ID A0A0H5CTB7_9PSEU Unreviewed; 398 AA.
AC A0A0H5CTB7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Aminopeptidase Y (Arg, Lys, Leu preference) {ECO:0000313|EMBL:CRK61381.1};
DE EC=3.4.11.15 {ECO:0000313|EMBL:CRK61381.1};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK61381.1, 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; CRK61381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5CTB7; -.
DR STRING; 1653480.gene:80950279; -.
DR KEGG; alo:CRK61381; -.
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:CRK61381.1};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005217062"
FT DOMAIN 47..270
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 275..398
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
SQ SEQUENCE 398 AA; 41392 MW; DD1483854E63298D CRC64;
MIERNWVRKL RKTLLVAVGT AAMIGAATGQ ALATPPPSQP GDVSPQVVGG TPAAQGQYPW
MVRLSMGCGG AMYSEQLVLT AAHCVSGTGN NTSITATYGV VDLQSPSRVT RTSSYVYKNP
GYSTSAGGDW ALIKLSSPIT GAATLPIATT AAYDNGTFDI MGWGSATEGG AQQRYLLRAE
VPFVSDATCR ASGGSYANLI DAVEICAGLP QGGIDTCQGD SGGPMVRRDA NNNWIQVGIV
SWGEGCARPN KYGVYAQVSA LSAAIKAKAD ELGGTPPPPP PPGKYFENLN NVNIPDSPGA
AVFSNLAVTG VTGNAPATLK VGVDIKHTWR GDLVIDLVAP DGSTYRLKNS SGNDSADNVI
ATYTVNASTE VANGTWKLQV RDVARYDTGY IDAFNLTF
//
