ID   A0A2H3TF52_FUSOX        Unreviewed;      1198 AA.
AC   A0A2H3TF52;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=FRV6_07477 {ECO:0000313|EMBL:SCO83264.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO83264.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FMJY01000004; SCO83264.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:FOC1_g10013687; -.
DR   VEuPathDB; FungiDB:FOC4_g10010394; -.
DR   VEuPathDB; FungiDB:FOIG_05735; -.
DR   VEuPathDB; FungiDB:FOMG_04995; -.
DR   VEuPathDB; FungiDB:FOXG_02072; -.
DR   VEuPathDB; FungiDB:FOZG_05165; -.
DR   VEuPathDB; FungiDB:HZS61_009976; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000219369; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   CDD; cd03272; ABC_SMC3_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; IPR041741; SMC3_ABC_euk.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
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   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719}.
FT   DOMAIN          522..634
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          837..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          186..220
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          260..294
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          323..374
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          399..503
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          726..770
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1198 AA;  136967 MW;  14CE1C4749036A4A CRC64;
     MYIKQIIIQG FKSYKDQTVI EPFSPKTNVI VGRNGSGKSN FFAAIRFVLS DAYTQMSREE
     RQGLLHEGSG SAVMSAYVEI IFDNSDDRFP TGNKDVILRR TIGLKKDEYS VDRKVVTKAD
     VMNLLEAAGF SRSNPYYIVP QGRVTALTNM KESDRLNLLK EVAGTQVYET RRAESLKIMH
     ETNNKREKID ELLEYIKERL SELEEEKEEL RAFQDKDRER RCLEYAYYHN IQLGIQANLD
     ELDNVRQDGI DSSDTNRAEY TEGEKAISRL DSEIHKLQRE MELLQIERRQ VEEDRRDGAK
     ALAKAEMKVR NLREGQSAQE QARAQHAAEL ESVQNEIASK EQQLSTINPA YSQKKQEEDE
     IRRQLDHAEA TRNRLFAKQS RGSQFRNKSE RDTWLRKEIQ ELELNISTQK ANKIDADEEV
     ERVRESIAQA EQDVADLRNR LANFSGEKTA LEEEVAKARD IIDKLNDERK LVRREDDKLN
     SVIANARQEK ETAERELAHA MDGSTARGLA TIRRLKQERD IPGAYGTLAE LLEVSDAYRL
     PVEQIAGASL FHYVVNNADT ATYLADTLYR QQGGRVTFMP LAQLRPRQIK LPRSNDAVPL
     LSKINYNEEY EKAFQQVFGK AVVCPNLTVA SQYARSHGVD GITPEGDTTN KRGAMTGGYI
     DPRKSRLHAV QAVNKWRDEY ERLLAQSRDI RKQTERKDQE ITAAMSDLQK ANERLRQAVD
     GFEPLKHELI NKSKHLEKEL SHLDAAIKRR DAVEKNMNSF LEDLAAHEAE LRSDFKKXLT
     AAEERQLEEL GTSTQELQKQ WNELSRARRD LERQKQLLEV DLRQNLQMKL DQLNSQAFED
     STGSSGGGLK DAQRELKKAQ KVQKAVEASL QELETKMDNT QARLEELANE KAQLEQAQSE
     ISARIERQQK KMDKSLRKKA VLSTQAAECA QTIRDLGVLP EEAFDKYENM DPNQVSTKIK
     KVNEALKKYK HVNKKAFEQY NNFTTQQDQL MKRRKELDDS QESIEVLVEH LDRRKDEAIE
     RTFKQVSKEF TTIFGKLVPA GHGRLLIQRR ADRRQEPVDE SDGEARGVEN YTGVGISVSF
     NSKHLDEQQK IQQLSGGQKS LCALCLIFAL QATESSPMVI FDEVDANLDA QYRTAVAALL
     ESISKEIGTQ FICTTFRPEI VHVADRCYGV TFRNKTSSID CVSTEQALEF VEGQAKPT
//