ID A0A239E0M4_9ACTN Unreviewed; 1217 AA.
AC A0A239E0M4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05443665_1003163 {ECO:0000313|EMBL:SNS38275.1};
OS Actinomadura meyerae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=240840 {ECO:0000313|EMBL:SNS38275.1, ECO:0000313|Proteomes:UP000198318};
RN [1] {ECO:0000313|EMBL:SNS38275.1, ECO:0000313|Proteomes:UP000198318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44715 {ECO:0000313|EMBL:SNS38275.1,
RC ECO:0000313|Proteomes:UP000198318};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOR01000003; SNS38275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239E0M4; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000198318; 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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198318}.
FT DOMAIN 532..641
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 310..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 672..811
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 853..922
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1003..1051
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 1217 AA; 131659 MW; 44B80287BB405C62 CRC64;
MYLKTLTLRG FKSFASSTTL KFEPGITAVV GPNGSGKSNV VDALAWVMGE QGAKSLRGGK
MEDVIFAGTA NRAPLGRAEV VLTIDNADGA LPIDYTEVTI SRLMFRSGSS EYAINGDSCR
LLDIQELLSD SGIGREMHVI IGQGQLDRVL HSGPEGRRAV IEEAAGVLKH RKRKEKALRK
LDAMQGNLTR VQDLTGELRR QLKPLGKQAE IARRAAVIQA DLRDARLRLL ADDLVTLRTR
LEQEAADEAA IRERRTETER ALGEAQRREA VLEAEEAEQA PELARVQDTW FRLSALKERL
RGVADLAAER HRNAAEAREE ERRGRDPEDM EREAAEIREQ EEMLRAALDE AQDGLANAVE
QRTGVEEALA AEERRLQAAA RAAADRREEL ARLRGRVEAL RSKAQAGRSE IGRLAEAREE
AEQRADDARV EFEAFEAEVV EDPALAAEHE AAQEALATAK DAAEAARAGV AGPRGALKEA
RAAVAAARSA DQAAQKKVTA LQARIEALNL TLASAADGGE ALLSAGADGS LDGVLGTVAS
LLNVRPGYET AVAAALGNAA EAIAVGSLDT AEAALALLRS RDAGRAGLLV GGGAVSPAAR
VPGADYAIDA VSVPEVVRPA MEHLLRDVVV VDDVPSAAAL VRREASLRAV TRDGELVGAH
WAQGGASGAQ SLLQMRATLD QATEDLAAAE TAAGVAADEL AASMEREQSA QMALEAAEAA
AGEAQARVNQ AQAELDRVGA RVREFDAKAA QEAKRAARLE ADVRAARGEV ERLTKALDAA
TESLERDTQA AEELTMRLAE SEEAAEVADE AGHDTDARDE LQARAQALRS AEMESRLAVR
TAEERVQAIT GRADALERGA RREREERARA AQRRARREEQ ARIAKAVHRG ARAALDRIEH
SLAAAVRRRE AAEQAKAARE AELKVVRTQV RELSATLERL VNVVHGNEVA RAEQRLRLEQ
YEQRALEEFG LEVESLVAEY GPDQPVPPDP EKGEDARPVP YDRAVQEKRA KAAERQLNQL
GKVNPLALEE FAALEERHAF LTSQLEDLKK TQRELLGLVK EVDDRVQEVF AAAYGDTARE
FERIFARLFP GGEGSLSLTE PDDMLTTGVE VSARPPGKKV KRLSLLSGGE RSLVAIAFLV
AVFKARPSPF YVLDEVEAAL DDTNTQRLIT VFEELRESSQ LIVITHQKRT MEGADALYGV
SMRGDGVTQV VSQRLRD
//
