ID F7PNB8_9EURY Unreviewed; 1188 AA.
AC F7PNB8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HLRTI_002941 {ECO:0000313|EMBL:ERJ05069.1}, HTIA_2484
GN {ECO:0000313|EMBL:CCQ34592.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ05069.1, ECO:0000313|Proteomes:UP000003861};
RN [1] {ECO:0000313|EMBL:ERJ05069.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05069.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ05069.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05069.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
RN [3] {ECO:0000313|EMBL:CCQ34592.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC SARL4B {ECO:0000313|EMBL:CCQ34592.1};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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DR EMBL; HF571520; CCQ34592.1; -; Genomic_DNA.
DR EMBL; AFNT02000045; ERJ05069.1; -; Genomic_DNA.
DR RefSeq; WP_008527514.1; NZ_AFNT02000045.1.
DR STRING; 1033806.HTIA_2484; -.
DR GeneID; 23798975; -.
DR KEGG; hti:HTIA_2484; -.
DR PATRIC; fig|1033806.12.peg.2472; -.
DR eggNOG; arCOG00371; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR Proteomes; UP000015381; 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; -; 3.
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; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF161270; PspA lactotransferrin-binding region; 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 406..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 990..1024
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 406..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..767
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 1188 AA; 134313 MW; B1B17A5E875865B8 CRC64;
MYITEVVLDN FKSFGRKTRI PFYEDFTTIS GPNGSGKSNI VDAILFALGL ARTSGIRAEK
LTDLIYNPGH QDGESPDRER EASVEVVLDN ADRTLSRSQV VSAAGSENVG DVEEITIKRR
VKETDDNYYS YYYINGRSVN LGDIQDLLAQ AGVTPEGYNV VMQGDVTEII NMTAGARREI
IDEIAGVAEF DQKKAQAFEE LEVVEDRIEE AELRIEEKET RLEQLEDERE TALEYQKLRD
EKEEYEAYQK AAELEDKRDD LDAVREEIAD LEETLEQRRR ELDEREGKVV RLEDELAELN
AEIERKGEDE QLALKRDIEE IKGEIARLED AIESAEEKRD EAEARRREAF VEIDRKQETI
DDLAADIRET KVEKSSVKAE IDDLEVDLAA VEEEIEEVGA EYEEVRAELE DQKSSLEEAK
ERRNDLQREQ DRLLDEARRR SNQQRDLEST IEDLEDSIPE LDAEIDDLQE ERRKAEANRE
TITDVIDDLA AEKRDLQAEI EAIDDDLEAA RQEYAELEAR AAESGDASYG RAVTTVLDGD
LDGVHGTVGQ LGGVDPTYAT ACETAAGGRL ANVVVDDDGV GQRCIEYLKN RNAGRATFLP
LTEMDNRSLP SLPSHDGVVD FAYNLVDFEA AYSGVFSYVL GDTLVVEDMA TARELMGRYR
LVTLDGELVE KSGAMTGGSS SGSRYSFSDS EGQLQRVAER ITELEDERQA YREELGDVEE
RLEDARDRKS EAADQVREIQ AEIERRERER EETEERIEQR REELDEIEDE REAVSAEMDE
IEADIESVES EIDDLEAEIA GLEAEIEDSR LPELTDEAES LESEIDERED ELDDLDAALN
ELQLEKQYAE DAIEDLHDEI ETAQNRKAEQ AERIEELNER VAEEESKLAD KQDAVAELEA
ELADLKGDRE DLRAELQAAQ QERDEQKERV NEIESNVDGK RETESRLEWE IDELEDAVGE
YDPEEIPNHH TVQTRIGQLE AEMERLEPVN MLAIEEYDEV EADLADLEDK RGTLVEEAEG
IRDRIDSYEA RKKETFMEAF ESIDAQFRDI FERLSNGTGR LHLENEADPF EGGLTMKAQP
GDKPIQRLAA MSGGEKSLTA LAFIFAIQRH NPAPFYALDE VDAFLDAANA DLVGEMVDEL
AGEAQFVVVS HRSAMLERSE RAIGVTMQGD NVSSVTGIDL TEEVPADD
//
