ID F3Y8G0_MELPT Unreviewed; 1192 AA. AC F3Y8G0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 11-JUN-2014, entry version 19. DE RecName: Full=Chromosome partition protein Smc; GN Name=smc; OrderedLocusNames=MPTP_0302; OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / OS NCIMB 702443). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Melissococcus. OX NCBI_TaxID=940190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443; RX PubMed=21622755; DOI=10.1128/JB.05151-11; RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M., RA Miyoshi-Akiyama T.; RT "Complete genome sequence of Melissococcus plutonius ATCC 35311."; RL J. Bacteriol. 193:4029-4030(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35311; RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D., RA Akiyama T.; RT "Whole genome sequence of Melissococcus plutonius ATCC 35311."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for chromosome condensation and partitioning CC (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- DOMAIN: Contains large globular domains required for ATP CC hydrolysis at each terminus and a third globular domain forming a CC flexible hinge near the middle of the molecule. These domains are CC separated by coiled-coil structures (By similarity). CC -!- SIMILARITY: Belongs to the SMC family. 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; AP012200; BAK20788.1; -; Genomic_DNA. DR RefSeq; YP_004455597.1; NC_015516.1. DR EnsemblBacteria; BAK20788; BAK20788; MPTP_0302. DR GeneID; 10595128; -. DR KEGG; mps:MPTP_0302; -. DR PATRIC; 54619270; VBIMelPlu182073_0292. DR KO; K03529; -. DR BioCyc; MPLU940190:GH20-302-MONOMER; -. 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-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 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; IPR011890; SMC_prok. 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; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 1. DR TIGRFAMs; TIGR02168; SMC_prok_B; 1. PE 3: Inferred from homology; KW ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; KW Nucleotide-binding. FT NP_BIND 32 39 ATP (By similarity){EA3}. FT COILED 167 203 By similarity. FT COILED 233 499 By similarity. FT COILED 675 924 By similarity. FT COILED 964 1019 By similarity. SQ SEQUENCE 1192 AA; 137791 MW; 3F8132F910499E4A CRC64; MYLKRIEIAG FKSFADRTII DFENGVTAVV GPNGSGKSNI TEAIRWVLGE QSAKSLRGGK MPDIIFAGTQ ERKPLNIAEV MIVLDNTDYY LPLDFSEISI MRRYRRTGES EFFINKQACR LKDIQDLFMD SGLGKESFSI ISQGKVEAIF NSKPEDRRGI FEEAAGVLKY KQRKKKAEQK LFETEDNLDR IKDIIHELAE QLVPLETQSK TAEKFLIIKK ELTTVDVGLT VVEIEDTKNL WETKKEEFHQ LEEQLKIVDQ QIHKLEDYLQ HTRTKRTALD KQIEIQQQQL LQIIESLKQT EGQKNVLSER SKHTLQTASE YEQSLNELTK EIANYQEELT HIQSKISLNE QQQKELKKEN QTAQANVAKY SKSSKELMEE LRSQYVEMMQ DQANVSNDLK YLERQYQQET TKNKQSIQKH ESLVNELSQA LIKKEELAAN NQAIEKVLKE QITRYEETKQ QLELKQQALT DKQKKMYQMM NQTQQVKARQ KSLQEIQENY TGFYQGIRII LKNRQQLSGI IGVVAELIKV PEKYTIAIET ALGSAAQHIV VESEKDGRTA INFLKQQHGG RATFLPITTI KARQLSTSVY TKIQKQTGFI GIASELVQYE EKVAAIIKNL LGTTLFADSL ENANQLAKLI SYQYRIVSLE GDIMNPGGSM TGGANKRGSQ GSLFNQSHEL QLLNEQVIEL ETKQRQTEKE VQQLINEEQQ LRENLEQLRL KMEEDRLKQQ ESMSQLSNVQ LLIERLTKEK RLFEFESHEI HQFLSDYQLQ KEELLKKQVF LLEEKERLDL EMNQIEQEAS QMEVYKNKAQ EIFNQIQSKQ AVMNEQFAYL LQQKNEKQSQ LTGIVEKKAS LTHQLQQLND HSVDHQTTEK DLAMQLDQLS DEREKIQTLI YEEKQTQQQL QKEINQTEAN LADKNKQQQQ LLSRQTQIEI QKDRTEVRLD HSLQYLQEEY NLTFDYAQSN YEPIKEKDTA RNQVEELKQA IKRLGPINLE SIDQYHQVNE RYQFLITQRD DLLSAKDQLF GTMDEMDQEV KERFSETFKA IRMQFQSVFP NMFGGGQAEL ILTDPNDLLN TGIEIEAQPP GKKLQGLSLL SGGERALTAI ALLFSIIHVR PVPFCVLDEV EAALDEANVA RFGRYLSTFE DEMQFIVVTH RKGTMEAADV LYGVTMQESG VSNLVSVRLE TIKEDEKIVK NV //