ID A5ZX66_9FIRM Unreviewed; 490 AA.
AC A5ZX66;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:EDM85824.1};
GN ORFNames=RUMOBE_03618 {ECO:0000313|EMBL:EDM85824.1};
OS Blautia obeum ATCC 29174.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=411459 {ECO:0000313|EMBL:EDM85824.1, ECO:0000313|Proteomes:UP000006002};
RN [1] {ECO:0000313|EMBL:EDM85824.1, ECO:0000313|Proteomes:UP000006002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM85824.1,
RC ECO:0000313|Proteomes:UP000006002};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM85824.1, ECO:0000313|Proteomes:UP000006002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM85824.1,
RC ECO:0000313|Proteomes:UP000006002};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus obeum (ATCC 29174).";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:EDM85824.1}.
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DR EMBL; AAVO02000023; EDM85824.1; -; Genomic_DNA.
DR RefSeq; WP_005422735.1; NZ_DS264302.1.
DR AlphaFoldDB; A5ZX66; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_1_9; -.
DR Proteomes; UP000006002; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 384..473
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 51414 MW; 7521EDF33807E037 CRC64;
MIEKKWNLNA PQNDTENNRQ NEPPRYEHYC MHQNTESDTV KELPEKKKNK KRGGKKLAET
ISLAVVFGLV AGVVFQGVNF ASEKYLGSDG KDSQIETAQL AGDSSADGSD SNESEGAASS
ETAASETAAA VSQTGSVAEV ADTAMPTVVA ITSVSVQEIP NYFRAFGFGY GTQQYSSEGS
GSGIIVGEND DELLIATNNH VVSGATTLSV CFVGNDVVNA EEETVDMSGS DGDVNVEDAV
SAKIKGTDES NDLAVVAVQK SDIPEDTLSQ IKIAQLGNSD DLQVGEQVVA IGNALGYGQS
VTSGWISALN RNISTDDGTS SSLIQTDAAI NPGNSGGALL NMQGEVIGIN SAKYADSAVE
GMGYAIPISK AQPILEELMN RQTRDKVESE NAAYLGVVTA DLSTEAIQMY DMPEGAFVIR
VEKNSAAGKA GIQKGDIIVS FDGQTVSGKD DLESKLAYYA SGETVDVVVS RADNGEYVQK
TISVTLGSKN
//