ID Q18KQ1_HALWD Unreviewed; 1198 AA.
AC Q18KQ1;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:CAJ51393.1};
GN OrderedLocusNames=HQ_1264A {ECO:0000313|EMBL:CAJ51393.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51393.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ51393.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180088; CAJ51393.1; -; Genomic_DNA.
DR RefSeq; WP_011570554.1; NC_008212.1.
DR AlphaFoldDB; Q18KQ1; -.
DR STRING; 362976.HQ_1264A; -.
DR GeneID; 4194701; -.
DR KEGG; hwa:HQ_1264A; -.
DR eggNOG; arCOG00371; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR Proteomes; UP000001975; 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; 1.20.1060.20; -; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001975}.
FT DOMAIN 547..661
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 199..518
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 700..970
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 996..1037
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 1198 AA; 134314 MW; 76F772B0B6A5C231 CRC64;
MHIKTLILDG FKSFGRATEI PFYEDFTVVT GPNGSGKSNI IDGVLFALGL ARTRGIRAEK
LTDLIYNPGH ATTEADGSNS SESPNEATVT VVLDNSAGTI DRTQVINAAG SESIGDVDEI
RVKRRVKQTE TNYYSYYYLN GRSCNLSDIQ DLLAQAGITP EGYNVVMQGD VTEIINMTPQ
QRRSIIDEIA GVAEFDAKRD DAFEELDAVE GRIEEADLRI GEKETRLRQL ADERETALKY
QSLRDERTEY EEYLKAAELE SKRADRDETA EQATEVEADL TEANETFSQR QQHVSRLTAE
LDAVTAEIER KGEDEQLALK SEIEEIKGAI RRRENDIETA EERITEAENT RREAFVQLDQ
KQEQIEELDT EIRSIKVEKA SITTEIESLE SDLADVEAEI EDVDATYDER KHELEAAIDR
VNEFKTKRSD AQREKDRLLD KTRRRASDIA DAKEELTKLR EELSTLQATL SDFHSEVDIA
EKNESTIEDA LSELQNKRSE LKDNLDTVRS EIQSKQSEYA TLEGHTGNDT DTSWPRAVTT
ILNADRTGVH GTVGQLGSVE KKYATACETA AGGRLAHVVV DTDTVGSDCI EYLKSRNAGR
ATFLPITKMD DRGIPRQPNH HGVIDFAQNL VSYDDMYRPI FSYVLGSTLI VETMETAREL
MGEYRMVTLD GDLVERSGAM TGGSGGGSRY SFSTSGGGRL ERLAEKIETL EDRRQEYQSK
IRTVDDDISD ARERAASARE RVRELESEID ATKTEIEETE AAIEQTESRI ANLREERAEA
DKTMQSVDDD IDTLNAEITT TEQEIQTIKE ALEESPVPEL TAEADELRTA IDDAESQIDD
LDARQNELEL ERQYANEAID ELNEQVERAQ AKKADAQETI STAQEDIETY NTTLEAKRVA
VDEIEDELIS LKSDRSDLQA TLNAAKNRRE SARDTVDKLE SKSSSLRGAI ERLEWEIDEL
ESEVGTYDST DIPDYDTVEA NIDRLTEKMD SLEPVNMLAI DEYDDVESQL DELSSRRDIL
VEEREAIEER INRFESQKRE TFMSSFRAIN ENFTDIFERL SDGTGELHLE SQDEPFEGGL
TMKAQPGDKP IQRLNAMSGG EKSLTALAFI FAIQRHNPAP FYALDEIDAF LDAANAERVG
EMVDDLATDA QFVVVSHRSA LLERSERAIG VTMQGNNISA VTGIQLQNDE SPEAPADD
//
