ID A0A0C1IZN6_9RHOB Unreviewed; 272 AA.
AC A0A0C1IZN6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=RA27_16050 {ECO:0000313|EMBL:KIC40313.1};
OS Ruegeria sp. ANG-R.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC40313.1, ECO:0000313|Proteomes:UP000031318};
RN [1] {ECO:0000313|Proteomes:UP000031318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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:KIC40313.1}.
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DR EMBL; JWLJ01000006; KIC40313.1; -; Genomic_DNA.
DR RefSeq; WP_039541138.1; NZ_JWLJ01000006.1.
DR AlphaFoldDB; A0A0C1IZN6; -.
DR STRING; 1577903.RA27_16050; -.
DR OrthoDB; 267336at2; -.
DR Proteomes; UP000031318; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR15462; SERINE PROTEASE; 1.
DR PANTHER; PTHR15462:SF8; SERINE PROTEASE; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|RuleBase:RU004296};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU004296}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT CHAIN 22..272
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5006986308"
FT DOMAIN 39..239
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|SMART:SM00020"
SQ SEQUENCE 272 AA; 29139 MW; AAA8F0B21C367DD6 CRC64;
MTRIFLCVVL FFSVLASSLQ AQNSGKRRLT DRDDLYGWEA VGRLDIGNQG FCTGTLIAQD
TVLTAAHCAL DKKTGKPYAP GEVTFRAGLS DGEALADRKV IQIAVHPDFV ANAPVSIPRI
RIDVALMRLE EPIPYSIADP FALHNGRVPD GEISVASYGR GRADAITRQR SCRILQRAEG
IISFNCDVTF GSSGSAILAR SGPRWQILSV TSAMSTDGRY KVGYGMELAG IVAELKAILR
RDAPRPVATI RRLQPGSAKS GSGAKFISSG GS
//
