ID A5GNN5_SYNPW Unreviewed; 1201 AA.
AC A5GNN5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:CAK24550.1};
GN OrderedLocusNames=SynWH7803_2124 {ECO:0000313|EMBL:CAK24550.1};
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK24550.1, ECO:0000313|Proteomes:UP000001566};
RN [1] {ECO:0000313|Proteomes:UP000001566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566};
RG Genoscope;
RL Submitted (MAY-2006) 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}.
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DR EMBL; CT971583; CAK24550.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GNN5; -.
DR STRING; 32051.SynWH7803_2124; -.
DR KEGG; syx:SynWH7803_2124; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_3; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000001566; 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; 1.20.1060.20; -; 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 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:UP000001566}.
FT DOMAIN 541..666
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 265..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 743..964
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 988..1043
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 265..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1201 AA; 134715 MW; 21C515512B82C2D3 CRC64;
MVHINQVGLT HFKSFGGAMT IPLEPGFTVV TGPNGSGKSN ILDGVLFCLG LANSRGMRAD
RLPDLVNSGV LKAGKSAETT VSVRFDLSDW QPDAAEEGIE APEEGPWIRP DQTEWTVTRK
LRVMPGGSYS SSYSADGIPC NLQQLQTQLR RLRIDPEGSN VVMQGDVTRI VSMSNRDRRG
LIDELAGVAL FDTRIEQTRR KLDDVQERQE RCRIVEQELL AARQRLEKDC AKARAYQELR
EQLQLGRRQE LVLAYEAAQA ERRRLQQRHQ DLGDQDTRDS QALEEQETTL QEAATKLKTL
QDNVKALGED QLLGVQAELA GLDPENRELE RQAAQHQQEG ERLQAVRHDL QARRGQIQSE
SESLRLSADP SGLAQAEQDC RDAEAAVERS RRQLGEVAGR SGTWIEEQRQ RSSRRQQLQV
SLAPLQEERQ QLKERLRQAE ERRLDLEQER DQDGAEDHKV QTLLAQLEQE WQALLNTIRT
GQEQLQQLAE SLAIQQRTRT RLAQEQTRLE RDIARQDSRR EALQESRGTG ALRLLLESGL
EGIHGPVAQL GEVEDRHRMA LEVAAGARMG QVVVDNDRIA ARAIDLLKSR RAGRLTFLPL
NKIRAPGGGG GAAMARGRRP DGGNADGLIG RAVDLIRYEP IYGDVFAYVF GDTQVFTDLG
SARRVLGRSR AVTLDGELLE KSGAMTGGSL GQRSGGLSFG VSNEGDDAAP LRQRLLELGE
TLAACCREEQ RLSAQLEEQR PGLRQLEQRQ AALEAERQAA RRSHGPLLER LQQRQRRLQE
LQETGSKESR RLQEIETALT PLQTELQQLD QQDSKEESNA DAERWQALQQ TLEQADGALE
TARRQRDTLL QQDRERQMSG QRLADQLQAV EREEQSLQEA VKTLAETHGR WKQQQQDLKT
RRDALNAQQQ ELQTRFGEER RARDEAEAAV AELRQALQQA RWNLERLREE RVSLEEQLRS
GSLRLEELKS SLPDPLPEIS DAIREGGVEA LQEQLQQLQR RMEALEPVNM LALEELQELE
QRLGDLGERL DVLSQEREEL LLRIGTVATL RQEAFMEAFE AVDGHFREIF ASLSDGDGKL
QLDNADDPLE GGLTLVAHPK GKAVRRLAAM SGGEKSLTAL SFLFALQRFR PSPFYALDEV
DSFLDGVNVE RLAALIARQA EQAQFLVVSH RRPMIGASTR TIGVTQARGA HTQVIGLPDA
A
//