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Database: UniProt
Entry: A0A0P6XI69_9CHLR
LinkDB: A0A0P6XI69_9CHLR
Original site: A0A0P6XI69_9CHLR 
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
//
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