SMC2_DICDI
ID SMC2_DICDI Reviewed; 1184 AA.
AC Q54PK4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
GN Name=smc2; ORFNames=DDB_G0284499;
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 smc4. 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 smc4 forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000066; EAL65176.1; -; Genomic_DNA.
DR RefSeq; XP_638528.1; XM_633436.1.
DR AlphaFoldDB; Q54PK4; -.
DR SMR; Q54PK4; -.
DR STRING; 44689.DDB0219933; -.
DR PaxDb; Q54PK4; -.
DR PRIDE; Q54PK4; -.
DR EnsemblProtists; EAL65176; EAL65176; DDB_G0284499.
DR GeneID; 8624621; -.
DR KEGG; ddi:DDB_G0284499; -.
DR dictyBase; DDB_G0284499; smc2.
DR eggNOG; KOG0933; Eukaryota.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; Q54PK4; -.
DR OMA; HNKIAME; -.
DR PhylomeDB; Q54PK4; -.
DR Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DDI-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q54PK4; -.
DR Proteomes; UP000002195; Chromosome 4.
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; 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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:dictyBase.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 3.40.50.300; -; 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 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; 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..1184
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000328135"
FT DOMAIN 520..639
FT /note="SMC hinge"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1184 AA; 135084 MW; B2E3F615789E80FB CRC64;
MYIEDIIIDG FKSYANRTVI EGFDPTFNAI TGLNGSGKSN ILDSICFVLG ISNLSQVRVD
SLQELVYKKG QAGITKASVT ITFNNSDKKQ SPAGYEHLDK ITVTRQVAIG GRNKYLINGH
NAQLSRVQDL FHSVQLNVNN PHFLIMQGRI TKVLNMKPPE ILAMIEEAAG TRMFEMKKNS
ALNTIEKKQK KVDEITKVLA EEITPTLDKL RGERTSYMKF TNNQTLIDRL QRFIIAYEYY
TYEKKLESSE FESFKAEIDK GQKRKKDLTL KSTDLKAKIS ELAKQREKET NLEEMDQQEQ
KLSKELVKYQ TSHKHQKESL DKEEGAINNL ANTREEIKQS IQQKQKEKQS MEKKIQSIVE
ENQQINAELK TLQNKHNTMT TGISTGADGS SAAEDGSYTE QLMEAKKTAV NAASEYKQAE
FRVKHLQSEL IAKRKAITQE QTDHKKLQAE QELVEREIQQ LTRSIQELQL DNSKQQELTE
KKRQLEPLVS KLREEVGNAS AQLSGLEFNY TDPSKSFDRS KVKGIVANLI TLKDVETATA
LEICASGKLY NIVIEDDETG KALLSKGQLK RRVTLLPLNK VEGRSIDPQK IKNAQKIAPN
GAVKPAIEFV EYDKELQPAM NFVFGSTFIA TDKKYAQKAA FDSSIKVRTI SLEGDEYNPA
GSLTGGSRPP SGSILTQIQR LNENNRCLRE NQSQLEHINF ELVQLKSVTD RFKQLEQQLN
IKQHAASLIA QRFQLNPHHQ LLESIKEMEK SIESDTQLIT NSMIKEKEAL EKVKQLESQV
NDFQSIRESQ LKDLEKKIQI TKEKCIKSNK IVKGEQVFIE KLDLEIQEMD NELENLSKET
QGNQGTISKM RKDVDTLARS ISETNKQIQD IRETLSEIRK DMAQKNDAIR SLHQELEKIQ
SEITEIDMST EKLKSRMNRV DKDRQEASKW LEAAIKKHTW IKNEKQLFNR PGSDFDFNAT
DPSKANSEYI KLQEEQEKLS KTINRKVMSM FEKAEQEYQE LMEKKKIIEN DKSKIEHVIR
ELDEKKNESL RTTWKKVNKD FGSIFSTLLP GTSAKLEPPE GQNELFGLEV KVAFGDVWKE
TLSELSGGQK SLLALSLILS LLLFKPAPMY ILDEIDAALD LSHTQNIGMM LKQHFTSSQF
IVVSLKEGMF TNANVLFETK FIDGVSKVHR TVFNKKDKQV GKKK
