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Entry: I1LVC8_SOYBN
LinkDB: I1LVC8_SOYBN
Original site: I1LVC8_SOYBN 
ID   I1LVC8_SOYBN            Unreviewed;      1176 AA.
AC   I1LVC8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=100780995 {ECO:0000313|EnsemblPlants:KRH27467};
GN   ORFNames=GLYMA_12G236600 {ECO:0000313|EMBL:KRH27467.1};
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:KRH27467};
RN   [1] {ECO:0000313|EMBL:KRH27467.1, ECO:0000313|EnsemblPlants:KRH27467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH27467};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH27467.1};
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:KRH27467}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH27467};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH27467.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH27467.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
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DR   EMBL; CM000845; KRH27467.1; -; Genomic_DNA.
DR   RefSeq; XP_003540523.1; XM_003540475.3.
DR   AlphaFoldDB; I1LVC8; -.
DR   SMR; I1LVC8; -.
DR   STRING; 3847.I1LVC8; -.
DR   PaxDb; 3847-GLYMA12G36520-1; -.
DR   EnsemblPlants; KRH27467; KRH27467; GLYMA_12G236600.
DR   GeneID; 100780995; -.
DR   Gramene; KRH27467; KRH27467; GLYMA_12G236600.
DR   KEGG; gmx:100780995; -.
DR   eggNOG; KOG0933; Eukaryota.
DR   HOGENOM; CLU_001042_9_0_1; -.
DR   InParanoid; I1LVC8; -.
DR   OMA; HNKIAME; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000008827; Chromosome 12.
DR   ExpressionAtlas; I1LVC8; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR   GO; GO:0000796; C:condensin complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR   CDD; cd03273; ABC_SMC2_euk; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR027120; Smc2_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   DOMAIN          518..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          239..287
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          317..448
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          473..507
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          789..928
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          982..1026
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1176 AA;  132499 MW;  9DA5547595D8A38B CRC64;
     MYIKEICLEG FKSYATRTVV PGFDPFFNAI TGLNGSGKSN ILDSICFVLG ITNLQQVRAS
     NLQELVYKQG QAGITKATVS VVFDNSHSSR SPLGYEGHSE ITVTRQIVVG GRNKYLINGK
     LAQPSQVQNL FHSVQLNVNN PHFLIMQGRI TKVLNMKPQE ILSMLEEAAG TRMYETKKEA
     ALKTLEKKQS KVDEINKLLD QEILPALEKL RKEKTQYMQW ANGNAELDRL RRFCIAYEYV
     QAKRIKDNAA SEVEEVKARI AEIDDVAKIN KVEIKEMETK ITQLTAEKEA NMGGEMKSLS
     EKVDALSQNL VRETSVLNNK EDTLRSEEAN KANLVKNIEE LKHSVQEKAS AVKKAEEGVA
     DLKNKVDELT KSLEEHEKEY QGVLAGKSSG NEEKCLEDQL RDAKVAVGST ETELKQLKAK
     ISHCEKELKE KTSQLRSKCE EANAVENELS TRKKDVGNVR MELESLSYKE GEMEDLQKER
     MTEMDCVQKL KDEIRNLSAN LANVEFTYCD PVKNFDRSKV KGVVAKLIKV KDRSTMTALE
     VTAAGKLYNV VVDTENTGKQ LLQNGNLRRR VTIIPLNKIQ SYSVSSRVQQ AAVRLVGKGN
     AEVALSLVGY EEELRSAMEY VFGSTFVCKT IDAAKEVAFN REIHTTSVTL EGDIFQPSGL
     LTGGSRKGGG DLLGQLHALS EAESKLSVHQ RRLSEIEAKI SKLLPLQKKF IDLKAQLELK
     LYDLSLFQSR AEQNEHHKLG ELVKKIEQEL NEVKSTVKDK QLLYKDCVKT VSSLEKSIKD
     HDNNRESRLK GLEKKIKTIK SQMQSSLKDL KGHDSEKERL VMEMEAVIQE QASLENQLAS
     LGTLISNLAS EVEEQRSSVV AARDNLDQVQ SQLKSVRLKM KECDQEISAI IKEQQKLEHK
     ISESNLERKR MENEVKRMEM EQKDCSVRVD KLIEKHAWIA SEKQLFGRSG TDYDFSSRDP
     TKAREELEKL QAEQSGLEKR VNKKVMAMFE KAEDEYNDLM SKKNIIENDK SKIKMVIEEL
     DEKKKETLNV TWIKVNNDFG SIFSMLLPGT MAKLEPPEGC SFLDGLEVRV AFGSVWKQSL
     SELSGGQRSL LALSLILALL LFKPAPLYIL DEVDAALDLS HTQNIGRMIK AHFPHSQFIV
     VSLKEGMFNN ANVLFRTKFV DGVSTVQRTV AAKQSK
//
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