ID   CVNH_TUBBO              Reviewed;         103 AA.
AC   Q5MK11;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Cyanovirin-N homolog {ECO:0000303|PubMed:18400178};
DE            Short=CV-N homolog {ECO:0000303|PubMed:18400178};
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAV85993.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=16698294; DOI=10.1016/j.fgb.2006.04.001;
RA   Montanini B., Gabella S., Abba S., Peter M., Kohler A., Bonfante P.,
RA   Chalot M., Martin F., Ottonello S.;
RT   "Gene expression profiling of the nitrogen starvation stress response in
RT   the mycorrhizal ascomycete Tuber borchii.";
RL   Fungal Genet. Biol. 43:630-641(2006).
RN   [2] {ECO:0000305}
RP   STRUCTURE BY NMR, AND FUNCTION.
RX   PubMed=18400178; DOI=10.1016/j.str.2008.01.015;
RA   Koharudin L.M.I., Viscomi A.R., Jee J.-G., Ottonello S., Gronenborn A.M.;
RT   "The evolutionarily conserved family of cyanovirin-N homologs: structures
RT   and carbohydrate specificity.";
RL   Structure 16:570-584(2008).
CC   -!- FUNCTION: Mannose-binding lectin. {ECO:0000269|PubMed:18400178}.
CC   -!- INDUCTION: Down-regulated by nitrogen starvation.
CC       {ECO:0000269|PubMed:16698294}.
CC   -!- SIMILARITY: Belongs to the cyanovirin-N family. {ECO:0000305}.
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DR   EMBL; AY763505; AAV85993.1; -; mRNA.
DR   PDB; 2JZK; NMR; -; A=1-103.
DR   PDB; 2KJL; NMR; -; A=1-39, A=90-103.
DR   PDB; 3HNU; X-ray; 1.56 A; X=1-39, X=90-103.
DR   PDB; 3HNX; X-ray; 1.37 A; A=1-39, A=90-103.
DR   PDB; 3HP8; X-ray; 2.00 A; A/B=1-39, A/B=90-103.
DR   PDBsum; 2JZK; -.
DR   PDBsum; 2KJL; -.
DR   PDBsum; 3HNU; -.
DR   PDBsum; 3HNX; -.
DR   PDBsum; 3HP8; -.
DR   AlphaFoldDB; Q5MK11; -.
DR   SMR; Q5MK11; -.
DR   UniLectin; Q5MK11; -.
DR   EvolutionaryTrace; Q5MK11; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.60.10; -; 1.
DR   InterPro; IPR011058; Cyanovirin-N.
DR   InterPro; IPR036673; Cyanovirin-N_sf.
DR   Pfam; PF08881; CVNH; 1.
DR   SMART; SM01111; CVNH; 1.
DR   SUPFAM; SSF51322; SSF51322; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lectin.
FT   CHAIN           1..103
FT                   /note="Cyanovirin-N homolog"
FT                   /id="PRO_0000381733"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   STRAND          7..13
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   TURN            14..17
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:2JZK"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:2JZK"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:2JZK"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:2JZK"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:2JZK"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2JZK"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:3HNX"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:3HNX"
SQ   SEQUENCE   103 AA;  11435 MW;  590473CD22F889AE CRC64;
     MSYADSSRNA VLTNGGRTLR AECRNADGNW VTSELDLDTC IGNPNGFLGW GMQNFSHSSE
     DIKLEEGGRK LTCRPKTVDG GFRERQGIDL NRIQNVNGRL VFQ