ID S7TJE5_DESML Unreviewed; 1187 AA.
AC S7TJE5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=dsmv_3066 {ECO:0000313|EMBL:EPR37292.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR37292.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR37292.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR37292.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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}.
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:EPR37292.1}.
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DR EMBL; ATHJ01000103; EPR37292.1; -; Genomic_DNA.
DR AlphaFoldDB; S7TJE5; -.
DR STRING; 897.B2D07_06015; -.
DR PATRIC; fig|1121405.3.peg.3157; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000014977; Unassembled WGS sequence.
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:UP000014977}.
FT DOMAIN 523..634
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 265..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 668..793
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 864..898
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 1187 AA; 133995 MW; E0B3B31921C46237 CRC64;
MRLKKMELVG FKSFGEKSVI AFPPGISAIV GPNGCGKSNI VDALRWAMGE MSVKQLRGKS
MEDIIFAGAN GRPPMNLAEV SLTLSNENGT APEAFKHFSE IMLTRRLYRS GESLYMINRQ
PCRLKDIHNI FLGSGMGAKS YAVIQQGNIG AITDAGPEER RFFIEEAAGV TRYKQRKKET
LRKLDATHQN LLRVRDIVSE VERQMKGLDR QARKAEQYRK YQEKIRILDL HLSITAYDGY
SERIKQNDDR LRGLKDADIA YTTRLNRLNA AVEEIKLRRS RKNQEISTQR SHKFELQRRI
DRAESDLSHR KNEIDRLIQE AVNLRKLYGE LASKNQKIIE ERTTVDQHNQ ALREEIAQIK
DLLTQEEKGA LAVRNRLAEL REAEARCKNH LMTVVGEEAK FQNICRNALH NQEHLKRRLR
KIDEDEALAS SRLKEIETQA TRIQESLSLS RSEIGSRDQR ILEIRACIDA GNRTLSDQVK
RVQALEYDRH HTHSRHAALK KMAENYEWYR DGVKTIMTGA DPSEILGLIA DVIDPSAGVI
PAIEAVLGEA LEYVLVRDAE VGGAAIDRLR EENAGRGGFV PVAALRQPDS CLPGETPNLL
LNHLKAKSGF EDVVHSLLGN VVLTDSLEAA IESHRRNGNG ATFVTREGDV VSHHGVMIGG
SSDRLSGILM KKQEMSALEG RLTELNDALA DARTVQETLE IRVRDLEKNL HLETEEKNEA
VKAAFEAEKS LIKVTETLKH AGQTLERLRM EQDQLLEESD HIDEEMRRCH TALSRTTEAV
KAAQAEVVDI ERDTAAVSSD FEGVEARIVD VKLRLTARTA AMENGLNAAR RLKEFQADGD
IRLEQLLKDI EIKEGKRREM KAGLATLESS LQGLHEEIRR LDEVLKSSEA DYEETEALLR
ARGDLISEVQ GLRNETVDKI RTIEMEQSQL HIKRETVESR VAERYQRPLA AFRPELADLD
LGRGMTVDET AAALEELRRK LERIGDVHLG AIDEYKALTE RHEFLKTQQA DLVKAVDDLH
KVIRKINRVS QDKFLDTFAR INEKLEEVFP RLFSGGSARL ILTEPNDPLE TGVEFMVHPP
GKKLTRLTLL SGGEKALSAI AFVFSIFLIK PASFCIMDEI DAPLDEANVY RFNELLRIIG
ENSQIIMITH KKKSMEFADT LFGITMEQKG VSRIVSVNLE GQAAPFN
//
