ID D2RWL9_HALTV Unreviewed; 395 AA.
AC D2RWL9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADB61520.1};
GN OrderedLocusNames=Htur_2644 {ECO:0000313|EMBL:ADB61520.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61520.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB61520.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP001860; ADB61520.1; -; Genomic_DNA.
DR RefSeq; WP_012943792.1; NC_013743.1.
DR AlphaFoldDB; D2RWL9; -.
DR STRING; 543526.Htur_2644; -.
DR GeneID; 8743257; -.
DR KEGG; htu:Htur_2644; -.
DR eggNOG; arCOG02833; Archaea.
DR HOGENOM; CLU_020120_2_2_2; -.
DR Proteomes; UP000001903; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
FT DOMAIN 276..349
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 41..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 39874 MW; BE39CAEF875DB894 CRC64;
MPLVGVTMGV TPDPDQCTRR RILGAVGAAG AAAAIGLGGT GGGSAQNETN GSNATVGQDD
GPAVDSPYTE TYRNTIDSVV LVTVSGTGGL EGGGGGLGTG FVVDDQHVVT NNHVVQNASE
GGIEIQFNNQ EWRTASVVGT DGYSDLAVLR VDDMPDIAAG LSLSESEPVI GQEVLAIGNP
LGFDASVSQG IVSGIDRSLP SPTGFSIPAA IQTDAPINPG NSGGPLVSLE GEVLGVVFAG
AGQTIGFAIS ARLANRVVPA LIEDGTYEHP YMGVGVLPVG PEIADEIGLE EANGVLVAEV
VPNSPADGVL QSANRVRPGS GDVIVAINGT EIPNQDQLSA YLALETSPGD TIELEIVRDG
EQQTVELTLE ERPGIERPGT RVPGGPGERP PAAGP
//
