ID K7WHE5_9NOST Unreviewed; 1272 AA.
AC K7WHE5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=ANA_C12198 {ECO:0000313|EMBL:AFW94938.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW94938.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW94938.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW94938.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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; CP003284; AFW94938.1; -; Genomic_DNA.
DR RefSeq; WP_015080095.1; NC_019427.1.
DR AlphaFoldDB; K7WHE5; -.
DR STRING; 46234.ANA_C12198; -.
DR KEGG; anb:ANA_C12198; -.
DR PATRIC; fig|46234.3.peg.2489; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_3; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000010101; Chromosome chANA01.
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; IPR008160; Collagen.
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; PF01391; Collagen; 2.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000010101}.
FT DOMAIN 619..736
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 753..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..471
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 507..604
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 814..1035
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1077..1111
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 753..771
FT /note="Polar 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 1272 AA; 142958 MW; CB7723593092DC0E CRC64;
MVYVKRVELT NFKSFGGTTA VPLLPGCTVI SGPNGSGKSN ILDALLFCLG LASSKGMRAE
RLPDLVNNAQ KHKGRSALEA SVTVTFDISD VSRRGAEARR EEVGEVGEVG EVGEVGEVGE
VGEVGEVGEV GEVGEVGEVG EVGEVGEVGE VGEVGEVGEV GEVGEVGEVG EVGEVGENLK
SKIQNPKSSE WSVTRRLRVS QQGGYTSNYY INGVACTLTE LHEDLEELRI YPEGYNVVLQ
GDVTSIISMN ARERREIIDE LAGVATYDRK IVQARSTLDE VKDKEDSCRI IQTELSIQCD
RLSQDKAKAE KYQLLKVEFI QKQSWESVLS WRSLQAQQEK LVAQVQEGDR NFSDFTTQLN
TTNSQIDQKT TELDQLNLRV KALGEEELLS VQSNLATQEA ERKQLQRQQR ELEASIQEST
RRLNQTYQEI QQYQLALEEA KKKQNIETVN VTSLQTERDT AQQNLESSRQ AAAEIASASE
AWVQQQTALN RQMESLLHTL EPQRTEQAQL QERNTQLQQL ISEQSQLIAT LEPELAQKQA
ECARLETEFN ASTQPIQNLA ENLAATEQEL QIQQDTQKRL LQEQRDKQRQ LDKLEAQTQA
QQEIQGTQAS KVILQSEMPG LCGLVVQLGK VDPKYQTALE MAAGGRLGHI VVEDDSVASA
GIELLKQKRA GRATFLPLNK IKVPKFTQDA TLRLADGFVN YAVNLVECDR RYHDVFAYVF
GATVVFATLA QARKNMGLYR IVTLQGELLE TSGAMTGGSS SQRSSLRFDN GEAGESQEVA
NLKSRLIDID RILERCGEAI SHLGTRTKTL TLELTEARQV RREQQLYLEQ LKKEIKSLTT
QLENTRSQLS QNTQKFTSAQ SRLEILDREL PEQETQLQQL RHTLAELESS QTPSEWQQIQ
AIIKTQEQEL QQRETALRDV QQQLKNLENQ QQRLQEKIEE SQTRVIQYQQ EETTGKQQQA
TVNSQVEELN NLITAIQAKL GQLEENLGEE KKNRDTAETE LRSLLLRQQQ LQWEIEKLQE
TQQKRREDLT ALQNQLRDLG AELPSPLPEV PNKVDLEDLQ KELRSLGKRL QAMEPVNMLA
LEEFDKVQSR LQELTEKLET LEGERTELLL RIENFTTLRQ KAFKEAFDAV NENFQSIFAI
LSDGDGYLQL DNPEDPFNSG LNLVAHPKGK PVQRLASMSG GEKSLTALSF IFSLQRYRPS
PFYAFDEVDM FLDGSNVERL ARMIKQQAEQ AQFIVVSLRR PMIESAQRTI GVTQARGAYT
QVLGIKLQSS DN
//
