ID C5CYC7_VARPS Unreviewed; 1577 AA.
AC C5CYC7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Ricin B lectin {ECO:0000313|EMBL:ACS17031.1};
DE Flags: Precursor;
GN OrderedLocusNames=Vapar_0368 {ECO:0000313|EMBL:ACS17031.1};
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS17031.1};
RN [1] {ECO:0000313|EMBL:ACS17031.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S110 {ECO:0000313|EMBL:ACS17031.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA Leadbetter J.R., Spain J.C., Han J.I.;
RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001635; ACS17031.1; -; Genomic_DNA.
DR STRING; 543728.Vapar_0368; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR KEGG; vap:Vapar_0368; -.
DR eggNOG; COG1858; Bacteria.
DR eggNOG; COG3391; Bacteria.
DR eggNOG; COG5276; Bacteria.
DR HOGENOM; CLU_245535_0_0_4; -.
DR OrthoDB; 8673369at2; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR032812; SbsA_Ig.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR47197:SF3; PE-PGRS FAMILY PROTEIN PE_PGRS17; 1.
DR PANTHER; PTHR47197; PROTEIN NIRF; 1.
DR Pfam; PF13205; Big_5; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00089; PKD; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51007; CYTC; 2.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Lectin {ECO:0000313|EMBL:ACS17031.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1577
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002950101"
FT DOMAIN 769..841
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1195..1320
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 1336..1440
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 1577 AA; 167000 MW; 08930C5409AA0104 CRC64;
MKIRYFLMAF LAPLVTLLTH AAITGVSPMT TLGNMATAVS EAVADPLPLQ GPGLGNLSYT
SAELFKPVSM ITSLAHPLDP AHSSAYESRE VPATYPGRKD YGMNAGIMVN GYFLTSFAPD
SGLGPGGFLL YDVSNPRQIR LVKKIYEPDD ATGGRTKEFR ETHSFGTAKI GGKTYVVLPS
INGVEFWDFT DVNDIKQVKK LALPGVNAGD YENVAWQLWW QAPYLYVASA GRGIFIVDAA
DPANAVVANR GAGKPNPVPT GELGNFRIGP IFTMGNHMVL TAMESNGGFA SLDISDPLNP
KVLDSIVGTT PFYYATCFDG RNLHVSTRGS GAKMYSYDLS DRSRFVAEDN RLVIDEQLYC
ATQDNYVIQG AQTRIHKVDV SNPLNHVEVG RGSILREDDP NYSHSDNGQV AMFGNLVFVG
NDHGSGSGFV VHAVDPDTTR PEVKQVSPAN GAKQQALSSR IGLGMTDNIR PESVNANTFI
VRPVGGNTLA GTYSVQLGII NFHPELPLSP GTSYEVFLPA NGVKDYAGNA IGADFKSTFN
TGNATDINLQ HYWTLAGNLS DPIGSNNGTP ASGDTFESIG MSFANRTAGV PLKNDSVATV
LGGTASLSFY MKTTQAGSAN PWTAPGIFGR DQASGADDVF WGWIDGSGFM NLSVANKAAN
NPGTRSLAAV NDGNWHHVVM TRDAASGAQA MYVDGVKTSS TGLTGTKGLA NKFQVMGQIQ
GNADLFKGTL AEVRVYSRVL TDGEVATLRG QAIIGDPGIG GGPKIVNGQL VFDPATLGSS
GAQFRWNFGD GTRTAYSTQP RYTYTYTRPG HYTVTLTVRD ASGRETFYTY NLTVIVPVTA
RAPTHTTNIA GDANSVYSLN PDSGTVAAVD AQTLAKRWEV RVGDEPKTLA VGPDGRIWVA
VQGEDKLVAL SAADGSLSAT VPLAYGSGPY GVAFTPDGAK GLLTLESKSV LMSFDPSNGA
TTGAVALEGS LRGIAVSSDA QVAYVTRFKS KLTGGQLHKV NLQSMSAMPT IALPVDTTTV
DTESRARGVA NYLSQVVISP DGRRAVLPSK KDNIVRGRFR DGVDLTHDQS VRSILSQVDL
QAAAEVFGEQ IDFDDRAPAR AALFSPPGDY LFVAQMEGNR VAIVDPYSRA VRGEINASSA
PHGLYLDAAR KRLFVNNFLA RSVSVHDVSL VLSSESAAAT FLQNVATVAQ EPMAAAALRG
KQVFYNASDR RMSKDNYISC ASCHADGGDD GMVWDFTQRG EGLRRTISLM GRRGAGHGKM
HWTANFDEVQ DFENDIRNEF GGTGFLTNAD FAATVDPLGA PKAGKSAQLD DLAAYLSSLN
KYMRSPARAA DGSLSVEAAR GQTVFNTAQC ATCHTGGTFR DGLRHDVGTI QLSSGKGHNQ
PLAGLGFDTP TLSGTWNTAA FFHNGQAATL QDVLNSGHGN ASSLPPADVV ALREYVRSLD
TAPAVVTRLR SDLNPTMCVN IKGGATASGT VAVQWPCGTA SHEKFTVTSV TGGYVQLVAE
HSGLCLAQNG TATTNAPVVQ LACTVGNTAQ WSLAVGTLRN RASGSCLDVP NGSTTQDTAL
ITWTCNGGNN QNWTQLP
//
