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Database: UniProt
Entry: R6CU54_9CLOT
LinkDB: R6CU54_9CLOT
Original site: R6CU54_9CLOT 
ID   R6CU54_9CLOT            Unreviewed;      1202 AA.
AC   R6CU54;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=BN687_00838 {ECO:0000313|EMBL:CDA68857.1};
OS   Clostridium sp. CAG:510.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262816 {ECO:0000313|EMBL:CDA68857.1, ECO:0000313|Proteomes:UP000018120};
RN   [1] {ECO:0000313|EMBL:CDA68857.1, ECO:0000313|Proteomes:UP000018120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:510 {ECO:0000313|Proteomes:UP000018120};
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:CDA68857.1}.
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DR   EMBL; CBCI010000077; CDA68857.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6CU54; -.
DR   STRING; 1262816.BN687_00838; -.
DR   Proteomes; UP000018120; 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; 1.10.287.1490; -; 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.
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:UP000018120}.
FT   DOMAIN          537..654
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          197..224
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          264..340
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          369..403
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          439..515
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          695..792
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          849..953
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1202 AA;  136889 MW;  200BB239A26610FD CRC64;
     MKRCLASENR AKEDRGMYLK SIEVYGFKSF ANKITFQFHN GITGIVGPNG SGKSNVADAV
     RWVLGEQRIK QLRGSSMQDV IFSGTEARKP LSYAYVAITL DNSDHQLAID FDEVTVARRI
     YRSGESEYLI NGAACRLKDV NELFYDTGIG KEGYSIIGQG QIDKILSGKP EERRELFDEA
     AGIVKFKRRK FAAQKKLEDE KANLVRVNDI LSELEKQVKP LEKQSETAKI YLKKKEELKV
     LDANTFLLES EQVKTQLADV QGKYDIASKD YEETSEKYEG IRQEYEAIQS RIETLEKEIE
     EARNNLTDTS VLRGKLEGEI NVLKEQIHSA TDNAAHLQTR KVNLNSQIAQ KDTEKQEILA
     KKAEIDEQVT ELTATRDEVK ISLESLQNRI QELNDSIEAG KNTIIDELNQ RATIKSKIGR
     FDTMLEQVAI RKAELNSRIL KAKSDEEDRE ENIKKLKEQF TAVSDALKEM KEKAEKDEAD
     IQKIRGELTG KDVKLRETQE QYHQEKSRLE ALSNLTERYE GYGGSVKKVM EQKNDNKGII
     GVVADIIKVD KKYETAIETA LGGNIQNIVT DDEETAKKMI GFLKKNRLGR ATFLPLTSIK
     NPQEFKNPEA LKEKGVVGMA DELVRTETRY KDVAKAMLGR IVVVDNVDNA VKIARKFDYG
     IRMVTIEGEL LVPGGAISGG AFKNNSNLLG RRREMEDLEK KIKDLLSSIE TIQKDIEETK
     QKRNTMRMEL EALKADIQRK FIEQNTARLS VESAEERMEE AEAGSRSLME ELKEMEKQVL
     EIKQGKEEIQ KELTGSEEME KSVEAGISEF QKELEEKRLL ETESSAKVSE WELKVEKMLQ
     TQGFHQQNVD RINAEIENLK GELSEIEDGI AGNEESLKEK KEHIAEIEKT IEASHTSQDK
     SQKELTENIA KKEELSAKQK NFFTEREELS QQMTRLDKEV YRLNAQKEKM EEAMETQINY
     MWDEYELTLS DAASLRKEEL TDLGSMKKEI SAIKDQIKKL GDVNVNAIED YKNLMERYTF
     LKTQHDDLIE AEKTLEGIIT ELDSAMRKQF QEKFAEINKE FDKVFKELFG GGRGTLELME
     DEDILEAGIR IIAQPPGKKL QNMMQLSGGE KALTAISLLF AIQNLKPSPF CLLDEIEAAL
     DESNVGRFAK YLHKLTKNTQ FIVITHRRGT MEKADRLYGI TMQEKGVSAL VSVNLIDKDL
     DN
//
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