ID D4KN00_9FIRM Unreviewed; 1186 AA.
AC D4KN00;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=ROI_10540 {ECO:0000313|EMBL:CBL08252.1};
OS Roseburia intestinalis M50/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=657315 {ECO:0000313|EMBL:CBL08252.1, ECO:0000313|Proteomes:UP000008807};
RN [1] {ECO:0000313|EMBL:CBL08252.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL08252.1,
RC ECO:0000313|Proteomes:UP000008807};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Roseburia intestinalis M50/1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL08252.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL08252.1,
RC ECO:0000313|Proteomes:UP000008807};
RA Pajon A.;
RL Submitted (MAR-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; FP929049; CBL08252.1; -; Genomic_DNA.
DR AlphaFoldDB; D4KN00; -.
DR KEGG; rim:ROI_10540; -.
DR PATRIC; fig|657315.3.peg.2144; -.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000008807; 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 CDD; cd03278; ABC_SMC_barmotin; 2.
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.
DR SUPFAM; SSF57997; Tropomyosin; 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 521..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 255..317
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 346..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 430..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 672..713
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 749..811
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 851..937
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; 135460 MW; 71E1E402EC898EAE CRC64;
MYLKSIEVQG FKSFANKIVF DFHNGITGIV GPNGSGKSNV GDAVRWVLGE QSAKQLRGAS
MQDIIFAGTE NRKPLSYAYV AITLDNADHK LPVDYEEVTV ARRVYRSGES EYLLNGNTCR
LKDVTELFYD TGIGKEGYSI IGQGQIEKIL NGKPEERREL FDEAAGIVKY KKRKATAQKK
LENERENLVR VNDILSELER QVGPLEKQAE KARVYLKKKE ELKTYDVNMF LMEMTRIDGQ
LHEVGEKCGI AEAQLHESKD SYEQVKTEYE RMESEIEQLE QAIGEVRENL SGSTVLKGKL
EGQINVLKEQ IHTAEMTDEH LKDRLDSIEK DTQDRLAQKD VYGREREELL EALAGISERK
QAAEKELDEL RNGMKECSDG IEHGKSEIIE LLNNKASVKA RQQRFDTMAE QINIRKAKLT
QRLLARKTEE EDLDNVLAAY QQELDDVNET IRELKESAAA MEEKNREWRR KYSQTSQQLE
QDVTRYHKEQ SRLETLKNIA ERYDGYGNSI RRVMEQKDRH KGILGVVSDL IQVEKKYEVA
IETALGGSIQ NIVTEDEETA KQMIAYLKQN RYGRATFLPL TSVNGSGGFK NQEALRERGV
IGLASTLVKN DARYDGVTNY LLGRVVVAET IDDAIALARK YRYSFRIVTL EGECLNPGGS
MTGGAFKNTS NLLARRREVE ELETLVASLQ SQIKESRDRL EDIKTAQSLL EEDMESGKEK
LQEQYILQNT AKMNLDRATE QKNERETVFA GLHAERAEIE EQLAELENNK AQIAAEIEAA
AVREKEIGQE NEDFQKRFEE YQTKEKEAAE TVSKIALEEA GIRQKAEFAQ SNISRIQSEI
TRFSQDRETL ITQAGDAKEE AKQKMAEIEE LKKTILASDD THAAFEQQLK DYTQKKEELS
ASHKGFFRKR EEISNQISEL DKEVFRLNSQ REKLNDAREY QTNYMWQEYE LTLHAAMDLR
DDTYDDLSTL KKMIAQIKDE IRKLGDVNVN AIEDYKEISE RYQFLKTQHD DLIEAEKTLI
GIIEELDTGM RKQFMEKFAE IQKQFDTVFK ELFGGGKGTL ELVEDEDILE CGIRIIAQPP
GKKLQNMMQM SGGEKSLTAI ALLFAIQNLK PSPFCLLDEI EAALDDSNVT RFAKYLHKLT
QNTQFIVITH RRGTMAAADR LYGITMQEKG VSTLVSVNLI ENDLDK
//
