ID   A0A1V9FHR2_9BACT        Unreviewed;      1767 AA.
AC   A0A1V9FHR2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A4R26_23650 {ECO:0000313|EMBL:OQP57903.1};
OS   Niastella populi.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=550983 {ECO:0000313|EMBL:OQP57903.1, ECO:0000313|Proteomes:UP000192276};
RN   [1] {ECO:0000313|Proteomes:UP000192276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=208 {ECO:0000313|Proteomes:UP000192276};
RA   Chen L., Zhuang W., Wang G.;
RL   Submitted (APR-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:OQP57903.1}.
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DR   EMBL; LWBP01000190; OQP57903.1; -; Genomic_DNA.
DR   STRING; 550983.A4R26_23650; -.
DR   OrthoDB; 9792152at2; -.
DR   Proteomes; UP000192276; 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; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR011635; CARDB.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF07705; CARDB; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192276};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240}.
FT   DOMAIN          229..491
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          846..912
FT                   /note="CARDB"
FT                   /evidence="ECO:0000259|Pfam:PF07705"
FT   DOMAIN          1697..1766
FT                   /note="Secretion system C-terminal sorting"
FT                   /evidence="ECO:0000259|Pfam:PF18962"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        263
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        437
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1767 AA;  190384 MW;  A3B26FF0B9FB10A4 CRC64;
     MKYPLLALSL LVILNGSAQE ILRPVQLKSG SLTKTSNLRN DLHLTDSLVK YRFRNKFYTL
     IQFNQLPDVA ERQALAKEGI VLYDYIPDNT FLAEINDRLS PGQLKRNTIS GVYTLNTKAK
     IAPALKQQLS AHSQDPDKLI AVSFYGSIDK TAVITALKQA GAQIVDTKIQ PAHVVFISAN
     ESDIEEIAAL PFVAYISSQQ MKPVTLNYSN RAAHSINAIA ATAGRNLQGS NVVLGHGDNG
     DVNFHLDLSG RLINRNPAPA AAHGTATMGT MGGGGIINQK IKGMAPRATL ISQYFSDILV
     NTPYYVADYD MVITNNSYHS AANGCAGEGD YDVLSNYVDA QMNNDLSLLH VFASGNDGAL
     TCSPYPGAFA TIKSGFQTGK NVLTVGNVDN LSNYAILNTS SRGPVDDGRL KPEIVAGGSA
     ITSSVPVNGY STLWGTSMSA PAVSGALGLM YERYRQLNGG ANPTAALIKA VACNTADDLG
     NAGPDFTYGF GNLNALNAVE ALENNTYFNG VVNNGGSQNF NISGVPAGTK QIKIMLYWND
     PAGTPYAATT LVNNLNLTVT APDASVHNPL ILDPSVSNVN NVAVEGVDNR NNIEQVVINN
     PPAGNFTVTV SGAAVPQGPQ DFVVAYQVIA PAVQVTYPYG EDTWVPGETE IIRWSATDDN
     TNPFTIEYSI DNGSNWTVIA NNVAANLRTY TFTTPNTPTV SALVRVSRNG TGYTDVSNYT
     FTILALPAVT LTNTCAGYVN LSWAAITGAT SYDVMMYKGN DMSVVANIPG TSYLLGGLNK
     DSIYYFAVRA VMGSTPGRRC VAQSVTPSGG ACASPTFDND LTTSLLVAPA TGRMHTTSQL
     AATAPQVSIK NMGSTAFSGA FDVIYQVNNG TPVTEATSQT IAAGATYTHT FATTYDFSAP
     GTYTIKAWVD ATTDPLHIND TLVTVVKQLA NDPILLTPSF TEGFESAAAN AYTNGTRGFD
     GLDRADFFSH STNGRVRTFV NTGFARTGNR AATLDQIANL GIISTDSLIT TFNLGAYSPT
     DQIWLSFYFR NQGIDFSAGN NRVYIRGSET GAWIPVYTLP TNTADFGVYR AATPVNITET
     LANAVPAQSV SSSFQVKFCE QGYRSANSVI VNGNLDDGYS FDDITLTITT DDVSMMQLVN
     PAPTNVCALT SAEPITVQVK NYSTGTLTSV PVSYQIDNGT VITENIPSIN AGQVLNYTFT
     QTANLATFKE YTIATWVNYA TDSYRVNDTV TNSFRTSPLI SSYPYLESFE SSEGNWYTGG
     LNSSWEWGTP AASVINKAAN GTNAWVTNLT GNHNNNELSY LYSPCFDLSE LTQPVLSFSH
     IFRMEDNCNC DFHWAEYSTD GTNWYKLGTT SGGTNWYDNP LYQAWKISNT RWHVSSFDVP
     VNTSKVRFRI VMYGDPGVTY EGVGIDDIHV FDKAAIYTGA NITGGLAQTV SGNNWIHFNS
     GGNRVASINP HGQNLGNTDV SVYINPTIVR NDGTQYYLDR NIVIRPANAP SGAVSVRFYF
     TNTEVNNMLN ETSCGTCSNL TGAYEAGITK YNGPPAEENG TIADNVSGLL SFITPANVDI
     IPYDNGYYAE YQVTSFSEFW INSGGPGQNQ PLPLVLGLFT VTKNNATALL HWTTLQETNT
     AEFIIERSTD GVHYEIIGSV TAGGNTTTES KYQFTDKQMA AGINYYRIKT VDKDAKYSWS
     PVRSVNNSDN DFTISVLPNP VTKGVVYINT SVNCNRIELR DVTGRLVKTV NVKGTHNPLQ
     VGELKKGMYF VTVITDNGDK VEKIVIQ
//