CVNH_CERRI
ID CVNH_CERRI Reviewed; 142 AA.
AC P86326;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Cyanovirin-N homolog {ECO:0000303|PubMed:18400178};
DE Short=CV-N homolog {ECO:0000303|PubMed:18400178};
DE Flags: Precursor;
OS Ceratopteris richardii (Triangle waterfern).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Parkerioideae; Ceratopteris.
OX NCBI_TaxID=49495;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chatterjee A., San Miguel P., Stout S.C., Banks J., Roux S.J.;
RT "Expressed sequence tags of cDNA clones from a C. richardii library.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP STRUCTURE BY NMR OF 28-142, FUNCTION, AND DISULFIDE BONDS.
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 -!- SIMILARITY: Belongs to the cyanovirin-N family. {ECO:0000305}.
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; BQ087517; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 2JZJ; NMR; -; A=28-142.
DR PDBsum; 2JZJ; -.
DR AlphaFoldDB; P86326; -.
DR SMR; P86326; -.
DR UniLectin; P86326; -.
DR EvolutionaryTrace; P86326; -.
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; 2.
DR SMART; SM01111; CVNH; 1.
DR SUPFAM; SSF51322; SSF51322; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Lectin; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..142
FT /note="Cyanovirin-N homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000381731"
FT DISULFID 29..128
FT /evidence="ECO:0000269|PubMed:18400178"
FT DISULFID 35..49
FT /evidence="ECO:0000269|PubMed:18400178"
FT DISULFID 85..100
FT /evidence="ECO:0000269|PubMed:18400178"
SQ SEQUENCE 142 AA; 15223 MW; 6DBB068AEACF3284 CRC64;
MRALAPSFRL LAGLLLLIVL SLSSANAQCN FANSCTGVEL YGYILRGDCI NEDGHPHATS
INLNYYIGND NGRLEYPGES FGSSCVKTAL NDGHTLTASC KGADGQYHDS SMDLNYVVGN
SYGYMEPCRA SNADHVLKSS SE