ID A0A1Q3SMB3_9CHLR Unreviewed; 1460 AA.
AC A0A1Q3SMB3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=BGO39_19605 {ECO:0000313|EMBL:OJV90617.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV90617.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJV90617.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJV90617.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the intimin/invasin family.
CC {ECO:0000256|ARBA:ARBA00010116}.
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:OJV90617.1}.
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DR EMBL; MKTJ01000070; OJV90617.1; -; Genomic_DNA.
DR STRING; 1895928.BGO39_19605; -.
DR Proteomes; UP000186384; 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 CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003344; Big_1_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SMART; SM00634; BID_1; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1460
FT /note="P/Homo B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012727374"
FT DOMAIN 965..1118
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 350
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 395
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 633
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1460 AA; 149953 MW; 7B11D3167151D698 CRC64;
MPKSSVNPPI FILLLFVFCF NSLPIPAQAQ NYLPATPNQP APAPAGLPAA QTTIPPGLNF
APGYNKVTID ATDKAALTAA AKNGGYQLAD YGSFSLWKIP AAPAMAAITR NNAVEAHPEF
DQIELRSGKV GTTQPNVKEA RTGGAQLWLV QFVGPIKTEW LETLRKAGIT PVTYMPNNAY
AVWADGSQLD QVNSLVATGN SVIQWAGNYK PEYRLAPSLQ NLKSAIAAKP VTVTVQFYTT
PSVQDSLNRL TALGGKVIEA PSQVLDFTDI TLEMPSSAVA GLSAWPDVFN VEPWVAPHLR
DEAQGQIVAG NITTTVTNTV VPASPGYLSW LTSKGFSSTP TDYPLVDVTD DGIDNGTNQP
LHPDFYELGS KNNPDRLIYN QNCTADPMAD GQAGHGNLNA GIVGGYNNTS GSPYEDANGY
QYGLGISPFG RLGGTKIFNN AGYYDLSGCG NSINGIVAAS YNAGARITSN SWGADVAGAY
NADAQAYDAR TRDASTTLAG NQQMFHIFSA GNAGSGSATV GSPGTAKNVL TVGATENVRD
DGILDGCNYT GANNADDMAT FSSRGPTSDS RTKPDIVAPG THIQGPASQD PTFDGTGVCG
GRNNGADLKA RYYPNFAQNG ITQTLYTWSS GTSHSAPALA GAASLVYNYY QRVLDPGQAP
SPAMLKGLLI NGTRYLNGSD TGDTLPSNNQ GWGGVDLKNS FDSSNHYCQL INQSVVLTGT
GQAYSTTCQV TDPSKPVRVT LVWTDAPGPT TGSSYVNNLD LQVSLNGQTY KGNVFNGAYS
TTGGSFDTRN NVENIFLPPG TSGLMGVKVT AANLAADAIN GGPGPQQDFA LVISNADPGP
AGGSAVLAVT GTAISDLPPG GNANGVLEPG ETIKLTPQLA NNGNGPASGV TANLTTVSPD
ITIITGTTTY PTVPANGTAA PDSPFSFSVS PSLACGQPVT FTLQINYGSS SLTSVLTYMA
GIPTLGASTT YTSTDVNLPM TIPDNNPVGI TSTLPITTSG TVGKVVAKVS VNHTWDGDVT
LQLTSPQGTP VTLVARRGGS GDNFFGTLFD DDATTPISQG FAPFTGSYRP ETPLSAVNDQ
PISGTWTLLA TDSALLDTGT LTGWSLAISP RIYVCGAPTP QPAASLQVNG YPSPVTLGSS
NPFTVTAKDS NGNLAANYTG TVTFATNAAS ASLPSSYTFQ PGDYGQHVFS ASFNVTGTYS
ITATDSVNSS ITGAQGGIMV QGLPAVISAT NSTGQSAELN QPFSSHLTAL VTDSGSDPLS
GIVVTFTAPA SGPSAVFFNS SNTITATTNS SGIADSGPVY ANGVAGSYTV TATVAGVGSP
ASYSLTNTNT CNTYVVTSPT DDGQGTTCGT LSRAITSANS LYKLNSVSLI VITFNLSGSS
TISVTGQLPA IQTGVRLDGG NCTNGPVITI DGTGNGGDGI TLAGGNLYNL RVANFGGRQI
VAGSGGGELR CVRAEKSYSP
//