ID E6U7X4_ETHHY Unreviewed; 1193 AA.
AC E6U7X4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Ethha_0320 {ECO:0000313|EMBL:ADU25906.1};
OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS YUAN-3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ethanoligenens.
OX NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU25906.1, ECO:0000313|Proteomes:UP000001551};
RN [1] {ECO:0000313|EMBL:ADU25906.1, ECO:0000313|Proteomes:UP000001551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC {ECO:0000313|Proteomes:UP000001551};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT "Complete sequence of Ethanoligenens harbinense YUAN-3.";
RL Submitted (DEC-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}.
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DR EMBL; CP002400; ADU25906.1; -; Genomic_DNA.
DR RefSeq; WP_013484287.1; NZ_CP025286.1.
DR AlphaFoldDB; E6U7X4; -.
DR STRING; 663278.Ethha_0320; -.
DR KEGG; eha:Ethha_0320; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000001551; 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 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; 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:UP000001551}.
FT DOMAIN 523..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 339..373
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 673..798
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 827..945
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 315..334
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 1193 AA; 132209 MW; 0B71DF94319FF5D7 CRC64;
MYLKSLTIQG FKSFPDKTVL TFGPGITAVV GPNGSGKSNI SDAIRWVLGE MSVKSLRGGK
MEDVIFGGTP VRRPLGYAEV SLTVDNSDHA LPVESEEVTV TRRYYRSGES EYRLGGAQVR
LRDIYELFMD TGLGHDGYAV ISQGRIAEIV GARSEDRREI FEEAAGIAKF RFRKAEAERR
LASTEENLVR LRDILSELEA RVGPLKEQAE KAKRYLTLAE EKRTLEVGLW LHLLDVRREE
LRAGENKLEI ARARHDELER KLDTVERTID EAYMQGQKAA AEADRLRGEA AAREQEAVQC
EAQAALCEGD AARADRTRAE VEEEHARNER SGSEDESGLA ALQTELNEKQ DALVGLRETL
EACECDVRAL TEEGDAQAAK TREASARLAQ VRARLAGLGQ RKSAAQAAAE SAAARVEEIG
LSAADRERRR EQAATMLVDA QARLVKARET VQALENAVQG CTLKQDARRQ KLAKEQERVR
ALSLRAGERA QRAAMLAEME KNLEGFAHSV KLVVRESRRG SLRGILGPVS QLLSAPAEVA
VAVETALGAS AQHIVVENEE NAKDAIRFLQ RAEGGRATFL PLTSVRGGLL DAREIAGCAG
YVGIASELVS FEERFREVAE HLLGRTVVAR DLDSAVTMAK RFRYRFRIVT LDGQQVNAGG
SLTGGSRRAG AGLVSRQAEI TRLEEEARVL QAQLAEAEQA ERRAKESLAA VEAEANGARG
EQARAKEAAI RLEGEEKRLA EQADLLGADM RSLEEERRAC MDKTAALRAQ AQAVEEQMAA
CEQEAEQAEQ ALAACGVEGE ALAAKREEQT ARLTDIRLRQ LGGEKDVQAV KQRIEALEAH
RSEKKAHAET LALRMHTLEE EAREARERAQ AQTAQAEVLR AKAADCRREA EQRAGEREDL
ERRTVELRAG SRALAEEKEN MSRELARLEE RKVTLQNSYD ALIAKLWEEY ELTRSQAEKE
VPRVERPDEA EKRLNTLRHD IKALGSVNLA AIDEYREVEE RYTFMKTQTD DVERSKAELE
TLIRGLTGEM RAQFSKKFAE INGHFASIFV ELFGGGRAWL ELTDPQDVLG CGIEIHVQPP
GKIIKNLASL SGGEQAFVAI ALYFALLKVR PSPFCVLDEI EAALDEQNVV RYASYLRRLC
GSTQFIVITH RRGTMDEADI LYGVTMQDQG VSKLLTLHLD ELMERLGLEQ KRG
//
