ID A0A3M8FXT0_9BACT Unreviewed; 613 AA.
AC A0A3M8FXT0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
GN ORFNames=ED559_12225 {ECO:0000313|EMBL:RNC82509.1};
OS Phycisphaera sp.
OC Bacteria; Pseudomonadati; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=2030824 {ECO:0000313|EMBL:RNC82509.1, ECO:0000313|Proteomes:UP000270436};
RN [1] {ECO:0000313|EMBL:RNC82509.1, ECO:0000313|Proteomes:UP000270436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin4 {ECO:0000313|EMBL:RNC82509.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-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:RNC82509.1}.
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DR EMBL; RHLH01000001; RNC82509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8FXT0; -.
DR Proteomes; UP000270436; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:TreeGrafter.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR050958; Cell_Adh-Cytoskel_Orgn.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR053783; Dockerin_dom_GC-type.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR NCBIfam; NF041540; dockerin_GC; 1.
DR NCBIfam; NF038122; metallo_LGF; 1.
DR PANTHER; PTHR45080; CONTACTIN 5; 1.
DR PANTHER; PTHR45080:SF8; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Reference proteome {ECO:0000313|Proteomes:UP000270436};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..613
FT /note="Ig-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018321252"
FT DOMAIN 385..466
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 471..551
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 613 AA; 64388 MW; 1AB8CCCA94148708 CRC64;
MSIKKKVSIA ALVSACAGAA LATEPNVTIS GRDAQTERYA DGSVASLPSE TVWKYMCGSD
TTGLTNEDLI AAMENHEALV AQGVTTIDNT AGRGGINVIF NVSGSIPGGA NGALSLAEAL
IESTFDDPTT IVVSLSFASL GGGVLGATGS NYVSDSWGDS RTGLINGMDG DDSIQSFLPT
GTTIPVRYNA SSTSITNENR VFWTRAAYKS TVGSLGGSDA SMTYNQNFNW DFDPTNGISG
SSFSFVDVVI HEVGHAMGFT SAVDFRNNDI ETIDIYRFQR TDGSNDYNPD TTAEFQTTPR
TVDFNNPNDD ANSDIISNEY RMSDGSPSQA SHFREQGNCS PTSNIGIMDP SFNGGCTFFS
RGYYSDADIN MFDAIGYDFV VGNPPQIVVQ PSPDTVCAGE TAQLSVVASG DAPLSYQWFD
VFLVPVPGAT NSTLTITNAQ ESDEGLYFCT VTNNVGSADS DFVQITVDQA PSITDQPDSQ
TVDEGDNVTF TVAASGTGTL SYQWRKDNSN ISGATSSSYT ITGATPSDDG DYDVVITNSC
GSVTSSDATL TVNPDAGECL ADVNGDGAVT PTDFTAWVNA FNNNLPGCDQ NNDGACTPTD
FTAWVNNFNA GCP
//