ID A6LG06_PARD8 Unreviewed; 389 AA.
AC A6LG06;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
GN OrderedLocusNames=BDI_2912 {ECO:0000313|EMBL:ABR44620.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR44620.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR44620.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|PIRNR:PIRNR005700}.
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DR EMBL; CP000140; ABR44620.1; -; Genomic_DNA.
DR RefSeq; WP_005860557.1; NZ_LR215978.1.
DR AlphaFoldDB; A6LG06; -.
DR STRING; 435591.BDI_2912; -.
DR MEROPS; C01.171; -.
DR PaxDb; 435591-BDI_2912; -.
DR DNASU; 5308061; -.
DR KEGG; pdi:BDI_2912; -.
DR eggNOG; COG3579; Bacteria.
DR HOGENOM; CLU_056707_1_0_10; -.
DR BioCyc; PDIS435591:G1G5A-2988-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0070005; F:cysteine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR004134; Peptidase_C1B.
DR PANTHER; PTHR10363; BLEOMYCIN HYDROLASE; 1.
DR PANTHER; PTHR10363:SF2; BLEOMYCIN HYDROLASE; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF03051; Peptidase_C1_2; 1.
DR PIRSF; PIRSF005700; PepC; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700,
KW ECO:0000313|EMBL:ABR44620.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005700};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005700};
KW Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..389
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002695535"
FT DOMAIN 31..129
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00112"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 324
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 345
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 389 AA; 44617 MW; D7A2093C26367D42 CRC64;
MRTFILSCAL ALGSLSTFAQ GYQFTDVVKV PATPVKNQAS TGTCWCFATT SFMESELLRM
GKGTYDLSEM FIVRQKYMNQ LQDNYVRQGR GNIGQGSLSH TFMNAFNQVG IVPEEVYSGI
NYDSDRHNHA EMVKYIKAIA TTAVDMKKRS PEYYKLIDNL FDTYLGKLPE KFTYQGKEYT
PKTFAASLGL NMDDYIELTS FTHHPYYQKF EVEVPDNWEH AQMYNLPLNE MMEVADYALN
NGYTVCWDGD VSEKGFSFKN GVAINPEVKK VEDYSTTDRA RFEKMDEKER LEEVYKFEKP
FPEVNVTPQV RQEGFEAFVT TDDHLMHLTG IAKDQNGTKY YITKNSWGTE RNTFGGYLNM
SDSFVRAKTI YIMVHKDAIP KAIKSKLGI
//
