ID A0A1H6E5T7_9ACTN Unreviewed; 1309 AA.
AC A0A1H6E5T7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05216223_12639 {ECO:0000313|EMBL:SEG92613.1};
OS Actinacidiphila yanglinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310779 {ECO:0000313|EMBL:SEG92613.1, ECO:0000313|Proteomes:UP000236754};
RN [1] {ECO:0000313|EMBL:SEG92613.1, ECO:0000313|Proteomes:UP000236754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2023 {ECO:0000313|EMBL:SEG92613.1,
RC ECO:0000313|Proteomes:UP000236754};
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; FNVU01000026; SEG92613.1; -; Genomic_DNA.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000236754; 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; 1.10.287.1490; -; 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 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; 2.
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:UP000236754}.
FT DOMAIN 515..738
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 309..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..194
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1086..1148
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 630..645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..824
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 1309 AA; 139854 MW; 5096FFB6BFE0239C CRC64;
MHLKSLTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNTDGV LPIEYAEVTI TRIMFRNGGS EYQLNGDACR
LLDIQELLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
LDAMQANLAR VTDLTGELRR QLKPLGRQAQ VARRAAVIQA DLRDARLRLL ADDLVALREA
LRAEVADEAA LKERKDAVET ELTAAVQREA RLEEQVRALT PRVNDAQATW YALSQLTERV
RGTIGLAEQR HRHAVGQPAE ERRGRDPEDM EREAARIREQ EAELTEALDA AERALEDTVG
HRAELERRLA EEETRLRAAA RAIADRREGL ARLNAQVNAA RSKAGSAEAE IGRLASARDE
ARDRAESAQA EYEELRAQVE GLDADDTELE ARFEAARSAQ AAAEEEFSAA RDAATTAERR
RAAVAARRDA LAPSLRRKDG TGALLARAGT PDGLAGVLGS AATLLRVAPG YEVPVAAALG
VAADAVAVTG PAAAAEALRL LRKEDGGRAA LILAAAPASV SATGPAGTAD GPGPGPSRSG
GDAAVLPGQS AGDRTYAGAD RDPQHGRVPG PAGPAAPPPA DPGAPPADGR DLGRVPGPAR
PAGTAGSAGP ETGAAPGAAP QETRQAQAVA APEAAALPGR ARHAVELVAA DADLLPAVRR
LLHGIVVVPT LEDAEAVVAS RPELTAVTAE GDVLAAHLAQ GGSAKAPSVL EVQAQVDEAG
AELERLAAEC EELAERQQAA KERRAAASRE VDELGQRRRA AEKAKSSVAQ QLGRYGGQAR
AAAGEADRAA AAVVRAEESL AAAREELEEL SYRLSEAQEE PGEEEPDTFA RDRLAADGAN
ARQTEMEARL QVRTHEERVK SLAGRADGLD RAARAERETR ARAERRRARL AYEASVAAAV
LAGARGLLEC VQVSLGRAEA ERVAAEQARA EREAGLGAER RRGRELKSEL DRLTGDVHKG
EVLGAEKRLR IEQLEAKALE EHGMEPAGLI GEYGPELLVP PSPPAEGEVL PEDPEHPRNQ
PVPYVRSEQE KRLKAAEKAY AQLGKVNPLA LEEFAALEER HKFLTEQLED LRKTRADLLQ
VIKDVDERVE QVFTAAFHDT AREFEGVFSR LFPGGEGRLL LTDPDNMLTT GVEVEARPPG
KKVKRLSLLS GGERSLTAVA MLVSIFKARP SPFYVMDEVE AALDDTNLQR LIRIMEELQE
SSQLIVITHQ KRTMEVADAL YGVSMQGDGV SKVISQRLRD GKRATAPAV
//
