ID W8RZQ5_9RHOB Unreviewed; 1270 AA.
AC W8RZQ5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=roselon_00952 {ECO:0000313|EMBL:AHM03352.1};
OS Roseibacterium elongatum DSM 19469.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseibacterium.
OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM03352.1, ECO:0000313|Proteomes:UP000019593};
RN [1] {ECO:0000313|EMBL:AHM03352.1, ECO:0000313|Proteomes:UP000019593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP004372; AHM03352.1; -; Genomic_DNA.
DR RefSeq; WP_025311228.1; NZ_CP004372.1.
DR AlphaFoldDB; W8RZQ5; -.
DR STRING; 1294273.roselon_00952; -.
DR KEGG; red:roselon_00952; -.
DR PATRIC; fig|1294273.3.peg.932; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_009911_0_0_5; -.
DR OrthoDB; 9795675at2; -.
DR Proteomes; UP000019593; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR42884:SF32; EXTRACELLULAR SERINE PROTEASE; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF00353; HemolysinCabind; 9.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF51120; beta-Roll; 5.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 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:UP000019593};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 339..480
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 905..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 39
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1270 AA; 130359 MW; AECF95B4345FCA88 CRC64;
MSYNSNPLYS QQWHFNLIGD IETIWAEYSG DGVLVAVYDD GVEDTHDDLD GNYDYGSELS
YDNGDPNFSG DAHGTSVAGI IAAENNNEGG VGVAWGADLV GVDFLNDAFG SAALRDMSQF
DVINNSWGYS GFYSTFDING GGWASTFAAD MMFAVENGRG GLGSIVVKSA GNSGRNVDHS
SQNDPFSVLH EAIIVGATDA NGFTEDYSSY GVNLLITAPS AAVTTDREGF AGYEAGDYNF
GFNGTSASAP VVSGVAALIL QANPNLGWRD VQQIMAMSAS HTGSAYGSAA AGFEDYSWFA
NGADNWNGGG MSYHNNYGYG MIDAFAAVRM AEVWSEFFPV PQDSSNVVES LSYYTSPAFA
ETISSTQPPV VDTIFVSETM DIEHIYVIVD GSHSWSADLE IVLTAPDGTE FILNDNNGGY
TDRFGNFIEG TAFAGYTFGV TAAMGMDSYG LWTITISDTV NLDDGLYTGF GLEFAGTTPD
NDDVYHFTDD FLSYEAVEGT RGDMTDTNGG TDWLNLAAVT GDVLWDVGLF TGVRFLAVDT
VRWVDFGNDE IENIATGDGD DDIWGNDYGN IVMTGRGNDS VWGSFGDDSV YGGAGNDTLR
GAYDDDMLLG EEGNDTLEGG TGSDTLNGGL GNDELSGESG ADHFIFDGGN DWILDFTAED
LVFIDPAIWG GTIAGLLAGA QTINGDLFLD FGSGNSLTFA GVTNTSELQG KVLFVGETPP
PPVTTPNAIT IDISAAGQAA GLALQDVEGA LSDLVIDAEI QAGQTSTGFT SISVGGGETI
VYAVTGTGLT YGTDAFGTFL TGGTVTNVNV TINGTFVGSF SGTVDAAQLS AAAFAEVGGS
LGALEAFFSA VNWTYNGSFN NDILPEGFLS EDGVPFALNG EDSLNLGGGN DSVFLANGDD
FANGGDGDDS IGGGDGNDTL EGGNGTDTLE GGSGSDTLEA TGGNGNLLRG GAGDDVLIGG
WGSDILQGND GADSFSGGTG ADDLYIDGQD TFFDGGGGYD RLIAVDPGGV NVALSGTNIE
RVIGGTGDDV FDGTGVALGL VISGEGGNDT LTGGSATDQV SGGAGDDVLI GGGGDDFLFG
DGGSDSFEGG AGDDRFFAES IDQSFDGGAG YDRLFLLDNG DFTFALAGTG IERVNSGDGN
DVLDATGVTD AVVLSGAGGN DALTGGSNND VLAGGDGQDT LEGGSGFDSF FGGAGADSFV
FEDGSGVDFL VGWEDGLDLL DFSGHAQVNG LSDLTITDNG VNSRIEFADG DALIVIGYTG
GFDASDFDFV
//
