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Database: UniProt
Entry: H8MQX8_CORCM
LinkDB: H8MQX8_CORCM
Original site: H8MQX8_CORCM 
ID   H8MQX8_CORCM            Unreviewed;      1202 AA.
AC   H8MQX8;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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:AFE10357.1};
GN   OrderedLocusNames=COCOR_02529 {ECO:0000313|EMBL:AFE10357.1};
OS   Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS   (Myxococcus coralloides).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Corallococcus.
OX   NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE10357.1, ECO:0000313|Proteomes:UP000007587};
RN   [1] {ECO:0000313|EMBL:AFE10357.1, ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RX   PubMed=22582372; DOI=10.1128/JB.00397-12;
RA   Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA   Sogaard-Andersen L.;
RT   "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT   coralloides DSM 2259.";
RL   J. Bacteriol. 194:3012-3013(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RA   Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT   "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT   DSM 2259.";
RL   Submitted (MAR-2012) 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; CP003389; AFE10357.1; -; Genomic_DNA.
DR   RefSeq; WP_014395356.1; NC_017030.1.
DR   AlphaFoldDB; H8MQX8; -.
DR   STRING; 1144275.COCOR_02529; -.
DR   KEGG; ccx:COCOR_02529; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_7; -.
DR   InParanoid; H8MQX8; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000007587; 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   CDD; cd03278; ABC_SMC_barmotin; 1.
DR   Gene3D; 1.10.287.1490; -; 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   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:UP000007587}.
FT   DOMAIN          528..645
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          761..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          171..219
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          399..433
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          680..707
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          1003..1030
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        777..798
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1202 AA;  133724 MW;  D5F6AB5B09C017A4 CRC64;
     MRIKRLDITG FKSFMERSVF SFDEGVTGVV GPNGCGKSNV VDAIRWVMGE QSAKNLRGRG
     MEDVIFNGSE NKPPLSMAEV SLTFLVDDTD TLAPQYQGFS EITVTRRLFR NGDSEYLINK
     TLCRLLDITE LFLGTGVGTK AYSIIEQGRV GLIVSSKPED RRHLLEEAAG VTKYKARRKA
     AERKMEATEA NLLRVNDITG ELEKRLDTLS RQAKKAEKYR KLKARMREID LHSTSHRSLE
     LMAEKRVLQS RLENLGGEER EGLDKVKELE EVITRRRAEL DAEGAALQQY AGEVHALESA
     LQREAQELSY GRRDFEETGT RVASAQAELD ALLARQAEVV QTMTAREAEL SGIAGSYKED
     EVAMAVALEE QRRVSVLQTE ISLRLEQERA GLVAVATRLA NHESNLVNLA RQRTDLEARR
     AKLGGELEAL RVQEQELDAV RTQAAKHVED TRHLASELAE RRGQEEEALT RTREAFTENE
     VQVIALREEL SDKRSRLSSL EDIQKNYDGF DRGVRAVMVR AAEAAREQGI FGLVADVLTV
     TNARYERAVE AALGERLQHV IVDSREKGVE LVEYLKGHAE GRGTFLPVPS GEQARGYVEP
     DLSRPGVLAH ALKEVSCEPA LEPVLKLLLG DVVIVQDLVA AREYAESTPV PVTLVTLDGE
     VFRADGSITG GEREGAAVGA LQKKREIAEL AAEVARVEER YNEILTRHYT LQKQMGQAEA
     VLKGLGKEQH AEEVNLASQE KDLHKASEDL ARVRERLRSL EGEEGQLAQS HTALANEEES
     SRGEVAHGQA DREAREERVR QYAGELEGLR QRADTASSDL MGLRVKVAAG SERGESARKE
     LESLVAQRRD MEARVSRLQA TVTEGRAKVE TLQGRLAELE STKEQRAEEH RVAAEALEAR
     RTAHTTATAE VREQDTAFRE LRGRLDELMQ GLSQITLREK EIGLELEHLA AGIRERYQLE
     LSAELHNYHL LAPLSPEVES ELKDLRAQVE KMGEINLTAI DEHAELSKRF EFLSAQRQDL
     QASISQLKEA IVRIDATSRE RFKQTFDVVN DKFQAIFPRL FGGGRASLIL TQEGPNGEPG
     VEIVAQPPGK KLQSVNLLSG GEKALTAVAL IFGIFLIKPT PFCLLDEVDA PLDEGNVGRY
     NDMVKEMSRQ SQFILITHNK RTMEIADTLY GVTMEEPGIS KLVSVKMREA SAHNDDKVPA
     AS
//
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