SMC_SYNY3
ID SMC_SYNY3 Reviewed; 1200 AA.
AC P73340;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=sll1120;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; BA000022; BAA17371.1; -; Genomic_DNA.
DR PIR; S77524; S77524.
DR AlphaFoldDB; P73340; -.
DR SMR; P73340; -.
DR IntAct; P73340; 1.
DR STRING; 1148.1652449; -.
DR PaxDb; P73340; -.
DR PRIDE; P73340; -.
DR EnsemblBacteria; BAA17371; BAA17371; BAA17371.
DR KEGG; syn:sll1120; -.
DR eggNOG; COG1196; Bacteria.
DR InParanoid; P73340; -.
DR OMA; HNKIAME; -.
DR PhylomeDB; P73340; -.
DR Proteomes; UP000001425; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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; IPR036277; SMC_hinge_sf.
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; TIGR02169; SMC_prok_A; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1200
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409282"
FT DOMAIN 542..656
FT /note="SMC hinge"
FT REGION 90..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 202..528
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 692..1046
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1200 AA; 136136 MW; E4FE00EBE6BBDF21 CRC64;
MVYVKRIELS HFKSFGGTTA IPFLPGFTVV SGPNGSGKSN ILDALLFCLG LATSKGMRAE
RLPDLVNNTF KGNRGSSEAS VSVTFELHDG ENLSEPGANH NGNGNGAKIS KEWTVTRRLK
VTKGGNYSSN YYINGETATV TELHEQLNEL RIYPEGYNIV LQGDVTRIIT MNSKERREII
DELAGVAEFD RKIVKTKETL TEVQDREERC QIIATELERT LERLAADRQK AEKYQALRQQ
VQEKQGWAKV IQYKAVEQQR QKLWGQLERD REQSQQIQQA LDQRSQAIQT QQTELEKLNA
QVKALGEEEQ LAVAAQLATQ KAQRDQLQQR YNDGDRQITN HQQQVGQIQA EISQSQQQFL
HIQQEKSFHN TQTLPQLEAA VQTSQQQLEQ LRHQAQAIAS ASEAWVQEQT QLSRTVNQLQ
DELIPQRSQL AQLEERQQQL LTNLAELTPL LTKVSVELEE KQFAQGQFNF QGEALTSQIQ
TLASDLAQLE QERSLLQETQ TRLLKEQQEK QRQLDKLEAA SQAQQEVQGT YATKVILQSD
LPGVCGLVAQ LGQVEPQYQL ALEIAAGGRL GFLVVEDDGV AAAGIEILKQ AKAGRATFLP
LNKIRPPKGQ NPNLSYAHGY IDLAVNLIDG DRRYADIFAF IFGNTIVFDT LVNARNHLGK
HRIVTLEGDL LEASGAMSGG SRNQRSGLRF GTMVSEDTAE VKQLRQRLQD IQQVQGRNEE
LLLERTVRSR QLTQQLMEMR QQQREAQLHG EQTERDIARL SQQQTQINQQ QINQQQKLAE
LQQNLALLQQ SLPPLEQQLA SAQQQLTALE TSQTHQQWQT IQIQIRTVEA EYQRQLQALR
QGEDHLKDLQ NSSQRLEEKI AQAQEKIAQH QAQDLTLAQE QEQLKIALAE MNGAIQTTEA
QLAKLSEKLG STKQERDRLE TQLNQLRSQQ QEQQWQWEKL QTNQQEYQEN LTQLQTQLEA
LEQDLPDPWP EIPLLQDRDE ANLDFANILE ELERSIRNGQ KRLEAMEPVN MLALQEYEKT
EARLGELSEK LQTIAGERTE LLLRIENFTT LRRRSFQDAF DAVNKNFQII FAELSDGDGY
LQLDDAEDPF NGGLNLVAHP KGKPVRRLSS MSGGEKSLTA LSFIFALQRY RPSPFYGFDE
VDMFLDGANV EKLSKMVRKQ AQQAQFIVVS LRRPMIEAAE RTIGVTQARG AHTQVLGIKL