ID A0A366K810_9BIFI Unreviewed; 796 AA.
AC A0A366K810;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:RBP97804.1};
GN ORFNames=CRD60_04200 {ECO:0000313|EMBL:RBP97804.1};
OS Bifidobacterium aemilianum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2493120 {ECO:0000313|EMBL:RBP97804.1, ECO:0000313|Proteomes:UP000252530};
RN [1] {ECO:0000313|EMBL:RBP97804.1, ECO:0000313|Proteomes:UP000252530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XV10 {ECO:0000313|EMBL:RBP97804.1,
RC ECO:0000313|Proteomes:UP000252530};
RA Alberoni D., Baffoni L., Di Gioia D., Gaggia F., Biavati B.;
RT "Bifidobacterium xylocopum sp. nov. and Bifidobacterium aemilianum sp.
RT nov., from the carpenter bee (Xylocopa violacea) digestive tract.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RBP97804.1}.
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DR EMBL; PDCG01000003; RBP97804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366K810; -.
DR OrthoDB; 3325701at2; -.
DR Proteomes; UP000252530; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000252530}.
FT DOMAIN 221..391
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 561..758
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 765..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 87009 MW; 74D6DF6744FF3E29 CRC64;
MQAIEDFPAR KARTLRFSCG APRSARLIGD GRRALFLRSR GSEDLVTALW MSLVNGPGAD
GEPAHQELLL ADPRELLADA DEERLPDEER ARRERAREGG QGIVSYSVDE AGRKIVFTIN
GQLFLTTIDP DGQGSNTRQL ATDSLGADGS PWLPVINPEI SPDGRMVAYT TGRRLVMVRI
DDREGLDADN AERLAYHDRV CGLADVSDRA DWLPGAGSGA SDSDETWKLG LAEFIAGEEM
DRYAGFWWSP DSRALLFEVF DSSPEPVWYI SDPANPDRPA ASRRYAQALR ANARVYLAEV
RLAFDTQGAY VSRETFPIDW DSEGYEYLAA VSWTGGHRPI ILVQNRTQSK DQVLEILESG
HTRLLEAHVN DHWLDLLPGT PALTPDGRLI CAFNDLEADS NRLTCDGRPC TPAGWQVRSL
LDVADDSLLV TASKDPKTID LLEIPLGCPG QGEETQVRVL NPSPGIWTGS RVGGQLLMTG
RTMESPAPIM THLGHSIASM AAEPGFSPQT RFVELGAHRL QTAITYPSAQ SPYAQAERLP
VLLKPYGGPG HQEVMLSQSH YWDSQWWADQ GFLVVTADGR GTTGRGPAWD RAIHKEMKAV
TLADQVEAVQ ALAEAEPKAD TGRVAMIGWS YGGFLSALAV LEAPDVIHAA CAGAPPTDWS
LYDTHYTERY LGLDPQTYER NSIIRDAPAL RRPLLLIHGF ADDNVSIANS LRLSQALMAA
GRPHSFLPLT GITHMTNDET VARNLLIMQR DFLYQALGME AGGAQSPARA ESDCAAGRRP
LVEGRGSRHQ GALRVS
//