ID C9LW80_SELS3 Unreviewed; 1181 AA.
AC C9LW80;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:EEX76883.1};
GN OrderedLocusNames=Selsp_0898 {ECO:0000313|EMBL:AEB99862.1};
GN ORFNames=SELSPUOL_01734 {ECO:0000313|EMBL:EEX76883.1};
OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX76883.1, ECO:0000313|Proteomes:UP000003505};
RN [1] {ECO:0000313|EMBL:EEX76883.1, ECO:0000313|Proteomes:UP000003505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX76883.1}, and ATCC 35185 / DSM
RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000003505};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEB99862.1, ECO:0000313|Proteomes:UP000011124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEB99862.1}, and ATCC 35185 / DSM
RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000011124};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Selenomonas sputigena DSM 20758.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; CP002637; AEB99862.1; -; Genomic_DNA.
DR EMBL; ACKP02000040; EEX76883.1; -; Genomic_DNA.
DR RefSeq; WP_006193028.1; NZ_GG698597.1.
DR AlphaFoldDB; C9LW80; -.
DR STRING; 546271.Selsp_0898; -.
DR KEGG; ssg:Selsp_0898; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000003505; Unassembled WGS sequence.
DR Proteomes; UP000011124; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
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 HAMAP; MF_01894; Smc_prok; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000011124}.
FT DOMAIN 521..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 441..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..316
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 366..393
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1181 AA; 133750 MW; 1BFB0F73034D9A74 CRC64;
MQLKRLEAYG FKSFADKIEI EFHAGVTAIV GPNGSGKSNV TDAVRWVLGE QNVRALRGSK
AEDIIFTGSA TRRAMGVAEV SLFFENEGDM PVDYREVVVT RRLFRSGESE FFINKSRCRL
KDISNLFADT GLGRDGMSVI GQNRIDEILN SKPEERRLYF EETAGITKYR NRKRESMRKL
EDMQGNLVRV SDIMQEIEGQ LEPLAESAEK TRRHDDLQTV YRRCALTELF QREGQLKKER
ADSAGKIEAM RDEALAAETQ VRLLDVKKEE LDQAILVLEE KLQEQAEKNN ALRTQIEQAN
SEIAILEERA HQHDALKARL LQQRADFEST AGEAAAEKQR LFAVEKELLE KHAAIDAAIA
KDRGSLKALG EKLREVKEKH RTLADKKDAA QRDMLARENE LLLIEHELER YSTSGTERAD
ELERATAAVD ALTTEAKAIG EERRRLEEER RTLEEERTKK TQEKEHLDEK LRTLLHAENR
TKEELHADEN KLKFLRNMQA SYEGFARAPK AVLQAKEPWQ KGVAGAVAEL VSVPHEYIRA
VDVALGSSLQ NIVTEDTDTA KAAIAFLKRA RLGRVTFLPL STLVVRRSQD EAAKREVGAI
GFANELVGAD AKYRKVVDFL LARTLVVDTL DHGLAIEKKM GWRLRIVTLD GELLNPGGSL
SGGGRQGQET SFLNRGGEIE RLEKSVRDAE ETLATLLKAR TFFDKAAREM AEALEFVARS
LQQKDVYAAE LRVKDERIAE ARKEKEKARE TLKKLAEEAE MTFSKAQAKK NDAVQQAKAA
RRLYEKMERE TKESEEELDD LEQDADDLSK YINERELKRA VLEQEKIRAR EQALLKEKEE
TRAKEQAEKT REEEIALDEE QSNGGTKREE IAARVAAWQE KHAEGKAAYD KQYQEKLERH
AENQENDKAA RAVGQRLSEM QGKLHQMEIA AAEVHVKIEQ VQAELLEQYG HTWETAAEEA
LDLTGTELKK KMQDISRALA ELGPVNPNAI REHEELVERH EFMGKQAADL EAARENLMAM
IHEMDVTMTR QFKAAFEEIR GYFADIFVRL FGGGKAELFL TDEKDVLHAG VEIEVQLPTK
KRQNLSVLSG GERALTVIAL LFSFLRYRPA PFSVLDEIDA PLDEANVARF GKFLGEFAEN
TQFIVVTHRK GTMEAADFMY GITIEDAGVS RVLSVRLDEA I
//
