ID   A4J2Q5_DESRM            Unreviewed;       482 AA.
AC   A4J2Q5;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Ig domain protein, group 2 domain protein {ECO:0000313|EMBL:ABO49358.1};
GN   OrderedLocusNames=Dred_0820 {ECO:0000313|EMBL:ABO49358.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49358.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO49358.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO49358.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000612; ABO49358.1; -; Genomic_DNA.
DR   RefSeq; WP_011877193.1; NC_009253.1.
DR   AlphaFoldDB; A4J2Q5; -.
DR   STRING; 349161.Dred_0820; -.
DR   KEGG; drm:Dred_0820; -.
DR   eggNOG; COG3291; Bacteria.
DR   HOGENOM; CLU_565885_0_0_9; -.
DR   OrthoDB; 1735970at2; -.
DR   Proteomes; UP000001556; Chromosome.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   Pfam; PF02368; Big_2; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..482
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002670673"
FT   DOMAIN          188..270
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|SMART:SM00635"
FT   REGION          273..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  54145 MW;  B70C4A174A99C229 CRC64;
     MKRFITLLSL VFFTFFIVNT AFAGLLEDTL QQLHYENPRV IHGKTLYARL AEGTDRPRVV
     YGTPNDVSGV NPPQSLKNGQ YRYLGYAYDG EPFTNSNFPN DDLKTNYDQR NWISEPWNNG
     LCNNQWNEDF SEDVWNSIFA ALPPSLHDRD KVKILVPPTP TTMGSVRAWH QRPDGIWYET
     FNSIQYLGPA SLEVVPDEAT VKVGGTHQYH AILHYSDPNM KPQDVTNTAE WSTNVPEISK
     VNKGLATGLA KGTATITAKH SGLTDRALFR VINDSEPEPP SPEKPEPPKQ GEEGNLYVLS
     IELLDANGSP FYGTLTAGQN YKVKATYKSK FDISGWARLG MFYKTSSDVR KVGDYVHVQM
     SPGDTTEKTW EFNAAPGNGS LIATIQLDWR SGEAFNPLQF EGKTETTYDD NKMSLSLGGS
     DSPTGPPSTR VYERTGYYHP VRTVAVPVYR KEYETIIEYV KVPFVPAKYK VKTILIPHKD
     DE
//