ID H1LHD1_9LACO Unreviewed; 417 AA.
AC H1LHD1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Serine protease do-like protein {ECO:0000313|EMBL:EHO50483.1};
GN ORFNames=HMPREF9104_02021 {ECO:0000313|EMBL:EHO50483.1};
OS Lentilactobacillus kisonensis F0435.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797516 {ECO:0000313|EMBL:EHO50483.1, ECO:0000313|Proteomes:UP000005025};
RN [1] {ECO:0000313|EMBL:EHO50483.1, ECO:0000313|Proteomes:UP000005025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0435 {ECO:0000313|EMBL:EHO50483.1,
RC ECO:0000313|Proteomes:UP000005025};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:EHO50483.1}.
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DR EMBL; AGRJ01000175; EHO50483.1; -; Genomic_DNA.
DR RefSeq; WP_008857177.1; NZ_JH591047.1.
DR AlphaFoldDB; H1LHD1; -.
DR STRING; 797516.HMPREF9104_02021; -.
DR PATRIC; fig|797516.3.peg.1807; -.
DR HOGENOM; CLU_020120_0_2_9; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000005025; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EHO50483.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 306..394
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 43340 MW; 987BA83A94D6B387 CRC64;
MAEKNGFGKI IATAVIAGAL GGGITYGGIS YFDNSNNTTG TEMISGSNKN GNAKVSNMKV
NLSTQAEQAF NATKSTVVSV INLQRQSESD NPLAGILGGD TSSSKSKKSG ELEASSEGSG
VIYKKSGNTA YIVTNNHVVS GANALEIILS DGSKVSAKVV GKDAVTDLAV IKIDSSKVNK
VATFGDSDNI KVAEPVLAIG SPLGSQYATS VTQGIISAKK REVPQTSESG QQIGNATVIQ
TDAAINPGNS GGPLINLAGQ VVGINSMKLA SDQQGTSVEG MGFAIPSNEV VTIINQLIKH
GQVVRPALGI GYTDLSNVSE EQQRSILKLP KSVTQGAVVL QVNANSPAKR AGIAKYDVIT
NLDGQNITEQ SQLRDILYKH KIGDRVSVTY YHKGEKKTGT ITLNQKATNK VLSEASK
//
