ID A9A9R6_METM6 Unreviewed; 1189 AA.
AC A9A9R6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=MmarC6_1276 {ECO:0000313|EMBL:ABX02089.1};
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158 {ECO:0000313|EMBL:ABX02089.1};
RN [1] {ECO:0000313|EMBL:ABX02089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 {ECO:0000313|EMBL:ABX02089.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) 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; CP000867; ABX02089.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A9R6; -.
DR STRING; 444158.MmarC6_1276; -.
DR KEGG; mmx:MmarC6_1276; -.
DR eggNOG; arCOG00371; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR OrthoDB; 9143at2157; -.
DR PhylomeDB; A9A9R6; -.
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; 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; TIGR02169; SMC_prok_A; 1.
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; 2.
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 539..652
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 185..476
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 693..957
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 1189 AA; 137530 MW; B427CF268E982E80 CRC64;
MASLSEIHMK NFKSFKNSKL KIPDGFTAIL GPNGSGKSNT IDGICFVLGK TSAKSLRAGK
FNQLITYHNG KRESFAEVTL FFDNKDRKMP VESNKVGISR KVKINGDNNY YLIWDEEKEV
KENGEIKKIM EEKRKKVKKS EILDFIGKIS LSADGFNIIL QGDLIKIIDT TPNERRKIID
EISGVAEFDE KGEKAEKELE KAREFIEKID IRINEVKNNL EKLRKEKEDA EIYVKLSEEL
KATKYILTSK KIDFLNGVLE KTKEEIEALK EMKVCFLKEI SEYDVKSNNI RNRLQNLINE
LNEKGNEEIM ELHKSIKEME VTVDNDKKSL NGALDDLKNV NSQSEKKGQD LVETRQKIET
IRTETLQKEA EINTIKTEME NLEVEKKKLK SKVEESETQT ELLKQQERKI SERINESQNE
LYNLKNEFNS LENEINKKSF NLTKNKETIE TLQKELNDIK AESEDTKVLY KELEDVAVEL
EYSKKKVITL LEDKKEYQEK LDKSHADYIK ENAKIKAMKD MEDFSLDRAV KSVLEAKLPG
VVDIAGNLGK TDAEYKTAIE NAGGNRLNYI VVKRMDDGAR AIQYLKKNNL GRTTFLPLDR
INGPEALYLD DEGVVGRAID LVEFKPEYED LFRYIFGNTI IVENLDYAKI LSKDHRARFV
TLEGEVIEPS GAMIGGHSRK KSVIKVDIDT SRIEKLAEQI SELDNTLSET KDEIERLQNK
NATYSTRKME LESRLKIIRD MENRKEGILT NNGIKIKELE LESKKLEEEL DYLEGSKEEL
ERKINEYTKK ISGFTAQRDR ISEEISSFEN SEHSKRIKVI DETILNFEKK KNEFENEIKR
DAVLIKEVLI PKISELNSNI KELSEKRVIL EQNIQFYKNN VEKNFEILKN KKERYEELTK
DLRELTEKKE AFEKELEMLN GEKRRIYGRI NQNESQINSL SIDMAKYETR LEEEDRKLYV
CENIEHISED ITSKIKEFDV DALESHQIDL EGNIKKLEPI NMRAIDDYQY IVDRYDELFE
KRTDYENEEK KYLQLIEEVS KRKKEVFMDV YVRVAENYEK IYNEIGGSGK LSLENPDDPF
SGGLLIDASP MNKKLQSLDV MSGGEKSLTA LAFLFAIQHL NPAPFYVLDE VDAALDTKNA
GLIGEMIKNA SKNSQFIVIS HREQMISKSD VMYGVCMENG LSKLVGLKI
//
