ID A0A094PC51_9ACTN Unreviewed; 1192 AA.
AC A0A094PC51;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=GM45_4380 {ECO:0000313|EMBL:KGA08492.1};
OS actinobacterium acAMD-5.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504319 {ECO:0000313|EMBL:KGA08492.1, ECO:0000313|Proteomes:UP000029322};
RN [1] {ECO:0000313|EMBL:KGA08492.1, ECO:0000313|Proteomes:UP000029322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGA08492.1}.
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DR EMBL; JNSF01000008; KGA08492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PC51; -.
DR STRING; 1504319.GM45_4380; -.
DR PATRIC; fig|1504319.4.peg.879; -.
DR eggNOG; COG1196; Bacteria.
DR Proteomes; UP000029322; Unassembled WGS sequence.
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 CDD; cd03278; ABC_SMC_barmotin; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 1.20.5.170; -; 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; 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; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01894}.
FT DOMAIN 511..621
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 807..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..375
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 411..480
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 866..893
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1192 AA; 129459 MW; 57440B56DEF7A47A CRC64;
MYLKSLTIRG FKSFASATTL QFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKTLRGGK
MDDVIFAGTS NRSPLGRAEV SLTIDNTDGA LPIEYTEVTI SRTLFRGGGS EYSINGNPSR
LLDIQELLSD SGIGREMHVI VGQGQLGDVL QATPEERRGY IEEAAGVLKH RKRKEKALRK
LEATDANLVR LQDLTNEIRR QLKPLGRQAE LARKAQVFQA DARDARLRLL ADDLLVIKSA
LDKEIADETI LRQRQQEVEQ ALAQALNEIT KLESAGIEAA PQISRAQEAW FTLSALRERY
IGLKQVVTER IRLTSEPVDE QPRGTDPELL DEQAKSARTE EFSLSQESES LKLELANLSA
VRAELESKLN AAESSFTAAM RSAADRREGL AQLGGQVAAA QSRRETRETE IGRLTGQVAD
ARRRAADAEA SFRKEEAEIA GLDAGEMQLD SHYEEVSATL NKAEAKVRQL QAAVHEAEKI
KAAKSATADA ISAALGAEND GAAELIAANT PGLTGRLATN LIIETGYETA IAVALGAAAD
ALAGNNVDAA TAALQSLKTN KGGRAAIVVP VTKSNEQLAA PSPSRSASSL VQVSGELKSA
INSLLADVVV ADTLDQARSI HQSNPNLRVV TKDGDLLSNG LIIGGGSSNR SRIENLASAE
TARQERDAAS HELERIKFEL ESAVAAAQSA ADEVKAALSK LHESDAAQAA VALRLAELSQ
QSRAAAAEAE RLSKALADAE VARGDDEQAL VDLQKRLANA QSTGSDESIP TSQQRDELLV
SVERARAKEV EGRLTLRTAE ERHRVATSKA EELERSASLE RSARTRDALR RKRRVREGEV
AAAVSTAIDL VLERLEVSLI TGSTLKSDLE QARAERETKL QALRVKSREL ESQRSVLVDS
VHRDELARTE QKAKIEAIED KAMSDFGIDA EVLINEYGPD VLVPPSMPTP GDEVDPNQEP
PAPAAYVRVE QEKRARDAER QLNLLGRINP LALEEFTAME ERNRFLGEQL EDVKRTRADL
LEVIKEVDQR VQQVFAEAFA DTSREFSKVF ARLFPGGEGR LILLDPDNLL ISGVDVEARP
PGKKIKRLSL LSGGERSLVA VAFLVALFKA RPSPFYVLDE VEAALDDTNL GRLLEIYEEL
RENSQLIVIT HQKRTMEVAD ALYGVSMRGD GVSAVISQRI RDVQTELVDV QK
//
