ID   A0A368MF42_9FLAO        Unreviewed;      1756 AA.
AC   A0A368MF42;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=DUF5011 domain-containing protein {ECO:0000313|EMBL:RCT53697.1};
GN   ORFNames=DUZ96_10870 {ECO:0000313|EMBL:RCT53697.1};
OS   Winogradskyella sp. KYW1333.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=2282123 {ECO:0000313|EMBL:RCT53697.1, ECO:0000313|Proteomes:UP000253188};
RN   [1] {ECO:0000313|EMBL:RCT53697.1, ECO:0000313|Proteomes:UP000253188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KYW1333 {ECO:0000313|EMBL:RCT53697.1,
RC   ECO:0000313|Proteomes:UP000253188};
RA   Yang H.G., Seong C.N.;
RT   "Complete genome sequence of Winogradskyella aestuarii KYW1333 isolated
RT   from seawater.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RCT53697.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QPHL01000017; RCT53697.1; -; Genomic_DNA.
DR   OrthoDB; 9792152at2; -.
DR   Proteomes; UP000253188; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   InterPro; IPR032179; Cry22Aa_Ig-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR045474; GEVED.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR15127; HEAVYWEIGHT, ISOFORM A; 1.
DR   PANTHER; PTHR15127:SF32; HEAVYWEIGHT, ISOFORM A; 1.
DR   Pfam; PF16403; Bact_surface_Ig-like; 4.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF20009; GEVED; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50853; FN3; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000253188};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1756
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017008861"
FT   DOMAIN          646..732
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          886..971
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   1756 AA;  187116 MW;  1D7DA6F16156BE2C CRC64;
     MKVKLLLLVL VMSSSILWSQ SKVFWQQQSF SSSTITKSSH QSLKTYQTFT LNAQALKQVL
     ANAPQRNFSQ NGSNLVLSFP NSEGKLERFA IMEASVMHPD LQARYPNIRS YVGQGVDDAT
     SRIRFSLTPQ GFNGMILSGN GPGTFIEPIA RNSNNYIIFK RQNRVNFNDN FECQVTAQLN
     ASISSDAGMR NADDSILRTY RLAVSTTGEY TQYHGGSVSQ ALAAINTTMT RVNGLFENDF
     NVTMVLIPNN DAIIYTNGNT DPYSNGSYNN QVQNVLTNII GEANYDVGHL FARASDNGNA
     GCIGCVCVNG QKGSAFTSRS TPEGDPFDVD YVAHELGHQF GGNHTFSFRN EGTNAHYEPG
     SGSTIMGYAG ITGSTDVQSV SDPYFHWYTI QQVTNYVKTT SCQINTNTGN SIPTVSAGPN
     FTIPRGTPFV LEGTASDNDI GDILTYCWEQ ADENDASTTF PSTNSTSGVS FRSFNPSTDN
     KRYFPRLSTI KSGATAWQWE AIPNVSRTLN FRLTARDNRA GGATNNSDDT SITVNGSAGP
     FILNSPNTNV TWDAGTTRTV TWDVAGTTGN GINATNVDIF LSTDGGDTYP ITLATGVPND
     GSHDIVVPNN EGNQNRVMVK GANNIFFDIS NTNFTIGPPV VCNATIPTGL VASNVATTTA
     TLSWNAVPGA SYDLRFREVG TSTWTTESVT GISSSLSSLT ALTQYEAQVR STCSGGATSA
     YSGLVNFTTT DVQLNYCDSA STNVNDEYIS RLQLNTIDNS SGAQFYSDFT NISTSLTKGT
     QYSVTITPTW TGTVYSEGYS VWIDYNRDGD FSDAGEQVFT QAPTQATPVS GSFTVPTNAV
     ENSTRMRVTL SYNANVGPCD SFQYGEVEDY TIIIQAAGPD EEAPSSPTDL TASNTTETST
     DLNWTAATDN VGVSDYDVYQ DGVQIANVIG TSVQVTGLSE STTYSFYVIA NDAAGNSSAQ
     SNIVNETTLS APTCSDGIQN GDETGVDCGG SSCAPCATST LNEGFFETGL DGWTDGGSDV
     ARVQTTNSYE GIWSIRIRDN SGTASSMTSP TYDLSDYESV EISFFYYPVS MENGEDFWLQ
     FNDGSGWTTV ATYVSGTDFT NGNFFNDSVT VTNSQFSFGP SAQFRLRCDA SGNNDQVYID
     QVITVGTLSG SDVTPPVITL NGASNLDLNV GDTYTEQGAT ATDNVDGDLT GSIVIGGDVV
     NTSVAGTYLV TYNVSDAAGN VANEVVRTVN VIPDTSAPVI TLNGAATVNL NVGDTYTELG
     ATATDNIDGD ISANIVIGGD VVDGNTAGTY LVTYNVSDDA GNAATEAVRT VNVILDTTAP
     VITLIGASSI SLELGDSFSE PGATATDNVD GDITANIVVG GDTVDSNTAG TYIITYNVSD
     AAGNTATQVT RTVTVNPDTT IPVITLNGSS VIDLIEGDTY TELGATATDN IDGDITANIV
     IGGDVVDTNA VGTYLVTYNV SDAAGNVANE VTRTINVSVA PTCNDGIQNG DETGIDCGGS
     CAPCSPTDVI LNEGYFETGL DSWIDGGSDC ARRLDEVRSF EGQYSIRIRD NSGVASSMTL
     NNIDVSSFST IEVDFYFYVR SMENGEDFWL RFFDGSSWFT VETWTRGVNI NNNTFYNATV
     SITPSQYNFA VNSGFRFQCD ASGNNDQIFI DQVTITGLTI SSRGRKDKLE IVGYGEPEEL
     SEFDISIYPN PVKGNIMNIE VSGVETFGYS IIDIVGKTVL KGKTAGSINV SKLDGGVYFI
     KVNDGDEIIT KKFIKN
//