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Database: UniProt
Entry: A5GNN5_SYNPW
LinkDB: A5GNN5_SYNPW
Original site: A5GNN5_SYNPW 
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
//
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