SMC4_DICDI
ID SMC4_DICDI Reviewed; 1415 AA.
AC Q54LV0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=SMC protein 4;
DE Short=SMC-4;
GN Name=smc4; ORFNames=DDB_G0286403;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with smc2. Component of the condensin
CC complex, which contains the smc2-smc4 heterodimer (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with smc2 forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64226.1; -; Genomic_DNA.
DR RefSeq; XP_637730.1; XM_632638.1.
DR AlphaFoldDB; Q54LV0; -.
DR SMR; Q54LV0; -.
DR STRING; 44689.DDB0219935; -.
DR PaxDb; Q54LV0; -.
DR PRIDE; Q54LV0; -.
DR EnsemblProtists; EAL64226; EAL64226; DDB_G0286403.
DR GeneID; 8625595; -.
DR KEGG; ddi:DDB_G0286403; -.
DR dictyBase; DDB_G0286403; smc4.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; Q54LV0; -.
DR OMA; QIYIDEC; -.
DR PhylomeDB; Q54LV0; -.
DR Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DDI-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q54LV0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000796; C:condensin complex; ISS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:dictyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:dictyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:dictyBase.
DR CDD; cd03274; ABC_SMC4_euk; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR041738; SMC4_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; DNA condensation;
KW Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1415
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000328140"
FT DOMAIN 695..812
FT /note="SMC hinge"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..479
FT /evidence="ECO:0000255"
FT COILED 533..675
FT /evidence="ECO:0000255"
FT COILED 855..1120
FT /evidence="ECO:0000255"
FT COILED 1162..1233
FT /evidence="ECO:0000255"
FT COMPBIAS 27..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1415 AA; 161555 MW; 75444BC92B3FD95D CRC64;
MVEDEEINDQ ISEEEEEKKK NNDSDEEMKD IDEEEEEEEE EEEEEEEEEK EEEEEEEEEE
TPKKPMPPPQ SKAKPSSQPP DIKKASQQSQ TQKNTPPPIQ TSQSSQSSQS SQSSQQQQPK
NISQTQQPKN TPPLQSSQTS QTSQKTPVSS NNGIEKRLMI TKMVMENFKS YAGAQEVGPF
HKCFSSVVGP NGSGKSNVID AMLFVFGYRA KQIRLNKISE LIHNSENHKN LTNGRVSVHF
QEIIDLPGED NYEVVKGSEF VVTRTAQKTG NNKDGVSKYY LNDKVVKLDD LKTILKDKGI
DLDNNRFLIL QGEVEQIAMM KPKGVHPGEE GLLEYLEDII GSKKYLPDIE ATSKLIEDIG
DKRTSSNNRM KVVEKEKDAL QQERDNALEY IDKELKLIHC KSIHYQIGRS KPEREKNEIA
AKQEMVEKQL EQELVTQKAS NDKLLEFEKN LKQQNKQLDE LNKQMAKCKN ELLTTEKKGV
KYKEETKHLK TKVKKNNSVI EEETKKQAEF ERSTIIHKQD IVRFEKEYVE LPKELIVEEK
KLESMLNSLK GEVTELQREM EEKQKQLLPW SKKHSEAKAV VDLKTSELAV LSKDFNGATQ
NLDDAIKALE DAKTISSTRK NNITKSKKEL ESVKAIIVDL EKRLASGKVT EENLYRNTMD
AKRQLEQIKT NLSENSSRNT ILDRLLKIKE SGQISGIHGR LGDLGAIDQK YDVAISTAAF
SQMDNIIVET TAAAEACVEL LRKENLGRAT FMILENLEYQ RQNLGPVQTP NNTPRLFDLI
KMKDEKKYAT AFFTAVGHTL VADTLDEATK IAYGAKRHRV VTLDGSLIDT SGAMSGGGLK
PRVGAMNSKL KGDPKEDKKK LIELQDNLSQ LDSDLRQCRD ELVEIENQIQ QAQNRRSELE
LELPKMDMDI KAAITKCEEL TKVIPQLKNK AKLSTEKKEQ IDSIKESLIV DQKSLDKVQE
KVNKLESEVQ EIQNSILNVG GPQLKMQKNK VESLQSRIDS NQTNTTKANV QIKSLAKSME
KSIKILNENT KEKDENEAAL AEILEKYKSL EKENLKATEA MEAVSEQLRE KEEETKEIRK
EHEKAKKVIE KIKVSNSKLE TQIEEFKTLI NEKQAEIADC LSKFANQAKK AKIYKDYVDE
SLINQVSAIL TPEEIEQYME ATEQQNLIAK IHELTTQIQK ISKENNVNIE VVKDFQKKEQ
EYHSRKAEFD EIEKERDNLS KRYESLRKNR LDEFMAGFTI ITMKLKEIYQ MITLGGDAEL
EIIDREDPFQ EGISFSVRPP KKSWKNISNL SGGEKTLSSL ALVFALHHYK PNALYVMDEI
DAALDFKNVS IIANYIKERT KNAQFIIISL RNYMFELADR LVGIYKTDNC TKSVTINPNS
FTSLSTTTTT TNNSQQQQQQ KQQQKQQQQN STSQK
