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Database: UniProt
Entry: R6WBY1_9FIRM
LinkDB: R6WBY1_9FIRM
Original site: R6WBY1_9FIRM 
ID   R6WBY1_9FIRM            Unreviewed;      1186 AA.
AC   R6WBY1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=BN605_01939 {ECO:0000313|EMBL:CDD08583.1};
OS   Dorea sp. CAG:317.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1262873 {ECO:0000313|EMBL:CDD08583.1, ECO:0000313|Proteomes:UP000018262};
RN   [1] {ECO:0000313|EMBL:CDD08583.1, ECO:0000313|Proteomes:UP000018262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:317 {ECO:0000313|Proteomes:UP000018262};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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}.
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:CDD08583.1}.
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DR   EMBL; CBGJ010000112; CDD08583.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6WBY1; -.
DR   STRING; 1262873.BN605_01939; -.
DR   Proteomes; UP000018262; 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   CDD; cd03278; ABC_SMC_barmotin; 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:UP000018262}.
FT   DOMAIN          521..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          248..366
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          402..478
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          672..769
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          833..937
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          1005..1032
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   1186 AA;  136293 MW;  FBF63F7218EC2009 CRC64;
     MYLKSIEVQG FKSFAHKLKF DFHNGITGIV GPNGSGKSNV ADAVRWVLGE QRVKQLRGGT
     MQDVIFSGTE NRKPLSYASV AITLDNSDHQ LPIDYEEVTV ARKLYRSGES EYLINGSTCR
     LKDVNELFYD TGIGKEGYSI IGQGQIDKIL SGKPEERREL FDEAAGIVKF KRRKLLSVKK
     LEEERQNLLR VNDILAELEK QIGPLERQSE KAKEYLKKKE SLKTYDINMF LLETERIREL
     LKSTEGKLAL TQEELSEAGI RYEDMKQEYE AVEEQVDTID ESIEHAKNQL NETTMLKQQL
     ENKIALLKEQ INSAHMNDEH YAQRALTIQS ETGTREQQLK ELGKERESLQ TELKERKAVE
     DAAREELIEV QSRIAALSDG IEKNKSDIIE LLNNRASTKA KIQKYDTMLE QIQVRKAQIN
     QRILEARSEV ELQNEEKNKY TGELQNISDQ IIRLSDEHHA YEKKIEDIQR ILAKETEKFR
     IGQTAYHREQ SRLESLKNIT ERYDGYGNSI RRVMDNKKQE PGLLGVVADI VKVEKEYEVA
     VETALGGSIQ NIVTEDEDTA KRMIQFLKKN KFGRATFLPL TSIQSYGAFH KPEALKENGV
     IGIASTLVNV DAKYRDLAGY LLGRTLVVDH IDHGTAIARK YKQTIRIVTL EGELINPGGS
     MTGGAFKNSS NLLSRRREIE EFEKTVKQLK SEMDQLEEYC NGLRKERAGY YEEIESLKEK
     LQKAYVIQNT AKMNVDQAEG RIRSIFNTLE DIESEAENLD RQITDIVDNQ ESITVELDTS
     EHLEEELSGK IDNEQSILEK ERELEAEKQK TVEEIHLVSA GLEQKEAFVV ENVTRIRDEL
     EKFAQEMKEL EESKSGTSKE IEEKEEQIAD LRQTIENSKE LFTEIQQEIE KFKKDREMLN
     QQHKTFLQKR EELSKHMSQL DKEVFRLESQ KEGYEEASEK QINYMWEEYE ITYNHALELR
     DENLTDLSKM KKRISELKGE IRSLGDVNVN AIEDYKNVSE RYEFLKTQHD DLVEAEATLE
     QIIEELDAAM RKQFKEQFAK ICSEFDTVFK ELFGGGKGTL ELMEDEDILE AGIRIIAQPP
     GKKLQNMMQL SGGEKALTAI ALLFAIQNLK PSPFCLLDEI EAALDDNNVT RFAKYLHKLT
     KYTQFIVITH RRGTMTAADR LYGITMQEKG VSTLVSVSLL EDELDA
//
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