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Database: UniProt
Entry: J9BSJ8_BACCE
LinkDB: J9BSJ8_BACCE
Original site: J9BSJ8_BACCE 
ID   J9BSJ8_BACCE            Unreviewed;       749 AA.
AC   J9BSJ8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IG3_05144 {ECO:0000313|EMBL:EJV76895.1};
OS   Bacillus cereus HuA2-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053201 {ECO:0000313|EMBL:EJV76895.1, ECO:0000313|Proteomes:UP000004136};
RN   [1] {ECO:0000313|EMBL:EJV76895.1, ECO:0000313|Proteomes:UP000004136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HuA2-1 {ECO:0000313|EMBL:EJV76895.1,
RC   ECO:0000313|Proteomes:UP000004136};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus HuA2-1.";
RL   Submitted (APR-2012) 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:EJV76895.1}.
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DR   EMBL; AHDV01000039; EJV76895.1; -; Genomic_DNA.
DR   RefSeq; WP_002203964.1; NZ_JH804674.1.
DR   AlphaFoldDB; J9BSJ8; -.
DR   PATRIC; fig|1053201.3.peg.5264; -.
DR   HOGENOM; CLU_011571_1_0_9; -.
DR   OrthoDB; 9795222at2; -.
DR   Proteomes; UP000004136; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.120.1250; Peptidase M60, enhancin-like domain 1; 1.
DR   Gene3D; 3.40.390.80; Peptidase M60, enhancin-like domain 2; 1.
DR   Gene3D; 1.10.390.30; Peptidase M60, enhancin-like domain 3; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035423; M60-like_N.
DR   InterPro; IPR004954; Mucin-bd.
DR   InterPro; IPR042279; Pep_M60_3.
DR   InterPro; IPR031161; Peptidase_M60_dom.
DR   PANTHER; PTHR15730; EXPERIMENTAL AUTOIMMUNE PROSTATITIS ANTIGEN 2-RELATED; 1.
DR   PANTHER; PTHR15730:SF5; TRPM8 CHANNEL-ASSOCIATED FACTOR HOMOLOG-RELATED; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF17291; M60-like_N; 1.
DR   Pfam; PF03272; Mucin_bdg; 1.
DR   Pfam; PF13402; Peptidase_M60; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM01276; M60-like; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51723; PEPTIDASE_M60; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..749
FT                   /note="Fibronectin type-III domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003822289"
FT   DOMAIN          82..377
FT                   /note="Peptidase M60"
FT                   /evidence="ECO:0000259|PROSITE:PS51723"
FT   DOMAIN          607..695
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   749 AA;  85065 MW;  F719CC9E423AD4E5 CRC64;
     MKRGQKQKTK NLVMITATLS MFATGITPSL EVFAEEQAQQ KKVSTTLQNE NSVNVENRVF
     AVPGKGDVSQ LQNIERRERN FSAYEPTGLY AKPNEQITIQ VQGNQSIQAY IGTFSFDASW
     REDSKIKSFT LNPGTNTIQS PNGGMIYFYN KQQGGTIQTT VITGGTATPL FELGKHTKQD
     LINMLNQYPN AHAVELKGER VLITASPVRV KKYLIDSNTD PVQLLKKMDE ATRIQDKISG
     LSEEQVDKHY LHYVEDNHSL DYYMYAYPHR TAYVGDAIQH VLDINKFTND GWGPWHEAGH
     MRQQTPWNFK NMTEVQVNLY SLAVEKAFTS NQPFRLQQEG AYTKAFQYLE QPNKNYDDIS
     DLFVKVVMLW QLQLAYGEDF YPKLHQLYRD MPSNEIPQTD ETKKQLFMIS ASKAAKQNLI
     PFFEKWGLRP NNDTIQKVAA LGYPNLTAEI WKSTDSNPVK PDTPNFSNIL EGNQFAWSMK
     GIGDFEFVKV NLNKSTEEMQ INLKAGVPHN YFDSTYASIK VQNTSGKVVY NKEIYGNKQQ
     NAEQAKVPVK VGDFIEFTHL EGANRANITN MEKNMQESFG YKAVYEITKE GLKKVDSIVN
     PKPDTEAPTQ PQGLYASNVT SNSVELKWNP STDNVGVKEY QVLRDGQLIQ TIQGTTFIDQ
     NLTANKEYKY AVKAVDAAGN TSNQSNILLI KIKDQNVSYE KWDPRKAYTK GDKVEHQGKV
     YEAVQNHQGN GDPNWIFALS LWKPLTLNF
//
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