ID M0E9D8_9EURY Unreviewed; 1193 AA.
AC M0E9D8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=C463_10365 {ECO:0000313|EMBL:ELZ42999.1};
OS Halorubrum californiense DSM 19288.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227465 {ECO:0000313|EMBL:ELZ42999.1, ECO:0000313|Proteomes:UP000011586};
RN [1] {ECO:0000313|EMBL:ELZ42999.1, ECO:0000313|Proteomes:UP000011586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19288 {ECO:0000313|EMBL:ELZ42999.1,
RC ECO:0000313|Proteomes:UP000011586};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ42999.1}.
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DR EMBL; AOJK01000050; ELZ42999.1; -; Genomic_DNA.
DR RefSeq; WP_008443377.1; NZ_AOJK01000050.1.
DR AlphaFoldDB; M0E9D8; -.
DR STRING; 1227465.C463_10365; -.
DR PATRIC; fig|1227465.4.peg.2033; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000011586; 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 Gene3D; 1.10.287.1490; -; 2.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 1.20.5.170; -; 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; 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 542..656
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..937
FT /note="Disordered"
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; 132924 MW; AFD4327ACFAE0E0E CRC64;
MHITEVVLDG FKSFGRTTRI PFYEDFTVVT GPNGSGKSNI IDGVLFALGL ARTRGIRAQK
LTDLIYNPGH DDGEAADGPN EASVTVVLSN EDGTLDRSQV VSAAGTENVG DVSEITIKRR
VKETEDNYYS YYYLNGRSVN LSDVQDLLAA AGVTPEGYNV VMQGDVTEII NMTPYQRRGI
IDEIAGVAEF DEKKEAAYEE LDTVEDRIGE ADLRIGEKQD RLDQLADERE TALQYQEFRD
ELEEYRGFRK ASELEEKRDA LADVEGDIDE SEADLDELRE ELDARQGKLT RLEEDLADLN
HEIETKGEDE QIRIRSEIEE VKGEASRLED KIESAESRAE SAETDRREAF VQIDRKEEKV
EEIDGEIREA KVEKASVKSE LATKRSELAD VEAEIEGADT EFDELKSDLA EKKAAIEALR
EEKNETQREK DRLLDEARRR SNAVSEAREE LEAARESLPE HKARISELKS ELDKAEKNQA
TIEDAVADLF AEKAEKEERL EEIEATLREK QNEYAKLEAA ADERGDASWP RAVTEVKNGG
IDGVHGAVGE LGSVEAQYAE ACETAAGGRL ANVVVDDDGV GSTCIDYLKQ RNAGRATFLP
ITKMDDRSLP RKPSLPGVVD FARNLVDYDA EYDSIFSYVL GSTLVVEDMS TARELMGDYR
MVTLDGDLVE KSGAMTGGSG GGSRYSFTKS GGGKIERLAT EISDLEDERQ SAQSEIDALD
DDIEDARDRK ADAAERVRSL EADVERAEDD LAEAEDRIAE LEAELDDLEA ERESVDAEMT
ALDERLAETD AEIDDLAAEI DDIEAELADS KIPELSERAD EIRAEIDDLE DRMSSFDSRI
NELELEKGYA EDALDDLHDD VEAAQNAKAE AEEAIADHEA AIEEKEAELA EKKAAIADLE
EELTELKAER EELREEIREA TQARDEQRSL VAEAESDLSD LTDRRDRLEW EIDELESQVG
EYDADQIPDL DEVESRIEEL EAEMEALEPV NMLAIDEYEE VQAALDELQE RRDVLVEERD
AIEERIEGYE AAKKETFMET FDSINDHFED IFARLSAGSG ELVLENPEDP FEEGLTMKAQ
PADKPVQRLD AMSGGEKSLT ALSFIFAVQR HNPAPFYALD EIDAFLDAVN AERVGEMIEE
LAEEAQFVVV GHRSALLERS DRAIGVTMQG DNLSAVTGMQ FGDDADEEVS ADD
//
