ID I1LIR6_SOYBN Unreviewed; 318 AA.
AC I1LIR6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN Name=100808422 {ECO:0000313|EnsemblPlants:KRH29133};
GN ORFNames=GLYMA_11G099800 {ECO:0000313|EMBL:KRH29133.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH29133};
RN [1] {ECO:0000313|EMBL:KRH29133.1, ECO:0000313|EnsemblPlants:KRH29133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH29133};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH29133.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH29133}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH29133};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH29133.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH29133.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000844; KRH29133.1; -; Genomic_DNA.
DR RefSeq; XP_006590796.1; XM_006590733.2.
DR AlphaFoldDB; I1LIR6; -.
DR SMR; I1LIR6; -.
DR STRING; 3847.I1LIR6; -.
DR PaxDb; 3847-GLYMA11G10610-1; -.
DR EnsemblPlants; KRH29133; KRH29133; GLYMA_11G099800.
DR GeneID; 100808422; -.
DR Gramene; KRH29133; KRH29133; GLYMA_11G099800.
DR KEGG; gmx:100808422; -.
DR eggNOG; KOG3004; Eukaryota.
DR HOGENOM; CLU_060030_0_0_1; -.
DR InParanoid; I1LIR6; -.
DR OMA; GLYREWH; -.
DR OrthoDB; 298741at2759; -.
DR Proteomes; UP000008827; Chromosome 11.
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:UP000008827};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 23..37
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 35649 MW; E2E66A8BF8C23409 CRC64;
MVQCESDCRE KMEGTGAGTA TGCYKCGKPG HWSRDCPFSA PNPNPNSNTA TTPNPNTPNP
SSSSFKSRSA TEKPKKLPRT KPKLTPELLL SDDGLGYVLR YFPREFKYRG RGHEVRDLGN
LLRLYTEWHS RLLPYYSFNQ FVHKVEKVAA TRRVKTCLRE LRERVASGGD PTKLREPPVV
HDIPSDEHGF SVSAEDGGAT HQEADLFAEF ENVNDIQEDM LNDIYDKATE EPSQSMHNVI
GTSMASESNA TEKTSEENGS SQSGKAEITE EQRARMEANR LKALERRAEI TEEQRARMEA
NRLKALERRA ALSQASQL
//
