ID J4TWM9_9FIRM Unreviewed; 1187 AA.
AC J4TWM9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:EJP30924.1};
GN ORFNames=HMPREF1147_1485 {ECO:0000313|EMBL:EJP30924.1};
OS Selenomonas sp. FOBRC9.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=936573 {ECO:0000313|EMBL:EJP30924.1, ECO:0000313|Proteomes:UP000006970};
RN [1] {ECO:0000313|EMBL:EJP30924.1, ECO:0000313|Proteomes:UP000006970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOBRC9 {ECO:0000313|EMBL:EJP30924.1,
RC ECO:0000313|Proteomes:UP000006970};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-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:EJP30924.1}.
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DR EMBL; ALJR01000033; EJP30924.1; -; Genomic_DNA.
DR RefSeq; WP_009658524.1; NZ_ALJR01000033.1.
DR AlphaFoldDB; J4TWM9; -.
DR PATRIC; fig|936573.3.peg.1697; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006970; 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; 2.
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}.
FT DOMAIN 522..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 262..345
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 423..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 736..763
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 841..903
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 987..1031
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; 134744 MW; 4799F9EA21059A72 CRC64;
MQLKRLEAYG FKSFADRIVV EFDRGITAVV GPNGSGKSNI TDAVRWVLGE QNIRMLRGLR
SEDIIFAGST ARRALSVAEV VLVFDNRDKT LPIDYEEVVV KRRLYRSGES EVYLNDARCR
IKDIYRLFAD TGIGHDGMSI IGQNRLNDIL DSRPEERRVF FEETAGITKY RTRKQEALRK
LSENDADLIR LSDIMYAQRA ELEPLAAQAE KTSAYRELEA ERCQYRLTSL VQTHEQLVGA
QENLMLLLHN DRDEEASLIG ERAQTEGKKR NIELEMEQID SDLAEIEKSD TELQNALDAL
KKESAMLLGR QDQCVRRKED LERLRESSRA KIEATEQEIV QIQNMLSGKI AAREEKEKAH
TEAQEQLKNI RTYRALYEEQ SARGSRSLRA VERVMVRLRE SLAVAADHSE RGDEGRLRRN
EELSQKKCRI IEAQSELSRM EAALQDLEQQ RDKCADDRVR LSHAVEEHRA KAQGIEEEMR
RTAEEIQRAQ QRYDFVRKLQ ESYEGFGKDV QMVLQAKEGW RSGVFGTVAD LISIPERYLT
AIEIALGGSV RNIITDDAQT AKAAIGCLKR RNGGRVTFLP LSSIVVQRPY DVDLCCVRGA
VGWANTLVSA EERFQRAVDH LLSRTLVMET LDDALAAAKE HGYRIRMVTL TGELLNPGGA
ISGGGQRHRQ SFLLNRRHEA ETLAETLRTQ KERHIAFQAD LEERNRLLHD DCTRRDAASA
EEAELNRDLL AARSQRDIYR TRLADQTAAV EDLERKERVA QESSARAARK KELLERHLAQ
CGDHARRFSK ETEEIAQKMT ALSSEEQSCA QGIHALEVES AALDAEIRTG TDHVKTRTLE
CREATEMLDG FTEQIAKLSE ELSAGEQRNA ALESAISEEE GKLRAHRDNA QILKDRRLRY
EADMRLLDDA IKRTIAYMEQ VRAKLHENDK QLDRINVRLA DCSENLISEF GMTAETAAQQ
ISPIDESVLN ERLNELTNAI NALGAVNPNA VEEYAEKKAR YEEEEAQIHD LQKAKEDIER
IIQKIDTDMT QTFREAFQQI QGYFNEIFMR LFGGGVAELR LTDQSDILSS GVEILVTLPH
KKRQNLSALS GGERALTVIA LLFSFLKYRP SPFSILDEID APLDEANVSR FGDFLQEFAH
NTQFIIVTHR KGTMRAADSM YGVTVEDAGV SKVLSIRLKD YEESATA
//
