADRV AATALGAGPD EVYRRGLVTP WVDGLHSVAY ERTYRGLPVV
GGDATVLTDG NGSVRASAKA SGVTVRIGTA PAVTGEAAEA TARRELARVD AVESRSLVVK
LTGDTPKLAW QTVLGGATAE GESHLTVWVD AVTGTVLDRH DDVEHGTGTS QWNGPSPLAI
TTSQSGGRYL LKDTTRPGLQ CADYSTGQVF SKTTDTWGTG NATSKETGCV DVMWAAQKEF
DMLKNWLGRN GHTGSGGSWP ARVGYNTTNA YWNGSSVTIG RNSAGQWIGA MDVVGHEYGH
GLDQFTPGGA NGEAGLGEGT GDIFGALTEA YANEPAPYDT PGDYLVGEKV NLTGNGPIRN
MYNPSLVNNH PNCYSASIPS TEVHAAAGPL NHWFYLLAEG SNPGGGKPVS PTCDSSSVTG
IGIQAAGKVF YGGMLLKTSG MTYKRYRTAT LTAAKNLDAT CNLYNRTKAA WNAVSVPAQT
ADPTCTAFAR GSTVDSIGAV DSIGAVDVLG GASAQAAPNV DVAKVQAHLT QFNALATQNG
GNRRAGSAGY TASVAYLKGK LQAAGFTVAE QTCTSCNYRS NNLIADWPGG DTSQTVMFGA
HLDSVSAGPG INDNASGSAV LLENALQLAA ANPAMAKHVR FAWWTDEESG LLGSRFYVNS
LTSAQRTAIK AYYNFDMVGS RNAGYFINNI STAVSAPMKA YWDSLGLAPE ENVEGAGRSD
DYSFKNAGIP SSGYATGASA RKTSAQAAKW GGTAGAAYDA CYHSSCDTTA NINATALDRT
ADGVAHTIWA QAVSSGGGTT CTPAELVVNG GFESGTTPWT LSTGVRDSST SQAPRTGTWK
AWLNGSGSAN TESAAQTVTI PAGCTGAVLT YWAHVDTAET GTRVYDRLTV TVGGTSVATL
SNVDAAAGFT QRTVPVGQFA GQTVALKFTG VEDASLQTSF VLDDISLRSA
//
