GenomeNet

Database: UniProt
Entry: R7CSW9_9FIRM
LinkDB: R7CSW9_9FIRM
Original site: R7CSW9_9FIRM 
ID   R7CSW9_9FIRM            Unreviewed;      1178 AA.
AC   R7CSW9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=BN625_00050 {ECO:0000313|EMBL:CDD81095.1};
OS   Dialister sp. CAG:357.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister; environmental samples.
OX   NCBI_TaxID=1262869 {ECO:0000313|EMBL:CDD81095.1, ECO:0000313|Proteomes:UP000018365};
RN   [1] {ECO:0000313|EMBL:CDD81095.1, ECO:0000313|Proteomes:UP000018365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:357 {ECO:0000313|Proteomes:UP000018365};
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:CDD81095.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBHT010000192; CDD81095.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7CSW9; -.
DR   STRING; 1262869.BN625_00050; -.
DR   Proteomes; UP000018365; 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:UP000018365}.
FT   DOMAIN          522..640
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          313..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..275
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          989..1019
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        825..856
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   1178 AA;  133488 MW;  A80022CEFED0BADB CRC64;
     MKLLRLILQG FKSFADKTTI EFADGMTVIV GPNGCGKSNI SDAVRWVLGE QNVRNLRGQK
     SEDIIFAGSE SRTRKNGAEV TLVLDNSNRE LPLDTAEVSI TRRILRNGDS DFQINKRNCR
     LKDIHELLAN TGLGKGSLAI IGQNRVDEVL TAKPEERRAI FEDVAGISLY RMRKNEGLQK
     LVKTAENMDR VKDMMAMLDE QTGPMKEKAE KAKAYKALAA EKRAVQATMS ALKLDSIKES
     LEKHKAETET LEQDSVKWKA ELTKAAAALA KLEQETLLHQ EKVKKAGTDF AEAKEKLDGI
     RVDYKIKEEA LEQEKKRTEE LKEDEEDQKE AEEELIEEIQ NDEEEMKAAE AEKADWLAKQ
     NQAEAEKEKL AGELEASEKA YSEILNFSRQ KMAEKQKLEQ GLAYLDNEVR RLKGESSRRE
     EAAKSIEGEL QKTNEALASL LAEEKEAMAR QEQLKEEGIR DRKALDEARN ECFSIGNELN
     EAESSFRTIH SRREYLEKAD KEYASFSRTT KTVMENRAIF GDAVHGALGE LIHVPSEYTA
     AAEVALGSQI SNIVTDTTKS AGDIIRWLKE KNLGRATFYP LESMKPSSYS GREQEASREE
     GILGIAADLF ETDSLYQDLL HSLLGRTLIA KDLDAARRVS KKYGYRLRIV TLDGQIVNAG
     GSMTGGSMKK KENTYFGRKE EIKELYAEEK KREKDLADLR KRKQEKETAR DSLSEKVAGE
     RESWHQMDLA LASFKGQKDG LEKTKTDQET RLKEGKDALA SISESLEKSV QQMTEGWELL
     KTYEDIPEPG KDEKSLAIRK QIDDKAGELI AIREGLTKAE SRASFAKRMM NDAKKAQEDQ
     KKDREDLENK KKANEEAKKN LAETLEKLNQ DFEEANGKWE SIRTKQESLQ GETDRYAALE
     RDSQAAWRKA QEKSSSVEKD LADKKARLER FKEEEAEELQ KISEEGMTRE EVETLKLPGT
     LNEMKNRDKV LAGKIADLGT VNPAGEEEYE EHLKKRNFYE EQINDMRGAE EELRTVIKDI
     DEKMASQFDE AFTKVNQEFG RIMQIMFQGG SAKLELTDPE HPLECGVEMY LQLPGKKRQP
     LTLMSGGERA LTVIALLISF MAYRPAPFCF VDEIDAALDD SNVDRYSRMI AEYKKKTQFI
     VISHRKRTME FADTLQGVTM GEKGVSSLVT VKMKDYVE
//
DBGET integrated database retrieval system