ID D8TK16_VOLCA Unreviewed; 448 AA.
AC D8TK16;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=BFN domain-containing protein {ECO:0000259|PROSITE:PS51658};
GN ORFNames=VOLCADRAFT_116201 {ECO:0000313|EMBL:EFJ52169.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ52169.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- FUNCTION: Bifunctional nuclease with both RNase and DNase activities.
CC Involved in basal defense response. Participates in abscisic acid-
CC derived callose deposition following infection by a necrotrophic
CC pathogen. {ECO:0000256|ARBA:ARBA00025428}.
CC -!- SIMILARITY: Belongs to the VHL family. {ECO:0000256|ARBA:ARBA00010057}.
CC -!- SIMILARITY: Belongs to the bifunctional nuclease family.
CC {ECO:0000256|ARBA:ARBA00009095}.
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DR EMBL; GL378325; EFJ52169.1; -; Genomic_DNA.
DR RefSeq; XP_002946943.1; XM_002946897.1.
DR AlphaFoldDB; D8TK16; -.
DR STRING; 3068.D8TK16; -.
DR GeneID; 9618339; -.
DR KEGG; vcn:VOLCADRAFT_116201; -.
DR eggNOG; ENOG502SAAR; Eukaryota.
DR InParanoid; D8TK16; -.
DR OrthoDB; 316848at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR CDD; cd05468; pVHL; 1.
DR Gene3D; 3.10.690.10; Bifunctional nuclease domain; 1.
DR Gene3D; 2.60.40.780; von Hippel-Lindau disease tumour suppressor, beta domain; 1.
DR InterPro; IPR036104; BFN_sf.
DR InterPro; IPR003729; Bi_nuclease_dom.
DR InterPro; IPR024053; VHL_beta_dom.
DR InterPro; IPR037140; VHL_beta_dom_sf.
DR InterPro; IPR036208; VHL_sf.
DR InterPro; IPR022772; VHL_tumour_suppress_b/a_dom.
DR PANTHER; PTHR15160:SF1; VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR; 1.
DR PANTHER; PTHR15160; VON HIPPEL-LINDAU PROTEIN; 1.
DR Pfam; PF02577; BFN_dom; 1.
DR Pfam; PF01847; VHL; 1.
DR SUPFAM; SSF103256; Hypothetical protein TM0160; 1.
DR SUPFAM; SSF49468; VHL; 1.
DR PROSITE; PS51658; BFN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001058}.
FT DOMAIN 258..388
FT /note="BFN"
FT /evidence="ECO:0000259|PROSITE:PS51658"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 46511 MW; 893EC5239E163B97 CRC64;
MTIVKDPSNN TYSSSSTGTT FDVPPGPPSW SRRAALFSLP ICAGVLLPGG WGRGAMEALA
SESTLVLPRP RPLRSLGWSV PSELTVLNDL EVPLKLYWLN YDGDAELFGS LSPGSVFTVL
TFESHAWRFV DGTSGATVAE HVMAAGQQIV RVAPSTAAAA GGALAGPSTS RPATSYTYQA
ATSRPQLGPR GSGTGGGAAA AEAGVAAAPP PGLEELPPPQ PPTTAVRSAT AGSASDGGVV
PAPLFEGFDG LGNEEQQYCL AQLREIEIFP GGGNVLLVLP GSKTPLELTL AGPEALSLVA
ATGSLEQRRP STLGTWTRSL MVSGVELRRV CINRMVDGVY YCRIVLSRPD GSLCSVDATP
GDSLSMALQL RKPIYVASEV ARVHQSVADV FASRRRAMEE AAASGLLDEA AEAEADLKAQ
AALDSITRGI PSAPRPVRVL QMDSHLDA
//
