ID A0A1H1AC30_9ACTN Unreviewed; 1226 AA.
AC A0A1H1AC30;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN04489764_0423 {ECO:0000313|EMBL:SDQ37207.1};
OS Thermostaphylospora chromogena.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermostaphylospora.
OX NCBI_TaxID=35622 {ECO:0000313|EMBL:SDQ37207.1, ECO:0000313|Proteomes:UP000217103};
RN [1] {ECO:0000313|EMBL:SDQ37207.1, ECO:0000313|Proteomes:UP000217103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43794 {ECO:0000313|EMBL:SDQ37207.1,
RC ECO:0000313|Proteomes:UP000217103};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNKK01000002; SDQ37207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1AC30; -.
DR STRING; 35622.SAMN04489764_0423; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000217103; 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; 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:UP000217103}.
FT DOMAIN 536..647
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 423..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 706..733
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 762..817
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 864..954
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1008..1070
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 1226 AA; 132476 MW; 12C00648030ADDBA CRC64;
MYLKKLTLRG FKSFASATVL RFEPGITCVV GPNGSGKSNV VDALAWVMGE HSAKSLRGGK
MEDVIFAGTA SRPPLGRAEV TLTIDNSDGA LPIDYTEVTI SRLMFRSGQS EYAINGEPCR
LLDIQELLSD SGIGREMHVI VGQGQLDAVL HAGPEERRAF IEEAAGVLKH RKRKEKALRK
LDAMQANLTR LQDLTAELRR QLKPLGRQAE IARKAAVIQA DLRDARLRLL ADDVLTLRET
LRKEEADEAA VLARRAEVEA ELETAQHREA ELEAAESSAQ PRLTAAQETF FRLSALRDRL
RGLAGLAAER HRNALEAAAV ERRGRDPEDY EREAEQVREE EERLIGELET ARDMLDRAVA
ERSAAEAALA AEERRLADAA RAAAARREEL ERLRGQVGAV RSRARAAEEE IGRLAAAVEQ
AAERAERARA EHDAQASAEP EADHELAREL ELAQEGVTAA EEAAEAARAA AEQAEREIDA
PRAALAEARS ATAAARAADQ EAQRAVAALE ARKEALELGL SRGGDGAEAV LAAGLPEVMG
PLAAVMTVKR GAEAAVAAAL GDAAEAVVVG SLPAAVDVVE FLRSREAGRS TLLVGSGEAA
SAQARPQVPG EWAADLVDVP EALRPAVHHL LGDVVVVDDL GTARKVVETH PRLRAVTRDG
DLVGAYLARG GTADGTSGLQ VRAALEAAVA DLAAARATAE ATAGELERAV ADERAAQEAV
EAATARAQEA RAQVSAAQSG VSAAQAALDR VRARQREHDQ KAAAAARRLA QLAAAAEAAE
AERARLAEAV RAAEEARDRD VAGLADLEER LAAAERESEL EVEPTTEIRD ELAAACEAAR
QTEMETRLAV RTAEERVNSI AGKAEALLRA ARREREERQA AAAERARRRR QAEVARAVAA
GAEHALGVLE SSIAAAAAER DEAEAARGEI DAELKAVRAR VRELTAELDK LVNRAHGSEV
ARTERRMRLE QLEQRALEEF GIEPDALVAE YGPDVPVPAD PEPVPYVREE QEKRARTAER
QMAQLGKVNP LALEEYAALE ERHAFLTSQL EDLKKTRRDL LTVVKEVDER VEQVFAAAYE
DVAREFQSIF TRVFPGGEGR LVLTDPSDML TTGVEVEARP PGKKVRRLSL LSGGERSLTA
VAFLISIFKA RPSPFYVMDE VEAALDDTNT QRLLTLFEEL RQNSQLIVIT HQKRTMEIAD
ALYGVSMRGD GVSQVVSQRL RERDTA
//
