ID A0A0M8WR67_9ACTN Unreviewed; 1189 AA.
AC A0A0M8WR67;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=ADL01_00220 {ECO:0000313|EMBL:KOV88823.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV88823.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV88823.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV88823.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) 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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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:KOV88823.1}.
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DR EMBL; LGDW01000001; KOV88823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8WR67; -.
DR PATRIC; fig|1519490.3.peg.46; -.
DR Proteomes; UP000037738; 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; 1.10.287.1490; -; 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; TIGR02168; SMC_prok_B; 1.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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:UP000037738}.
FT DOMAIN 507..628
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 305..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 162..196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 243..270
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 816..850
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 310..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1189 AA; 128811 MW; 37522866FAD5A93E CRC64;
MTLRGFKSFA SATTLRFEPG ITCVVGPNGS GKSNVVDALS WVMGEQGAKS LRGGKMEDVI
FAGTTGRPPL GRAEVSLTID NSDGALPIEY AEVTITRIMF RNGGSEYQIN GDTCRLLDIQ
ELLSDSGIGR EMHVIVGQGQ LDSVLHADPM GRRAFIEEAA GVLKHRKRKE KALRKLDAMK
ANLARIQDLT DELRRQLKPL GRQAAVARRA AVIQADLRDA RLRLLADDLV RLRGALRTEV
ADEAALKERK ETTEAELKKA LQREALLEDE VRQLTPRLQR AQQTWYELSQ LAERVRGTVS
LADARVKSAT SAPAEERRGR EPEDMEREAA RIREQEAELE AALEAAEHAL EDTVAHRADL
ERELVIEERR LKDLARAIAD RREGLARLNG QVNAARSRAA SAQAEIDRLA AARDEAQERA
VAAQEEYETL QAEVDGLDAG DADLAQRHDT AKAALADAEA ALTAAREAAT AAERRRAATQ
ARHEALALGL RRKDGTGVLL AARDSLTGLL GPAAELLTVT PGHEVAVAAA FGAAANAIAV
TTPASAASAI RLLHKQDGGR ASLLLAGAPE EAGSGTGTDA ADGQGSAPGG PPRAADLVRG
PAELMPAVRR LLRGIVVVGT LEDAEELVYA RPELTAVTAE GDLLGAHFAH GGSAGAPSLL
EVQASVDQAA AELDELAVRC EELVGVQQLA GERRKECAAF LEELGERRRA ADREKSTVAQ
QLGRLAGQAR GAAGEAERST AAAARAQDAL DRAVQDAEEL AERLAVAEEM PVEEEPDTGV
RDRLAADGAN ARQTEMEARL QVRTHEERVK GLAGRADSLD RAARGEREAR ARAEQRRARL
KHEASVAEAV ASGARQLLAH VEVSLSRADE ERTAADAAKA RREQELTAAR AAGRDLKGEL
DKLTDSMHRG EVLGAEKRLR IEQLETKALE ELGVEPEGLV AEYGPHQLVP PSPPAEGEEL
PEDPEHPRNQ PKQFHRAEQE KRLKATERAY QQLGKVNPLA LEEFAALEER HKFLSEQLED
LKKTRADLLQ VVKEVDERVE QVFTEAYRDT AVQFEGVFSR LFPGGEGRLI LTDPDNMLTT
GVDVEARPPG KKVKRLSLLS GGERSLTAVA LLVAIFKARP SPFYVMDEVE AALDDTNLQR
LIRIMQELQE ASQLIVITHQ KRTMEVADAL YGVSMQGDGV SKVISQRLR
//
