ID A0A218WSP7_PUNGR Unreviewed; 424 AA.
AC A0A218WSP7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Protein IQ-DOMAIN 14-like {ECO:0000313|RefSeq:XP_031383337.1};
GN Name=LOC116197355 {ECO:0000313|RefSeq:XP_031383337.1};
GN ORFNames=CDL15_Pgr021801 {ECO:0000313|EMBL:OWM75636.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM75636.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
RN [2] {ECO:0000313|EMBL:OWM75636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM75636.1};
RA Xu C.;
RT "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_031383337.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_031383337.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; MTKT01003240; OWM75636.1; -; Genomic_DNA.
DR RefSeq; XP_031383337.1; XM_031527477.1.
DR OrthoDB; 1130596at2759; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR Proteomes; UP000515151; Chromosome 2.
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:SF174; PROTEIN IQ-DOMAIN 24; 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}.
FT DOMAIN 347..379
FT /note="DUF4005"
FT /evidence="ECO:0000259|Pfam:PF13178"
FT REGION 225..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 47115 MW; 4CBA5648AA9E3F1C CRC64;
MGFLQRLFGG KKKKEKSGDN PSNWKLWSFF QSLNSNKRLA LPSSSFNPAP YPDDLELDPN
KHAIAVAVAT AAVAEAALAA AQAAAEVVRL TGGGGGGVSG APLPQTSRPP RLVLVEEAAA
VKIQCAFRGY LARRALRALK ALVKLQALVR GHMVRKRMTD MLRRMQTLVR LQARARASRN
CLSASSNSPG SSSFHQLRCG SYASHSLDPA QVGSSWLDRW MEESARNNKK DSQVRNGHDD
DKGTKILEVD TWKPRFNPPQ NHEYRRTADR DFPSCYVSSG HMVLDSPLKH PISSRGAFCL
NEQGGKGEAL RYFENIQQAN PVPSRPGSSS SWRDPFSPTK SEVSWGGYSR YLGHPSYMAN
TESSRAKVRS QSAPRQRVEF DNCSSMRRNV LTESWDGGLN SERRYPPHAE FRTRAYSERQ
HSIR
//
