ID A0A286E105_9ACTN Unreviewed; 1189 AA.
AC A0A286E105;
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=SAMN06297387_11837 {ECO:0000313|EMBL:SOD64586.1};
OS Streptomyces zhaozhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1300267 {ECO:0000313|EMBL:SOD64586.1, ECO:0000313|Proteomes:UP000219072};
RN [1] {ECO:0000313|EMBL:SOD64586.1, ECO:0000313|Proteomes:UP000219072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7095 {ECO:0000313|EMBL:SOD64586.1,
RC ECO:0000313|Proteomes:UP000219072};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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; OCNE01000018; SOD64586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286E105; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000219072; 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; 2.
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:UP000219072}.
FT DOMAIN 512..627
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 418..487
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 976..1038
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 315..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1189 AA; 129012 MW; 92281086E549441A CRC64;
MHLKSLTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNADGA LPIEYAEVTI TRTMFRNGGS EYQINGDTCR
LLDVQELLSD SGIGREMHVI VGQGQLDSVL HADPAGRRAF IEEAAGVLKH RKRKEKALRK
LDAMQANLAR VQDLTDELRR QLKPLGRQAA VARRAAVIQA DLRDSRLRLL ADDLVTLRGA
LRAEVADEAA LKERKEAAEE RLKGALRREN ELEQEVRTLV PRVARAQETW YQLSQLAERV
RGTVNLADAR VNSARSQPAE ERRGREPEEL EREAARVREQ EAELTAALEA AGVALEDTVA
HRAELERALA DEERRLKDEA RALADRREGL ARLHAQANGA RGRAASAGAD RERLTASRDE
ALLRATEARE AYEALRAEVE GREADDGELA EAHERAKDEL DDAETALSAA RERLTGVERE
RAAVEARREA LALGLRRKDG TGALLGAGEE LAGVLGPAAE LLTVTPGYEV QVAAALGAAA
ESVAVAGPAE AVEALRLLRK RDAGRAALLV GGPAADDHGA PAAEPAPAPW CWAVDLVRGP
AALLPAVRAL LRDVVVVDTL DDALRVVQAR PGATAVTGEG DVLSRRLAGG GSAGAPSLLE
VRASVDEATA ERERLTALAA ELTEARDAAT ERRRAARAAV DELAGRRSAA ERERSRVAQD
LGRLGGQARA AAGEAERAEA AVERAGEEWA RAVEQAEELA ERLAVAEEAS ETVEDPDTSA
RDRLAADGAN ARQTEMEARL QVRTHEERVR GLSGRADGLD RAARAEREAR ARAERRKARA
RHESEVAGAV ADGSRQLLAH VEASLARAET ERAAAEAARA ERDRALDRER AAGRELKEEL
DKLTDSVHRG EVLGAEKRLR IEQLETRALE ELGIEPAGLV AEYGPDQPVP PSPPADGEEL
PQDPEHPRNQ PVPFVRAEQE KRLRAAERAY KQLGKVNPLA LEEFAALEER HQFLSEQLED
LKKTRADLLQ MVKEVDERVE QVFTAAYHDT AREFEGVFSR LFPGGEGRLV LTDPDSMLTT
GVEVEARPPG KKVKRLSLLS GGERSLTAVA LLVSIFKARP SPFYVMDEVE AALDDTNLQR
LIRIMRELKD SSQLIVITHQ KRTMEVADAL YGVSMQGDGV SKVISQRLS
//
