ID F6H068_VITVI Unreviewed; 792 AA.
AC F6H068;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=DUF4005 domain-containing protein {ECO:0000259|Pfam:PF13178};
GN OrderedLocusNames=VIT_18s0001g13870 {ECO:0000313|EMBL:CCB46016.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB46016.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- FUNCTION: May be involved in cooperative interactions with calmodulins
CC or calmodulin-like proteins (By similarity). Recruits calmodulin
CC proteins to microtubules, thus being a potential scaffold in cellular
CC signaling and trafficking (By similarity). May associate with nucleic
CC acids and regulate gene expression at the transcriptional or post-
CC transcriptional level. {ECO:0000256|ARBA:ARBA00024682}.
CC -!- SUBUNIT: Binds to multiple calmodulin (CaM) in the presence of Ca(2+)
CC and CaM-like proteins. {ECO:0000256|ARBA:ARBA00024378}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000256|ARBA:ARBA00024341}.
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DR EMBL; FN595227; CCB46016.1; -; Genomic_DNA.
DR AlphaFoldDB; F6H068; -.
DR STRING; 29760.F6H068; -.
DR PaxDb; 29760-VIT_18s0001g13870-t01; -.
DR EnsemblPlants; Vitvi18g01080_t001; Vitvi18g01080_P001; Vitvi18g01080.
DR Gramene; Vitvi18g01080_t001; Vitvi18g01080_P001; Vitvi18g01080.
DR eggNOG; KOG1075; Eukaryota.
DR HOGENOM; CLU_019543_0_0_1; -.
DR InParanoid; F6H068; -.
DR Proteomes; UP000009183; Chromosome 18.
DR ExpressionAtlas; F6H068; baseline and differential.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.190; -; 1.
DR InterPro; IPR025064; DUF4005.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32295; IQ-DOMAIN 5-RELATED; 1.
DR PANTHER; PTHR32295:SF154; PROTEIN IQ-DOMAIN 32; 1.
DR Pfam; PF13178; DUF4005; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 2.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT DOMAIN 712..777
FT /note="DUF4005"
FT /evidence="ECO:0000259|Pfam:PF13178"
FT REGION 189..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 85874 MW; D8EBD310459F6F18 CRC64;
MGRSASCFKI ISCGGDSVGQ DELDLAERKG YSDKRGWSFR KRSARHRVLS NTVVSEIPSS
GNKESPESAA INFQTPVDST IPEKTSVPQW ADEKPQLSTS FNSKASETVV ASENESKVDV
NVDESAAIAI QAAVRGFLAQ RALLKLKNVI KLQAAVRGHL VRRHAVGTLR VVQAIVKIQA
LVRARRVQAG KLDDRKDKPS SKPMEKENSS ADPSATYTSI DKLLSNGFAR QLLESNPRTK
SIHIKCDPSR PNSGWQWLER WMSVSSSNLG QPQIPVLEKE ELEHERVENS AVQVETGITS
ETTSESEDLK SNVRETAVPS ESEENLITYD AESFDFQTCC PTSSSVKDNL ELPPSENTGG
TSHAKDSPSE IDLLPNHTMQ PEEKSLTEFN SVSGKSEMES EQPKRSVKRF ASEQLETEGK
KFVFGSRKVS NPAFVAAQSK FEELSSTANS GRLISPSHQD VGVESNIETV SSAADTSITT
KDLNSEDNSI PPNSRLQVGG SECGTELSIT STLDSPDISE VGAMEFDNEA KVSEEVICNL
NSTGGLDVES KDVSTIAVSN LSDTMLAPPE KRDAVNGEPV NSVVDVDSSQ VKQKPERTAS
DLQIELDPQT GRQAYRSSPE ASPRSHITVP ESQGTPSSQV SVKAKRSKTD KSGSNQKRAS
LSAGKRSPSN PNHDSGARSS MEQLPKDQKT GKRRNSFGST RPDNVDQEPR DSSSSNSLPS
YMQATESARA KLHANNSPRS SPDVQDKDIY IKKRHSLPGA NGRQGSPRIQ RSMSQAQQGA
KGNSANPPHG IF
//
