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Database: UniProt
Entry: E1VKX8_9GAMM
LinkDB: E1VKX8_9GAMM
Original site: E1VKX8_9GAMM 
ID   E1VKX8_9GAMM            Unreviewed;       386 AA.
AC   E1VKX8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   ORFNames=HDN1F_18870 {ECO:0000313|EMBL:CBL45470.1};
OS   gamma proteobacterium HdN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL45470.1, ECO:0000313|Proteomes:UP000002677};
RN   [1] {ECO:0000313|EMBL:CBL45470.1, ECO:0000313|Proteomes:UP000002677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA   Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with possible
RT   involvement of the electron acceptor in substrate activation.";
RL   Environ. Microbiol. 0:0-0(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; FP929140; CBL45470.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VKX8; -.
DR   STRING; 83406.HDN1F_18870; -.
DR   KEGG; gpb:HDN1F_18870; -.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_006842_7_4_6; -.
DR   OrthoDB; 9813836at2; -.
DR   Proteomes; UP000002677; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF99; AQUARIUS-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002677};
KW   Serine protease {ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN          47..296
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          310..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  39334 MW;  5F2A4B2826D2606E CRC64;
     MKLSVDIATD NAKRKANRRL KSSLWALTGA LIVASSSAWS FDKSPRIVNG RDASPGQFPW
     QVALLQGDGA PINTFFCGGS IIHPRWILTA AHCRPDSDAA IASVHVLAGT NSLAQADSGQ
     TIAIKRWINH PEYVTEGSTA GIVFDNDIAL IELERDIDMG LCGEKCAAAK LATPSNDGTL
     SMPVQLSGWG DTSETVSSTP ANLQWASLRI VDCSVSPSLI PPAEISTHMM CATVPGNNTD
     ACSGDSGGPL VMPSSSGVGY VQVGLVSFGY GCANQGYPGV YTRVSQYGDW LTQTTGGACC
     NNDGSGGGIV DDGTGGDNGT GGDNGTGGDN GTGGDNGTGD DGGLEQPKKR GSGGGGSLPL
     ATLVVAALAG LARKGTFSGS NTHQTH
//
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