ID A0A0H5CSD0_9PSEU Unreviewed; 1253 AA.
AC A0A0H5CSD0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Aminopeptidase Y (Arg, Lys, Leu preference) {ECO:0000313|EMBL:CRK60819.1};
DE EC=3.4.11.15 {ECO:0000313|EMBL:CRK60819.1};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK60819.1, ECO:0000313|Proteomes:UP000076116};
RN [1] {ECO:0000313|Proteomes:UP000076116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA Ramaraj T.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LN850107; CRK60819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5CSD0; -.
DR STRING; 1653480.gene:80949709; -.
DR KEGG; alo:CRK60819; -.
DR Proteomes; UP000076116; Chromosome i.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase 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; 3.10.450.490; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 2.
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; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51829; P_HOMO_B; 2.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CRK60819.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CRK60819.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000076116};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1253
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005217047"
FT DOMAIN 618..746
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 1134..1253
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 325
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 411
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 1253 AA; 128435 MW; 0CFA6AD821FB6928 CRC64;
MKRSMSTALL AAAVAAGALV VSLPAGAAPT ISAAQQAQVA AAAAADNFVR GNSQRFLTSQ
QDEVQQVKVD SSDNGLQYIS YERKHRGLPV VGGDFVVVTN ASANVVNSSV AQETVLDVAV
SPRITVEAAR ATAKRHLPHV DSQRSSRLVV LAWGTPKLAW EIVMEGRTAS APSVLHVFVD
ALTGSVIDEY DEVKAGTGRG YYNGDVTIQT SGSGSSYTMT DTTRSGLKCG GQNGSAYTGT
DDAWGNATGT DLETACVDAM YAAQKEWDML SAWLGRNGFN GQGGAFPARV GLAQVNAFWN
GSYTNYGHSQ DNQRQVVPID VVAHEYGHAI FQNTPGGAGS GNENGGLNES TGDIFGALTE
FYANNANDPG DYLVGEEVNL VGNGPIRNMY NPSALSDPNC YSSSIPNTEV HAAAGPQNHW
FYLLAEGSAP GGGKPNSPIC TGGPASVTGI GIQNAGKIFM NGLLSKTSTW NHAKARVATL
AAAKNLWPND CTNFNATKNA WLAVSVPAQA GEATCTGTPT NDFSVSASPT SGTIPAGGGS
VTSTIGTTTT SGSAQTVNLS ASGLPSGVTA AFNPTSVTSG SSSTLTLTST AAAAAGTYNV
TITGAGSVSR TTTFALTIGP GGPGGSCEGS NTNALAIPDN TTVESSITIS GCSGNASATS
TIPVDINHTW RGDVVIDLVA PDGTAYRLKN SSSNDSADNI KQTFTANLSS EVANGTWKLR
IQDVATNDTG TLNNWSLKVG DGSTPVNDFS IATSPTSGSV QAGASATTTV STTTTSGSAQ
TVNLTASGLP AGVTASFSPT SVTSGNSSTL TLATTAAAAA GNYNVTITGT GSVTKTANYA
LTVTGTTPNP GIPDIDIAKV QAHLNEFGTI AANNGGNRRS TSAGYRASLA YVKGKLQAAG
YTVTEQTCTS GCTSGSGNNL IAEWPHGNAN TVYMFGAHLD GVSAGPGIND NGSGSGALLE
AALVLAEKNP TMTNRVRFGW WTDEEQGLNG SEFYVNNLPS TEKAKIKAYY NFDMVGSKNG
GYFINNINSA ASAPMKAYYD SLNIQPEENT EGQGRSDDYS FQQGGIPTSG YAMGASARKT
SAQATKWGGT ANAAYDACYH ASCDTTSNIS ATHLNRAADG IAYTIWKQAV SGGTPPPPPG
CAGTNTNAVN IPDNTTVESA ITIANCSSAP SATATVPVDI NHTWRGDVVI DLIAPDGSAY
RLKNSSSNDS ADNVKQTFTV NLSGETSNGT WKLRVQDIAT NDTGVINSWS LNL
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