GenomeNet

Database: UniProt
Entry: D3QBZ5_STANL
LinkDB: D3QBZ5_STANL
Original site: D3QBZ5_STANL 
ID   D3QBZ5_STANL            Unreviewed;       467 AA.
AC   D3QBZ5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADD44884.1};
GN   OrderedLocusNames=Snas_5250 {ECO:0000313|EMBL:ADD44884.1};
OS   Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS   NBRC 102104 / LLR-40K-21).
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Stackebrandtia.
OX   NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD44884.1, ECO:0000313|Proteomes:UP000000844};
RN   [1] {ECO:0000313|EMBL:ADD44884.1, ECO:0000313|Proteomes:UP000000844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC   LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX   PubMed=21304662; DOI=10.4056/sigs.47643;
RA   Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT   40K-21).";
RL   Stand. Genomic Sci. 1:292-299(2009).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; CP001778; ADD44884.1; -; Genomic_DNA.
DR   RefSeq; WP_013020455.1; NC_013947.1.
DR   AlphaFoldDB; D3QBZ5; -.
DR   STRING; 446470.Snas_5250; -.
DR   MEROPS; S01.168; -.
DR   KEGG; sna:Snas_5250; -.
DR   eggNOG; COG3291; Bacteria.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_561004_0_0_11; -.
DR   OrthoDB; 5243523at2; -.
DR   Proteomes; UP000000844; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00146; PKD; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00089; PKD; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50093; PKD; 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:UP000000844};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..467
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003049725"
FT   DOMAIN          50..282
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          408..467
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          24..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  48217 MW;  18FCCCBE7CD06B65 CRC64;
     MRIARAVAVV AAATLLLSAP LAGTASADPP KSKAANPTDE LRPDDVGTDI VNGELASYTE
     RPSLITGLRV GGGGPQGSSC TASVVGKRQI LTAAHCMIDV GGAKSYLYGD DDLSSAGDEK
     WKSPVTKFTP HPDYGGSGGW RTGYDVAIVE VADDIPVPES DWAKFATSAD ADLSQPGRDS
     LTYGWGKTAA NGTMGRLKKT TLPINDADSC QVFDVTVNPE LMICAGYDDG RTGICSGDSG
     GPLIVDGVVI GITSWGASAC DRYSIFARLT NAMGDWAHEQ LQAPAEDDFS VSLSPDSATV
     EPGQSTETTV STKVSRGSAQ DVSLTATGLP DGAEATFSPS AIRSGESAKL SVSTSSDTPQ
     GTHRITVTAD GAKVDRTAVF TLQVGEDGEG PTADFTAQCF SGPGVCFFNG QGSKGEIASY
     RWTFGDGGTG QGQLVHHWYA AAGQYRVTLT VTDSRGGSHS TTKTITV
//
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