ID A0A0P0CYX6_9BACT Unreviewed; 766 AA.
AC A0A0P0CYX6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=DC20_13100 {ECO:0000313|EMBL:ALI99737.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI99737.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALI99737.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALI99737.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP012643; ALI99737.1; -; Genomic_DNA.
DR RefSeq; WP_062544242.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0P0CYX6; -.
DR STRING; 512763.DC20_13100; -.
DR KEGG; rti:DC20_13100; -.
DR PATRIC; fig|512763.3.peg.2876; -.
DR Proteomes; UP000061382; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000061382};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 23..766
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023000074"
FT REGION 742..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 86487 MW; A1AE4446A374A102 CRC64;
MLKKIYSLLL VGCLGLSMTA QADEGMWLPL LVKRLNHVDM QKQGLQLTAE EIYNVNNASL
KDAIVQFGGF CTGEFVSKEG LLLTNHHCGY DAIASNSTPQ DDILKNGWWA MTRQQEKKNE
GLFVDILVRM EDVTSQVLQG ITPQTPEQER SRLVAERSKS IADAAKNNGQ YVSYVRDFFN
GNEFYMFVYE RFSDVRLVGT PPESIGKFGG DTDNWMWPRH TGDFSVFRVY MSPDGKPATY
SEKNVPYRPK HHLPISMSPV KEGDFSMVFG FPGRTTRFMA GSGLGMAVDQ SNPARIKLRE
RRLALMKEAM DASPADRLKL ASNYASISNY YKYFIGQNEG IKRMKTLDKK SAEEKAFQDW
ANAERKALYG SALADINASY AGQRTYNLSS IYRSEAALAP QLIAHAYQYT PLYNMLKAGN
VDKAKLQELT TAYKDMNKEF YASYVPSSDQ KIFAELMQMY YNDVPKAQHA DIFKDLTSTY
KGDFRKWAAD VYSKSLLSSE AKANAFLANP TQKALETDPA FKFMRAVQTN YQDNILPKLN
EYNAALGRAN RLYVAGLREM HPNKVFYPDA NSTLRLSYGT VKDYEPRDGV QYKYYTTLQG
IAEKEDPTNP EFIVPAKLMQ LYNQKDYGRY GQNGELRVGF ITNNDITGGN SGSPVINGRG
ELMGLAFDGN WEAMTGDLVF DPEYKRCINV DIKYVLFVMD KLGGAGHLVN EMTLVDNGNP
NTTFNPAIND IKMQGKMEIE TPEGQIKIKK KKNETKIKKE TKKQKS
//
