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Database: UniProt
Entry: F2JRK0_CELLD
LinkDB: F2JRK0_CELLD
Original site: F2JRK0_CELLD 
ID   F2JRK0_CELLD            Unreviewed;      1472 AA.
AC   F2JRK0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Cellulose-binding family II {ECO:0000313|EMBL:ADZ83921.1};
GN   OrderedLocusNames=Clole_2208 {ECO:0000313|EMBL:ADZ83921.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ83921.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ83921.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; CP002582; ADZ83921.1; -; Genomic_DNA.
DR   RefSeq; WP_013657215.1; NC_015275.1.
DR   STRING; 642492.Clole_2208; -.
DR   KEGG; cle:Clole_2208; -.
DR   eggNOG; COG1800; Bacteria.
DR   eggNOG; COG4305; Bacteria.
DR   HOGENOM; CLU_250122_0_0_9; -.
DR   Proteomes; UP000008467; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.290; -; 2.
DR   Gene3D; 4.10.1080.10; TSP type-3 repeat; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR027797; PT-TG_dom.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR37467; EXPORTED CALCIUM-BINDING GLYCOPROTEIN-RELATED; 1.
DR   PANTHER; PTHR37467:SF1; EXPORTED CALCIUM-BINDING GLYCOPROTEIN-RELATED; 1.
DR   Pfam; PF00553; CBM_2; 2.
DR   Pfam; PF14449; PT-TG; 1.
DR   Pfam; PF18884; TSP3_bac; 5.
DR   SMART; SM00637; CBD_II; 2.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS51173; CBM2; 2.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1472
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003280533"
FT   DOMAIN          44..165
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          162..272
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          718..873
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
SQ   SEQUENCE   1472 AA;  163719 MW;  F6402E9BD2F8772F CRC64;
     MKTKKRILAY LLTLTLAMTS LPTQLFAQTT KDVPLPMSAL VDTQTTTPGA IQINPSKYIG
     DGYQVEFKVT NQWPGAFNGE FVLTNTGDKP LENWTLKFDF EHEITSMWNA QILTRESNSY
     AIKNMGWNQD IEPGSSITIG FQANGDGTIN NPSKYSLNME EQVASDVDYT IGFKLTGNWN
     GGFNGEISIT NQSNAPIEDW SLAFDFEANI NNLWTATIVE HTGNHYVIKN KGYNANIAPG
     QTLTLGFSGD NLEDSTIEPN NYKLSYIGSA TDKEEIDYEL DSDNDDLPDY YENILGTDPL
     NADTDGDGLP DGYEYCELMT DPLLQDSDGN NTSDADEDFD KDGLINREEF LLSTDPYNND
     TDKDSLLDGD EVNKFGTDPL VYDEIDIRID TDGDGLADQT ERIIGTDLTK IDTDNDGLPD
     NYEYFDFITN PTLSDTDNNG INDADEDFDN DGLTNLEEYT IRTDSFKPDS DNDGLIDGDE
     VNTYHTNPLI ADTDGDTLND GDEISMGLDP LNPFTFGTPD QEYVFVQDVA DDNLSAINTE
     DSPYKVSIQV KASGNAKGNT IVGQSEYAHT IEDNNAIVGK AISIKYHDGV LEEGKISFEL
     DESLVTQDNI VNDQRVTGIK RYQIFNFNEE YGILVPLPTI VDVKTNVIST EMIGQGTYCV
     MNLEKWLSNV GAFKTNQEVN ILKQSASIMA SVDTQTYDLK NNNLFNTTYP NTKSKKVDLA
     FVIDTGYTMQ KIMPSLKASM KEIVRGLKEE YNLDVEVSII DFKDINYMSP SSAIQINGIQ
     ASKAEGNRVL SFSNSLSEIE QIIDGLDAYG GYDTDISGTP LAGLGYVTTL PFRKDASKFA
     FLVTDKSYSI ANCHGFNTVY EMIEKLNTSG VNLGISYKTR EETGSISDNT ATFYRRWLQK
     INGVFVPLRI MADVESGFKE FIITNLIDQK EFQILGSTSL KEIILKEPLA KGGSADTDKD
     QLTDSEEVYW DSKLISYGID GYELPKIGDI WTLIYETHGY DISQIPFPEL LQDIVVLPIL
     SDPTDIDSDS DGLTDYVEHT NHFEHDTWSA LHYDKTNVDI YNTYERTVAH SKDEHTFILN
     PYIVTRPYTI NVNSDINLDI SVYYIGITGM SDPELVTTKY NIQDRIDFVP EKGGYYEVRI
     KLSSITSIGD YSMTIELLDM YKEAGFVEGD DVLVYAANHK GLYPFLATLE EGTYGILIPK
     FEDAEEFGQF NCAFSPGDGL SLVLDLTPLI GDAKTFIELI EGRDIITKQE INRWLLAGAI
     IVPRVVSEAI GLFGKNADDV AKYILKGDPK TVAKLKELGA TDGLITSIQK SEGAAGLDRL
     EKLLMQYFSC DDIATLSKYG ISTAEYQAKG ITYSSVAENV SKMLNTSDSY VELYRAVGVD
     EFEDIMSSNI FRPSPSGFVS KQFGFSFDEI LKLSNNFPES VAIFKAKIPK EVFIKLDFNA
     VDTAILKSGN ATVQEDVLKI FNDSLLEVKQ VY
//
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