ID E7MZN8_9FIRM Unreviewed; 1050 AA.
AC E7MZN8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HMPREF9555_00180 {ECO:0000313|EMBL:EFW30552.1};
OS Selenomonas artemidis F0399.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW30552.1, ECO:0000313|Proteomes:UP000004633};
RN [1] {ECO:0000313|EMBL:EFW30552.1, ECO:0000313|Proteomes:UP000004633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0399 {ECO:0000313|EMBL:EFW30552.1,
RC ECO:0000313|Proteomes:UP000004633};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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:EFW30552.1}.
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; AECV01000001; EFW30552.1; -; Genomic_DNA.
DR AlphaFoldDB; E7MZN8; -.
DR STRING; 749551.HMPREF9555_00180; -.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000004633; 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; 6.10.140.1720; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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}.
FT DOMAIN 385..501
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 125..243
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 286..362
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 599..626
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 704..766
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 850..894
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1050 AA; 119414 MW; 0884716BCDDA7226 CRC64;
MSIIGQNRLN DILDSRPEER RVFFEETAGI TKYRTRKQEA LRKLRENDAD LIRLSDIMYA
QRAELEPLAA QAEKTSAYRE LEAERRQYRL TSLVQTHEQL VGAQENLMRL LHNDRDEEAS
LIGERAQTEG KKRNIELEME QIDSDLAEIE KSDTELQNAL DALKKESAML LGRQDQCVRR
KEDLERLRES SRAKIEATEQ EIVQIQNMLS GKIAAREEKE KAHTEAQEQL KNIRTHRALY
EEQSARGSRS LRAVERVMVR LRESLAVAAD HSERGDEGRL RRSEELSQKK CRIIEAQSEL
SRMEAALQDL EQQRDKCADD RVRLSHAVEE HRAKAQGIEE EMRRTAEEIQ RAQQRYDFVR
KLQESYEGFG KDVQMVLQAK EGWRSGVFGT VADLISIPER YLTAIEIALG GSVRNIITDD
AQTAKAAIGC LKRRNGGRVT FLPLSSIVVQ RPYDVDLCRV RGAVGWANTL VSAEERFQRA
VDHLLSRTLV METLDDALAA AKEHGYRIRM VTLTGELLNP GGAISGGGQR YRQSFLLNRR
HEAETLAETL RTQKERHIAF QADLEERNRL LDDDCTRRDA ASAEETELNR DLLAARSQRD
IYRTRLADQT AAVEDLERRE RVAQESSARA ARKKELLERH LAQCGDHARR FSKETEEIAQ
KMTALSSEEQ SCAQGLHALE VESAALDAEI RTGTDHVKTR TLECREATEM LDGFTEQIAK
LSEELSAGEQ RNAALESAIS EEEGKLRAHR DNAQILKDRR LRYEADMRLL DDAIKRTIAC
TEQVRAKLHE NDKQLDRINV RLADCSENLI SEFGMTAETA AQQISPIDES VLNERLNELT
NAINALGAVN PNAVEEYAEK KARYEEEEAQ IHDLQKAKED IERIIQKIDT DMTQTFREAF
QQIQGYFNEI FMRLFGGGVA ELRLTDQSDI LSSGVEILVT LPHKKRQNLS ALSGGERALT
VIALLFSFLK YRPSPFSILD EIDAPLDEAN VSRFGDFLQE FAHNTQFIIV THRKGTMRAA
DSMYGVTVED AGVSKVLSIR LKDYEESATA
//
