ID A0A0A2DZF2_9PORP Unreviewed; 940 AA.
AC A0A0A2DZF2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN ORFNames=JT26_00030 {ECO:0000313|EMBL:KGN71941.1};
OS Porphyromonas sp. COT-108 OH1349.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1537504 {ECO:0000313|EMBL:KGN71941.1, ECO:0000313|Proteomes:UP000030126};
RN [1] {ECO:0000313|EMBL:KGN71941.1, ECO:0000313|Proteomes:UP000030126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-108 OH1349 {ECO:0000313|Proteomes:UP000030126};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-108_OH1349 Genome sequencing.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
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:KGN71941.1}.
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DR EMBL; JRAH01000002; KGN71941.1; -; Genomic_DNA.
DR RefSeq; WP_036844383.1; NZ_JRAH01000002.1.
DR AlphaFoldDB; A0A0A2DZF2; -.
DR OrthoDB; 1489355at2; -.
DR Proteomes; UP000030126; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003961; FN3_dom.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR032304; Peptidase_S8_N.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR026444; Secre_tail.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16361; Peptidase_S8_N; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000030126};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 556..671
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 486
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 940 AA; 101056 MW; F5D5B0B0F2DBCF35 CRC64;
MKKVYLLSVL FGLLTVGGCQ NEREVQYADN SQQKEQPNTS SSSLKMYNVP PGAAVPGEII
IKITDEVEQS LTQAQLGEVQ MSSVPSSMGS ALQSIKATAI TRLFPPAGEF EERSRKEGLH
LWFIVRFDKG VEISRAMQAL DSVDGVEIVE FNPIIVPASA NQHPAAINLL SSTEDYLKRN
AKMPFNDPLL KEQWHYNNIG TGVPAGVMGS DINLFKAWEI STGTPNVIVC VVDGGVDVDH
PDLADNMWVN QAEQNGTSGV DDDNNGFVDD INGYCFVTDQ GNLRPDEDAH GTHVAGTIAA
KNNNGVGVAG VAGGNGDPNT GVRIMSAAIF REGAQGGNAA AAIKYGADNG AVISQNSWGY
PYRSGIYTTP NSLKVAIDYF VKYAGTDGKG SQRPDSPMKG GVVLFAAGND GLEFTSQPAA
YEGCIAVSAI GTNFKRATYS NYGDWVDISA PGGDQMLYGT KAGVLSTTDK NAANVADWYT
YYQGTSMACP HASGVAALIV SHFGGPGFTS EDLKTRLLAS ILPVDIDKIN PGAAGRLGSG
YVDAYAALTL KNDQKAPESP KFNSSKINAN VDFTELTLFW NVPKDEDDGT ADKYAVYMST
TPLNANNYKK EGELISNPLV GGKGLSVNDE VSFVVKKLTP DKEYHFALVA IDRWNLFSAP
SFISVKTKKN NPPVISNVPE NPLVLLNILG KVEYEFNISD PDGHKWQYTL EDKTNCVSVA
RIDKGLKVTI RPLSSAGEYS FNLKLTDELK SSFTYTIPFR IVTVTEPEFK KAFPTPTIGA
KGEGASLNLA DYVTPQEFLT FTYKASSSNG SVASADVDDK GKLTIKGYKP GRTTISVEVS
NGHMSSMASF SVTVVEDPSL DVYSVWPLPM QKELNVWLNP THKKAHITLI SITGAVVLDK
EVPADHTGVA KINTSKVAPG TYTLKVKTGG KPYERAVQKR
//
