ID A0A0W1RBZ1_9EURY Unreviewed; 1228 AA.
AC A0A0W1RBZ1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AUR64_08280 {ECO:0000313|EMBL:KTG10651.1};
OS Haloprofundus marisrubri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloprofundus.
OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG10651.1, ECO:0000313|Proteomes:UP000054387};
RN [1] {ECO:0000313|EMBL:KTG10651.1, ECO:0000313|Proteomes:UP000054387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB9 {ECO:0000313|EMBL:KTG10651.1,
RC ECO:0000313|Proteomes:UP000054387};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT archaeon isolated from the Discovery deep brine-seawater interface in the
RT Red Sea.";
RL Submitted (DEC-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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:KTG10651.1}.
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DR EMBL; LOPU01000017; KTG10651.1; -; Genomic_DNA.
DR RefSeq; WP_058580975.1; NZ_LOPU01000017.1.
DR AlphaFoldDB; A0A0W1RBZ1; -.
DR STRING; 1514971.AUR64_08280; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000054387; 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; 1.20.5.340; -; 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; 2.
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 419..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1032
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 1194..1228
FT /note="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 1228 AA; 137694 MW; 2B898A8EFCEC1444 CRC64;
MHIKELVLDN FKSFGRKTRI PFYEDFTVVT GPNGSGKSNI IDGVLFALGL ARTRGIRAEK
LTDLIYNPGH DDGSSSGGPR EASVEVVLDN SDGTLERSQV TTAAGTDSVG DVDEITIRRR
VKQTEDNYYS YYYLNGRSVN LSDIQDLLSQ AGVAPEGYNV VMQGDVTEII NMTAFQRREI
LDEIAGVAEF DAKKDAAFEE LETVEDRIGE ADLRIEDKEE RLDQLADERE TALEYKGLRE
EKEEFEGYLK AAELEDKRAD LQRTTSKIDS KEETLAELRE ELDTRQGRLS RLEDELEGLN
REVERKGEDE QLRIKREIES VKGDISRLEG QIENAEERKE TAENERRQAF VEIDHKQEKV
DDVATQMRQV KVEKASIKSD IVDKRTTLAE IEDEIANVDT EFDELKADLA DRRERVETLK
SEKNEKQREK DRLLDEARRR SNRVSEARND IEAAHESIPE RKAKLSELHS ELDKAEKNES
KSKEIVSEFR EKKQNLQDEL SDVEDDIRSK QSEYAELEAR AGKNGDNSFP RSVTTVLNAG
IDGVHGAVGQ LGSVAGEYAV ACETAAGGRL ANVVVDDDGV GSSCIDYLKS RNAGRATFLP
ITKMQNRRLP RKPKDPGVVD FAYNLVEFDS RYDSIFSYVL GSTLVVEDMQ TARQFMGDYR
MVTLDGDLVE KSGAMTGGSR GGSRYSFSKS GEGRLERVAK EISKLEDRRR TLNAEIRDLE
EKLDDARDRQ SNAADKVRTI EGDIERVESD LEDAESKIEE LEATLDELEA ERDSVDEEMG
ALDADIAELD AEISEVEAEI EKLEAELADS KIPELTSEAD DVRADIDDLE TRMDELDSRL
NELGLEKQYA EEAVSDLEET VESAQNRKAA AEEKIAEAEA AIEEKEAVLD EKHEAVEALE
DELVELKEER NELREELREA KNERDEQKEA VSRAESRLES LESAKERLSW EIDELEAEVG
EYDPEEIPDH ETVEKNVDRL ESEMEALEPV NMLAIDEYDS VEADLSDLQE RRDVLVEERD
GIEERIEQFE TQKKRTFMES YEAIDAQFQR IFERLSAGSG ELHLEDPEDP FEGGLTMKAQ
PADKPIQRLD AMSGGEKSLT ALAFIFAIQR HNPAPFYALD EVDAFLDAAN AERVGQMVDD
LAGDAQFVVV SHRSALLERS ERAIGVTMQG DNVSAVTGIR FDNQRSENGS DTDGDGSDGG
DGDSDTDSNS DTDGDSDEGL AAEVSADD
//
