ID L0IBW1_HALRX Unreviewed; 1190 AA.
AC L0IBW1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Halru_1109 {ECO:0000313|EMBL:AGB15726.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15726.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) 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; CP003050; AGB15726.1; -; Genomic_DNA.
DR AlphaFoldDB; L0IBW1; -.
DR STRING; 797302.Halru_1109; -.
DR KEGG; hru:Halru_1109; -.
DR eggNOG; arCOG00371; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000010846; 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 Gene3D; 1.10.287.1490; -; 2.
DR Gene3D; 1.10.287.2610; -; 1.
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; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46579; Prefoldin; 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:UP000010846}.
FT DOMAIN 542..656
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 910..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..520
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 991..1032
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 910..928
FT /note="Basic and acidic residues"
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 1190 AA; 135008 MW; 8020599C39CEF3E1 CRC64;
MHIKALVLDN FKSFGRKTRI PFYEDFTVIT GPNGSGKSNI IDAVLFALGL ARTRGIRAEK
LTDLIYNPGY DDGERPASTR EAEVEVILDN ADRTLERSQV ATAAGSDDVG DCDEIRIRRR
VKQTEDNYYS YYYLNGRSVN LTDIKDLLAQ AGVTPEGYNV VMQGDVTEII NTTPHSRREI
IDEIAGVAEF DAKKEDAFEE LEVVEERIDE AQLRIEEKQT RLDQLEDERQ TALRYRRLRR
EKAEYEGYLK ASELEDKREE RDDVEARVDD LEDELESLQR SLDEKQGAVV RLQEDLEDLN
DEIEQKGEDE QLKIKGEIEE VKGEIARLED KIETAEERIE AAEADRRDAF VQIDRKQERV
DDLADEMREC KLEKASVTSE IQEREAEIES LETELENVDT EYDEVKAELA ECKDAVEEAK
TEKNDLQREQ DRLLDEARRR SNQIAELESS IEETEELLPE LEDERSELER ELDKAETNRE
NIDSVVTDLK RERFSLQDDV DELEDELQAK QQEYAELEAK AGESGDSSFG RAVTTILNTG
FDGVHGAVAQ LGSVDGAYAT ACETAAGGRL ANVVVDDDGV GQRCIDHLKS KNAGRATFLP
MTEMYSRSLP SAPSDPGVVD FAYNLVDFDD QYDGIFSYVL GDTLVVEDIE TARSYMGDYR
MVTLDGDLVE KSGAMTGGSR KGSRYSFSTD GRGKLERVAT QITELQDQRD DLRDELRDVE
SRLDDARDRQ TDAADEVRSI ENEIEKLDEQ RDRLEAEIES DEAELEDLEA EREEVDEEMT
DISAQIEAKQ DEIDEIEGTI ADLEAELADS KIPELTGQIE DLEAEIDERT ERIDELDSKL
NELELEKSYA EEAIDDLHDE IEAAQNQKAD YEERIETFED EIESQEAVLE EKRAAVAQLE
DELAELKEER TGLRDDLDEA RQERDEVQDE VNDVEADLSN ARERLDALEW EIDSLEEEVG
EYDPEEVPDH DTVVEMVDLL ETDMQALEPV NMLAIDEYAE VRDELDELEA NRETLVEEAE
GIRERIERYE SLKKETFMEA YEAINEQFTE IFEQLSEGTG SLHLENEEDP FDGGLTMKAQ
PGDKPIQRLD AMSGGEKSLT ALAFIFAIQR HNPAPFYALD EVDAFLDAVN AERVGRMVDQ
LAGDAQFVVV SHRQAMLDRS ERAIGVTMQQ DNVSAVTGID LSEEGVVADD
//
