ID A0A0P6XI69_9CHLR Unreviewed; 1200 AA.
AC A0A0P6XI69;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SE15_08685 {ECO:0000313|EMBL:KPL83291.1};
OS Thermanaerothrix daxensis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Thermanaerothrix.
OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL83291.1, ECO:0000313|Proteomes:UP000050544};
RN [1] {ECO:0000313|EMBL:KPL83291.1, ECO:0000313|Proteomes:UP000050544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL83291.1,
RC ECO:0000313|Proteomes:UP000050544};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL Submitted (JUL-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: 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:KPL83291.1}.
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DR EMBL; LGKO01000004; KPL83291.1; -; Genomic_DNA.
DR RefSeq; WP_054521713.1; NZ_LGKO01000004.1.
DR AlphaFoldDB; A0A0P6XI69; -.
DR STRING; 869279.SE15_08685; -.
DR PATRIC; fig|869279.4.peg.2468; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000050544; 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; -; 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; 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.
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:UP000050544}.
FT DOMAIN 525..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 243..375
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 404..494
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..797
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 824..942
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1008..1045
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1200 AA; 137413 MW; EA51407A07F6A3BF CRC64;
MASRLKSLEL QGYKTFASRI LFEFPGRITA IVGPNGSGKS NIADAIRWVL GEQSFSLLRA
RKTEDMIFSG SEHRPRAGMA MASIIFDNED QWLPLEFSEV SIARRAYRDG QNEYLLNGQR
VRLKEITELL SRAGLSERTY TIIGQGLIDA ALSLRPEERR RFFEEAAGVG LYRIRREEAL
TRLDATRRNL ERVQDILIEL EPRVKSLERQ AQRAQEYERI SADLKLLLRE WYGYHWFQSQ
QRVVQSRETV RRIEQRLAEQ RARTEEQENR LKEIREAWVE VGSRIESLKE RALALEREKT
QLERNAAVLE ERRAALLAQQ KSLGSDRERL EAEQTEIQVQ ILAVEREREQ VQVELETARR
EIQTLSQQLE SREAEERALI TQRSSLQTTL SGLEKRQYAY EVERESYKRR LSDLQDQIKR
ATNQKEESLR LLGEAKERLA QQRQGVEALE ARTRELSAEL STLSQRLEAA RETLREIQKE
QDAVEAAILK ARAELSVIEQ AEATFEGLSQ GTQALLQAIQ NGQLPARVKR LSQVLSVAQD
YEQAIAAALG ERIEGLVLED PEAVDTLLAF LEGSERGRAI LLVGQGEILQ HDLTSLNDEA
CLGRAIEFVQ VTPANQGLLR ALLGNVWVVR HRRDARRLWP ALPEGGRLVT LQGEVFSSDG
VIAAGLDRRT TLITRSQRQR ELQATLRRLE QKLAALGQSR VAHEADLAQV ENDRVAVERE
LKRRRAELEQ KRREYEALVG RVRRQEEDLR RVEETLRQAE SQKSVIEQQA QALEQAAKAS
QSEVKALQAQ LEQINAAIQA LAVGTLKDQI NHWRSVERMT TQRMNHLSQR LSDYQQALQR
TTSRLNELEA RSVQIQTTLM SLEQEAAALQ GRLREFERDE AELREQYAPL ETEHHRLQAD
QERVMAEWRA QQQQLTLLEK QAQQAQLEHM REEEALASLQ RRIEEDLGLV SFTYIETVAG
QEPLPLNGMV EALPALQQLP PDIEDSIARY RSQLKRIGHI SPDLLKEYQE LRARYDYLRD
QMEDLKKAES DLREVIAELD GLIREAFLKT FKAVAREFQQ NFVRLFGGGE ARLYLEDETK
PGESGIEIEV RLPGRREQGL ALLSGGERSL TSVALVFSLL KVSPPPFCIL DEVDAMLDEA
NVGRFCDMLK ELSQETQFII ITHNRNTVQT ADVIYGVTMG KDMTSQVISL RLENLAEVLV
//