ID K9YH94_HALP7 Unreviewed; 1184 AA.
AC K9YH94;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=PCC7418_3641 {ECO:0000313|EMBL:AFZ45750.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45750.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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DR EMBL; CP003945; AFZ45750.1; -; Genomic_DNA.
DR RefSeq; WP_015227622.1; NC_019779.1.
DR AlphaFoldDB; K9YH94; -.
DR STRING; 65093.PCC7418_3641; -.
DR KEGG; hao:PCC7418_3641; -.
DR PATRIC; fig|65093.3.peg.3845; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_3; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000010481; 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; 1.10.287.1490; -; 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; 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 NCBIfam; TIGR02168; SMC_prok_B; 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; 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:UP000010481}.
FT DOMAIN 521..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 654..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..506
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 656..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..915
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 1184 AA; 135161 MW; BB9DF77FA72FAB1D CRC64;
MVHVKRLELS RFKSFGQTTQ IPLLTGFTVV SGPNGSGKSN ILDALLFALG LASSRGMRAE
RLPDLVNNQN NGKGRAETTV KVTFELDDET EWSVARRLRV TKEGSYASTF YINDETCTQS
QLHEQLRALR IYPEGYNVVL QGDVTRIISM NGRERREIID ELAGVAEFDR KIAKAKETLE
TVKEKEERCE ILQQELIKTR DRAASERNKA EKYRQLKAEI QEKQQWEAVL EWKALKQQID
TLQGEITGNE QTLTQLQQTI QTTETQIQQA SQTLDDLNAQ VKALGEDEQL EATSKLATQK
AQQEQLQQRE AELNQTLEET ATAQEQTRTQ LQEQQTRLQT LQQELADLSE KQLQELQQAQ
HTAQTKLAES REQANAIASA SEEWIQQQTQ LSQQINQLQN SLNPQRTEQA QLQERETQLQ
QKIEEQQTTL ASLTPELEVK QQTLQELEQT VNQLQAQVQT LAQQLSHAEE EKKLQQATQT
RLLQEQRDKQ RKLDKLEATK EAEEKAQGTY ATQIILQSPI TGVCGLVAQL GQVEPRYQLA
LETAAGGRLA QIVVENDQVG AKAIELLKEK RGGRATFLPL NKIQPPRQNM TAALRYANGF
VDYAANLIEC EPRYQVIFAY VFGNTAVFTT LEKARPHLGK TRIVTLEGEI LESSGAMSGG
SRSTRSSLHF GTATETESDE IQQLKARLAE IEEILAVCDP KIEQATTESQ RLTEQLNETR
QQHQEQQWQY KQTQQEIERL SQQQQQVSEQ LSQNENELMQ LQGRLELLAN SIPQQETELV
QLQAELAELE ASHSNTQWQE IQQVIKQQEA ELKQAETALN EAKQQQQQLE TEQLRLQEKI
STSEQRLTEY EQRVVETNQQ KATVEQQKQD IAAKIAETDT VIAQLQEKLG KLKEERDRAD
KTLRSHQRQQ DKQTWKQQKL QETLSEQQEK LATLQSQYEE KGNSLAQPLP EIPELVQETP
SETITFANYS EQLTHLQEEL RQMQKRLQDM EPVNMLALEE YEKTQARLDE LTEKLTTLQE
ERNELLLRIE TFTTRRIEAF NEAFNAVNEN FQTIFATLSD GDGYLQLDKP DDISNANLNL
IAHPKGKPVQ RLHSMSGGEK SLTALSFIFA LQRYRPSPFY AFDEVDMFLD GANVQRLANM
IQQQAQEAQF IVVSLRRPMI EASMRTIGVT QARGAYTQVL GIKL
//
