ID   SMC_METVO               Reviewed;        1199 AA.
AC   Q69GZ5;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894};
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RA   Feldman R., Overbeek R., Whitman W.;
RT   "Chromosomal segregation protein SMC.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=15186409; DOI=10.1111/j.1365-2958.2004.04084.x;
RA   Long S.W., Faguy D.M.;
RT   "Anucleate and titan cell phenotypes caused by insertional inactivation of
RT   the structural maintenance of chromosomes (smc) gene in the archaeon
RT   Methanococcus voltae.";
RL   Mol. Microbiol. 52:1567-1577(2004).
CC   -!- FUNCTION: Required for chromosome condensation and partitioning.
CC       {ECO:0000255|HAMAP-Rule:MF_01894, ECO:0000269|PubMed:15186409}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC       near the middle of the molecule. These domains are separated by coiled-
CC       coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- DISRUPTION PHENOTYPE: Mutants show a high rate of anucleate cell
CC       production and a subset of cells that is extremely enlarged with
CC       irregular morphology. {ECO:0000269|PubMed:15186409}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01894}.
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DR   EMBL; AY288521; AAQ22369.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69GZ5; -.
DR   SMR; Q69GZ5; -.
DR   PRIDE; Q69GZ5; -.
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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..1199
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409286"
FT   DOMAIN          546..658
FT                   /note="SMC hinge"
FT   COILED          192..528
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          691..1051
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1199 AA;  137830 MW;  6BB179C2979CAA1D CRC64;
     MISISEIHLK NFKSFKNTKL KIPDGFTAIL GPNGSGKSNT IDGICFVLGK TSAKSLRAGK
     FNQLITYHNG KRADYAEVTL FFDNINREIP IDSDKVGICR KVKLNGDNNY YVVWYEVEKQ
     NTKINTESSQ KKTSKASKVE KRRRMKKNEV LDLLSKISLI ADGPNIILQG DLLRIIDTSP
     NERRKILDEV SGVAEFDEKS EKAKKELSQA REYIEKIDIR INEVRANLEK LKKEKEDAEK
     YTVYNKKLKV TKYILTSKKV EFLKMVLDET KDEIEALKET KNCYIQDISN IDSEIIGLKV
     KINELVNELN EKGSEEVMEL HKSIKELEVN LNNDKNALEN AIDDLKHTLK MEESKNNDLN
     ETKEKINNIR IDTLKKEAEA KVLIKEIEKL NEERQNLEKK VEQSESQVKA LKNQESKLSE
     RINDTQKELY GLKNELNQLE NTLNNRTFDY QKNNETIENL TNQIAEFSDL EDTKKLYKEL
     EDIAVELEFS KKKLQEKITE RNDSQSKLDN LHSEYVKENA RIKTLKDMEN FSLDRAVKGV
     LDAKLPGVVD IAGNLAKTKG EYKTAIEVAG GARLNHIVVK KMDDGSRAIN YLKQKRLGRA
     TFLPMDRIKG MDAKDISDTG IIGKAIDLVE FDIKYTNVFK FIFGNTHIVD NLENAKKLSL
     KYKARFVTLE GEVIEPSGAM VGGNIRRNSA IKVDIDMKKL TNLSEDIKEL EQILSNVKDE
     IERLNNKINT CSTRKLELDN RLKIARDQEF KKEEITKSNN LKIKELNMLN SKIDDEISEL
     TDEKEILSQK VQNLDNKLSE VMGQRERIVN EIKSYENSEL SKRIKEIDHK IRENESSKNT
     LENEIKKGAI LVKEVLIPKI SELNSNIKSL ADKKNMFKNS VEIYKSNIES NSSILSDKRG
     KYEELTKGLK DLTDKKECYE LEIENLQNNK EELREKATDI DNQVNVINVD RAKYETRLEE
     EERKLYLCDT LENIEDISDE MIEETYSLEI DDLERNQALL ESSIKKLEPV NMRAIEDYDF
     INERYEELFG KRKEYEQEEG KYLQLISEVQ KRKKETFMKT YDRVAENYEQ IYGEIGGNGK
     LSLENEEDPF SGGLLIDASP MNKQLQNLDV MSGGEKSLTA LAFLFAIQRL NPSPFYVLDE
     VDAALDTKNA SLIGDMISNA SKESQFIVIS HREQMISKSN VMYGVCMENG LSKIVSVKL