ID F8D4H6_HALXS Unreviewed; 388 AA.
AC F8D4H6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:AEH38723.1};
GN OrderedLocusNames=Halxa_4118 {ECO:0000313|EMBL:AEH38723.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH38723.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH38723.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP002839; AEH38723.1; -; Genomic_DNA.
DR RefSeq; WP_013881609.1; NC_015666.1.
DR AlphaFoldDB; F8D4H6; -.
DR STRING; 797210.Halxa_4118; -.
DR GeneID; 10799060; -.
DR KEGG; hxa:Halxa_4118; -.
DR eggNOG; arCOG02833; Archaea.
DR HOGENOM; CLU_020120_2_2_2; -.
DR OrthoDB; 350578at2157; -.
DR Proteomes; UP000006794; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT DOMAIN 265..349
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 23..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 39577 MW; 00B054314873166A CRC64;
MTPDHVSRRR LLRAAGAASI LGVGTASTAA QNETDDSSDG AEPSDDQGSS APESQYTEVY
RNTIDSVVLV TVSLGPTDGR GGGGGLGSGF VVDDQYIVTN NHVVQGATEG GIEIQFNNQE
WATASIVGTD PYSDIAVLSV ENMPDSAEPL SLVESEPAIG QEVLAIGNPL GLDASVSQGI
VSGTNRVLPS PVGNSIPATI QTDAPINPGN SGGPLVNLEG EVVGVVFAGA SQTIGFAISA
RLANRVVPAL VEDGTYEHSY MGVGVVPVGP EIAETVGLEE ATGVLVAQVV PNSPADGALQ
PASAGQPGSG DVIVAIDGQE VTTQAQLLSY LALETSPGDT IELEVVRDGE RETVELELAA
RQEFDRQQPP IGGQPGGEPG EQPPFPQS
//
