ID   A0A2L2SPU9_9HYPO        Unreviewed;      1200 AA.
AC   A0A2L2SPU9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI38800.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) 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; LN649232; CEI38800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2SPU9; -.
DR   STRING; 56646.A0A2L2SPU9; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000245910; Chromosome iiii.
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:UP000245910}.
FT   DOMAIN          522..634
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          292..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          399..503
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          673..714
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          780..807
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          991..1022
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        292..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1200 AA;  137024 MW;  C52EDE12FF9AF825 CRC64;
     MYIKQIIIQG FKSYKDQTVI EPFSSKTNVI VGRNGSGKSN FFAAIRFVLS DAYTQMSREE
     RQGLLHEGSG SAVMSAYVEI IFDNSDDRFP TGNKEVILRR TIGLKKDEYS VDRKVVTKVD
     VMNLLEAAGF SRSNPYYIVP QGRVTALTNM KESDRLNLLK EVAGTQVYET RRAESLKIMN
     ETNNKREKID ELLVYIKERL NELEEEKEEL RGFQDKDRER RCLEYAYYHN IQLNVQSALE
     ELDNARQDGI DSSDTNRAEF SQGEKAISRL DSEIHKLQRE MELLQIDRRQ LEEDRRDSAK
     TMAKAEMKAK NLKEGQSAQE QVRAQHAADL ESVQNEIASK EQQLSTILPA YNEKKQEEDN
     VRRQLDHSES TRNRLFAKQS RGSQFRNKSE RDAWLKKEIQ ELELNISTQK ANKIDADEEV
     QRVHESIIQA EQEVAELRNR LANFSAERGA LEEEATKAGD VIDKLNDERK LVRREDDKLN
     SVIANARQEK EAAERELSHT MDGATARGLA TIRRLKHERD IPGAYGTLAE LLEVGDAYRL
     PVEQIAGASL FHYVVDNADT ATYLADTLYR LQGGRVTFMP LAQLRPKPIN LPRSNDAVPL
     LSKISYDQQY ERAFQQVFGK VVVCPNLTVA GQYARSHGVD GITAEGDTTN KRGAMTGGYI
     DPRKSRLQAV QAVNKWRGEY ERLLAQSRDI RQQIELKDQE ITAAMSELQK ARERLRQAVD
     GFEPLRHELM NKSTHLENER SHLDAAVKRR DAVESNMNSF LEDLAGHETE LKSDFKKNLT
     SAEERQLEEL GNSIQEFQKQ WNELSKARRD LGRQKQLLEV DLRQNLQMKL DQLNSQAFEN
     STSGSSAGGL KEAQRELKKA QKAQKNVEAR LQEVEAKLDD SQARLEQLEN DRAQREQAQQ
     EISARIEKQQ KRMDKSLRRK AVLTTQASEC AQTIRDLGVL PEEAFDKYEN MDPKTVSSKI
     KRVNDALKKY KHVNKKAFEQ YNNFTTQQDQ LMKRRKELDE SQESIEELVE HLDRRKDEAI
     ERTFKQVSRE FTTIFGKLVP AGHGRLLIQR RADRRQEPAD ESDGEARGAV ENYTGVGISV
     SFNSKHLDEQ QKIQQLSGGQ KSLCALCLIF ALQATESSPM VIFDEVDANL DAQYRTAVAA
     LLDSISNEIG TQFICTTFRP EIVHVADRCY GVTFRNKTSS IDCVSTEQAL DFVEGQAKPT
//