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Database: UniProt
Entry: D7TAF5_VITVI
LinkDB: D7TAF5_VITVI
Original site: D7TAF5_VITVI 
ID   D7TAF5_VITVI            Unreviewed;       291 AA.
AC   D7TAF5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN   OrderedLocusNames=VIT_01s0010g01670 {ECO:0000313|EMBL:CBI27478.3};
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:CBI27478.3, 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: Plays an important role in the control of DNA replication and
CC       the maintenance of replication fork stability.
CC       {ECO:0000256|RuleBase:RU366049}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU366049}.
CC   -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000256|ARBA:ARBA00006075,
CC       ECO:0000256|RuleBase:RU366049}.
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DR   EMBL; FN595754; CBI27478.3; -; Genomic_DNA.
DR   RefSeq; XP_002272919.1; XM_002272883.3.
DR   AlphaFoldDB; D7TAF5; -.
DR   STRING; 29760.D7TAF5; -.
DR   PaxDb; 29760-VIT_01s0010g01670-t01; -.
DR   EnsemblPlants; Vitvi01g01435_t001; Vitvi01g01435_P001; Vitvi01g01435.
DR   GeneID; 100240999; -.
DR   Gramene; Vitvi01g01435_t001; Vitvi01g01435_P001; Vitvi01g01435.
DR   KEGG; vvi:100240999; -.
DR   eggNOG; KOG3004; Eukaryota.
DR   HOGENOM; CLU_060030_0_0_1; -.
DR   InParanoid; D7TAF5; -.
DR   OMA; GLYREWH; -.
DR   OrthoDB; 298741at2759; -.
DR   Proteomes; UP000009183; Chromosome 1.
DR   ExpressionAtlas; D7TAF5; baseline.
DR   GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0043111; P:replication fork arrest; IBA:GO_Central.
DR   GO; GO:0031297; P:replication fork processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR012923; Csm3.
DR   InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR13220; TIMELESS INTERACTING-RELATED; 1.
DR   PANTHER; PTHR13220:SF11; TIMELESS-INTERACTING PROTEIN; 1.
DR   Pfam; PF07962; Swi3; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU366049};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366049};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          11..26
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32473 MW;  57D19AD68983BE70 CRC64;
     MEKSGAAPTG CYKCGRPGHW SRDCPSSNTN PNPNPNPNPN SQNQYSSFNK GTASKPLAKS
     SEKPKKAPRT RPNLTPELLL SDNGLGYVLR HFPGAFKFRG RGHEVSDLGN LIGLYSEWHS
     HLLPYYSFDQ FVHKVEKVGT TKRVKICIRE LRERVENGGD LTKFHEPPVE HEDCPNHDQG
     LPATEEVMNS VDPSHYQGDT SLNHEDVQED MLHEVYRSAT EEPSQTLASD MVAGDVPSEG
     SSKKELPNQV PENGPIRSDI QITEEQKARM EANRQKALER AAARVRLQQA V
//
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