ID A0A2G5L1S2_9BACT Unreviewed; 1382 AA.
AC A0A2G5L1S2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=BFP72_09225 {ECO:0000313|EMBL:PIB35559.1};
OS Reichenbachiella sp. 5M10.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Reichenbachiellaceae;
OC Reichenbachiella.
OX NCBI_TaxID=1889772 {ECO:0000313|EMBL:PIB35559.1, ECO:0000313|Proteomes:UP000229466};
RN [1] {ECO:0000313|EMBL:PIB35559.1, ECO:0000313|Proteomes:UP000229466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5M10 {ECO:0000313|EMBL:PIB35559.1,
RC ECO:0000313|Proteomes:UP000229466};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Reichenbachiella sp. strain 5M10.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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:PIB35559.1}.
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DR EMBL; MDGR01000007; PIB35559.1; -; Genomic_DNA.
DR Proteomes; UP000229466; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR044023; Ig_7.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF19081; Ig_7; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF00801; PKD; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49299; PKD domain; 2.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50093; PKD; 2.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000229466};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 916..964
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1245..1283
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1382 AA; 152870 MW; 1AA75C6600E2FF03 CRC64;
MLDLLGQQKV VYVKIKEAAV AQGRIRNILS MDQLNNHEMV HSLVSLQVQS KIVTQARVTS
TPKSKYLDGI YRLSVSQDGA EEFVQELQSY SNVVAVELEP QFEVLLVPND EWIANQDYLQ
LIEAYEAWDI TRGDEEIIIG VSDTGFDFEH EDMVDRAYVN SFDPINGVDD DGNGYIDDNR
GWDFGDEDND ASYASNESVS HGAHVAGIVS ATPNNSIGIA GVSYSSPYLP IKVAQSSNGE
FHNAYESIIY AADMGCAVIN LSWGGVFGYS EIAQSVINYA VLERNMAVVA AAGNTDAELD
FYPASYDHVL SVGKSNAKDE KASNATWSYQ IDLMAPGQAV LSTNIKDGYL SESGSSFSAP
QVASTVALVK SVFPELNAIE LMERVRMTAD DIYAVGSNSQ YWGQLGKGRL NVLRAVSEVQ
VASIRSFGMQ YHSKFDGSIF AGDTVDVSLG FVNVLREVSG AGVEIVSESP YAEVVNPELV
LGSMYSFDSI NDVSVKVWVS PDAPADTRLS FRMNYFDAAG YEDFEYFHLY TAPPYVTIDN
GQISQTIGAN ANLGYSEDVF QGGHGLNHNG VRVAYEMGIA IGNARDTLSN NITNSWVSHT
RDQDFESIEN IRPYESTEVD RYARGSFVDT GAETVQGLRI EQEFMLWTDE QQDGYMIQEY
RVTNTLDKMR PGMSMGLYVD FGVGAVEDNF SEWNEEKKLG YCYSLVDGTL MTGVALLTGQ
PSVFRAIDLY DSEGEALDIT EGFSDSLKYA YMINPKWTAG GTNGNDVAQL LTAQMGDLAP
YSSQKVAFVT VFGYSLDELM ANVEKAQVQY DAFLEQPQVS WIEQTCTGVP VSLENEKVLH
IYSDSNGMDL VNSGVGLMLT GLDRDSMFYY TVQETGYTSD LYAMQVEVAD PKVQFRSEPQ
EFYLGDTEQN KVQFVDETLS ASSWSWDFGN GFYSAAKNPF TPFNTVGEYA VNLSIVTSQG
CAASGARVFK VGERGEMPNV KDQMVCAGQS ARITASNSES LRVYAHENDE VPVGEGSEWS
TPMLDETTVY YVSSIETTNE SVRVPVTIVV DPVQAAFEYS PDTTDWSGSE MIHLQDVSTG
AEFYQWQIDG EDWGQQSVLV IDVSTKNQME VVLEAKSSTG CTSVVSQRVE FATSTQPGIN
QNTRRTVCKG TRVFSQPLHG EYFVFYSDAS LTHIVAKGSE AWLGPIESDT SFFITNVSDY
HESNAVELEL KRVVFDPVWS VMPEVMVLEQ QSTAIFKVSS ETKVVSYRWS IDDAVVGVSD
QLVYTFFEEG EYLVAVSVSS ELGCVDTLRR QYQVKTHDVL GLVDGKGFVI YPNPASDWLY
LDAQLGDVNC FELFDVFGKK WDVSMNKDGK QWVVDVRTFR PGLYVYQFQI KGQEYRGLLS
IN
//
