ID A0A0H5CIC5_9PSEU Unreviewed; 403 AA.
AC A0A0H5CIC5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Aminopeptidase Y (Arg, Lys, Leu preference) {ECO:0000313|EMBL:CRK57466.1};
DE EC=3.4.11.15 {ECO:0000313|EMBL:CRK57466.1};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK57466.1, 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 S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; LN850107; CRK57466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5CIC5; -.
DR STRING; 1653480.gene:80946330; -.
DR KEGG; alo:CRK57466; -.
DR Proteomes; UP000076116; Chromosome i.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CRK57466.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000076116};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005216828"
FT DOMAIN 45..265
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 278..403
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 41564 MW; 9640E9A8B9DE0D2E CRC64;
MIKLSKLQKA MMLAATTVAA AATVAGQALA SQPPASQPGD VSPQIVGGTP AALGDYPWMV
RLSMGCGGAM YSEQLVLTAA HCVSSTGNNT SITATYGVVD LQSSSAVKRT SSYVYKNPGY
STSTGGDWAL IKLSSPIAGA ATLPIATTSA FDNGTFDIMG WGAASEGGSQ QRYMLKAKVP
FVSDATCKSA YANLKPATEL CAGLPEGGID TCQGDSGGPM VRRDNNNNWI QVGIVSWGEG
CARPNKYGVY GEVSALSAAI KAKATELGGG TTTTPTTTPP TTTTAPPSRV FENTNNVNIP
DSPAAAVTSD VAVSGISGNA PSTLKVDVDI KHTWRGDVVI DLIAPDGSAY RLKNSSSNDS
ADNVIATYTV NASTEVANGT WKLKVQDIAR YDTGYIDSVK LTF
//
