ID K3VAG2_FUSPC Unreviewed; 1183 AA.
AC K3VAG2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=FPSE_09102 {ECO:0000313|EMBL:EKJ70732.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ70732.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ70732.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ70732.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKJ70732.1}.
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DR EMBL; AFNW01000305; EKJ70732.1; -; Genomic_DNA.
DR RefSeq; XP_009260494.1; XM_009262219.1.
DR AlphaFoldDB; K3VAG2; -.
DR EnsemblFungi; EKJ70732; EKJ70732; FPSE_09102.
DR GeneID; 20367719; -.
DR KEGG; fpu:FPSE_09102; -.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000007978; Chromosome 4.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT DOMAIN 522..634
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 291..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..503
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 780..814
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 974..1005
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 291..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 134712 MW; 4A27D8BBB4A612BC CRC64;
MYIKQIIIQG FKSYKDQTVI EPFSSKTNVI VGRNGSGKSN FFAAIRFVLS DAYTQMSREE
RQGLLHEGSG SAVMSAYVEI IFDNSDDRFP TGNKEVILRR TIGLKKDEYS VDRKVVTKAD
VMNLLEAAGF SRSNPYYIVP QGRVTALTNM KESDRLNLLK EVAGTQVYET RRAESLKIMN
ETNNKREKID ELLVYIKERL NELEEEKEEL RGFQDKDRER RCLEYAYYHN IQLNVQSALE
ELDNARQDGI DSSDTNRAEF SQGEKAISRL DSEIHKLERE MELLQIDRRQ LEEDRRDSAK
SMAKAEMKTK NLKEGQSAQE QARAQHAADL ESVQNEVASK EQQLSAILPA YNEKKQEEDN
VRRQLDHAES TRNRLFAKQS RGSQFRNKSE RDAWLKKEIQ ELELNISTQK ANKIDADEEV
QRVHESIAQA EQEVAELRNR LANFSAERGA LEEEATKAGD VIDRLNDERK LVRREDDKLN
SVIANARQEK EAAERELSHT MDGATARGLA TIRRLKQERD IPGAYGTLAE LLQVSDAYRL
PVEQIAGASL FHYIVDNADT ATYLADTLYR QQGGRVTFMP LAQLRPKSIN LPRSNDAVPL
LSKISYDEAY EKAFQQVFGK VVVCPNLTVA SQYARSHGVD GITAEGDTTN KRGAMTGGYI
DPRKSRLQAV QAVNKWRGEY ERLLAQSRDI RQQTELKDQE ITAAMSELQK ARERLRQAVD
GFEPLRHELM NKSTHLENER GHLDAAVKRR DAVESNMNSF LEDLAGHETE LKSDFKKNLT
SAEERQLEEL GNSIQELQKE WNELSRARRD LGRQKQLLEV DLRQNLQMKL DQLNSQAFEN
STSGSSAGGL KEAQRELKKA QKAQKTVEAS LQEVEAKLDD SQARLEQLEN DRAQREQAQQ
EISARIEKQQ KRMDKSLRRK AVLTTQAAEC AQTIRDLGVS SKIKRVNDAL KKYKHVNKKA
FEQYNNFTTQ QDQLMKRRKE LDESQESIEE LVEHLDRRKD EAIERTFKQV SREFTTIFGK
LVPAGHGRLL IQRRADRRQE PADESDGEAR GAVENYTGVG ISVSFNSKHL DEQQKIQQLS
GGQKSLCALC LIFALQATES SPMVIFDEVD ANLDAQYRTA VAALLDSISN EIGTQFICTT
FRPEIVHVAD RCYGVTFRNK TSSIDCVSTE QALDFVEGQA KPA
//
