ID A0A1F8EJ17_9BACT Unreviewed; 650 AA.
AC A0A1F8EJ17;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=A2650_01700 {ECO:0000313|EMBL:OGN00618.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_41_53.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802663 {ECO:0000313|EMBL:OGN00618.1, ECO:0000313|Proteomes:UP000177117};
RN [1] {ECO:0000313|EMBL:OGN00618.1, ECO:0000313|Proteomes:UP000177117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGN00618.1}.
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DR EMBL; MGJD01000018; OGN00618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8EJ17; -.
DR Proteomes; UP000177117; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Serine protease {ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 650 AA; 73695 MW; 638BBBD9230AA7CE CRC64;
MIKQASRILV FAVTILVGTN LIFADEGMWL LSNLPLNELR QKYNFVPSDQ WTEQVQKSSA
RLPNCSASLV SSDGLIMTNG HCAQEAVQAL STPQNNLYEN GFYARTLLAE KKTSLNLKVL
ISVEDRGVQK QGLVCEEVIL YQGGQYNNYC YKVYDDIRLV FSSEKNTWFF GGDADNFEYP
RFAMDVAFLR AYENDKPAQT SNHFKWSKSG ASEDELIFVS GHPGSTERML TSAALETERD
IKAPFILDLI RRREITTQQF MLRGKEQTRI AKSDLFSWQN GRKLYTGKIR GLQDLDLTDS
KKIYEKKVTD DAKNKPHLTK KLEDGRLMVA DAQTAIREIY SKVVLLLARH GFDSRLFKYA
QSLVSGNQQF AESVLEERNN EPPLNLEYEE AKLRDSLTHF TEVFGVNNLA TQDLLMRYHE
RPSDVASLLI SSTRLADFNE HKLIVQEFIK SGSLPFGNGD LIVGLVRDIQ VKHAPQYEKA
WHDALEKERQ GYAKISEVLF ELYGTDIYPD ATFTLRLSFG TVSGYEENGR QIAPFTTIGQ
AFAHSAEFDN TGDHQLPLSW YKARRLLRSA TPLNFTSNLD ITGGNSGSPV FNKELEIVGL
VFDGNIHSLV SDYDYNYSPK SRAISVHSSG ILEMLQKVYK ADRLVKELTR
//
