ID F2RIL8_STRVP Unreviewed; 434 AA.
AC F2RIL8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Aminopeptidase Y (Arg, Lys, Leu preference) {ECO:0000313|EMBL:CCA57574.1};
DE EC=3.4.11.15 {ECO:0000313|EMBL:CCA57574.1};
GN OrderedLocusNames=SVEN_4288 {ECO:0000313|EMBL:CCA57574.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA57574.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA57574.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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DR EMBL; FR845719; CCA57574.1; -; Genomic_DNA.
DR RefSeq; WP_015035485.1; NZ_JABVZO010000002.1.
DR AlphaFoldDB; F2RIL8; -.
DR STRING; 953739.SVEN_4288; -.
DR MEROPS; M28.003; -.
DR GeneID; 69866372; -.
DR KEGG; sve:SVEN_4288; -.
DR PATRIC; fig|953739.5.peg.6788; -.
DR eggNOG; COG2234; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_024336_2_0_11; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CCA57574.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCA57574.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..434
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003286429"
FT DOMAIN 317..434
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
SQ SEQUENCE 434 AA; 44837 MW; 052EFD4B4E6D9565 CRC64;
MNISVPRRVT AVAALAALAL AGLTGTGATA APAAAAAAPD IPLANVKQHL ADLQSIATAN
GGNRAHGRTG YKASIDFVKA KLDAAGYTTT VQQFTSSGAT GYNLIADWPG GDPNQVLMAG
SHLDSVSSGP GINDNGSGSA AVLETALAVA RSGYQPTKHL RFGWWGAEEL GLVGSKYYVS
QLPTTERAKL SGYLNFDMIG SPNPGYFVYD DDPTIETTFK NYFAGLGVPT EIETEGDGRS
DHASFKNVGV PVGGLFTGAS RVKSSAQVQK WGGTATAFDR CYHSSCDTTS NINDTALDRN
SDAIAHAIWT LSAGTTTPPG TVFENTADVS IPDNGAAVTS TVNVTGIAGN APSALKVDVN
IVHTYRGDLV VDLVAPDGTA YSLSNRSGGS ADNIVQTFTV NASSEVANGA WKLRVQDKAS
ADTGYINSFK LTFP
//
