ID A0A100Y1E8_9ACTN Unreviewed; 1284 AA.
AC A0A100Y1E8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=ATE80_26700 {ECO:0000313|EMBL:KUH35863.1};
OS Streptomyces kanasensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH35863.1, ECO:0000313|Proteomes:UP000054011};
RN [1] {ECO:0000313|EMBL:KUH35863.1, ECO:0000313|Proteomes:UP000054011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX01 {ECO:0000313|EMBL:KUH35863.1,
RC ECO:0000313|Proteomes:UP000054011};
RA Zhang G., Han L., Feng J., Zhang X.;
RT "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT kanasensis ZX01.";
RL Submitted (NOV-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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KUH35863.1}.
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DR EMBL; LNSV01000106; KUH35863.1; -; Genomic_DNA.
DR RefSeq; WP_058944839.1; NZ_LNSV01000106.1.
DR STRING; 936756.ATE80_26700; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000054011; 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 PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 2.
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:UP000054011}.
FT DOMAIN 512..688
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 571..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1064
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 330..480
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 796..830
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 876..910
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1071..1133
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 573..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1064
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 1284 AA; 137462 MW; 8F49542C322A0992 CRC64;
MHLKALTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNSDGA LPIDYAEVTI TRIMFRNGGS EYQINGDTCR
LLDIQELLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
LDAMRANLAR VQDLTDELRR QLKPLGRQAA VARRAAVIQA ELRDARLRLL ADDLVRLREA
LDAEIADEAA LRERKERAEA DLKAAAARES ALEDEVRRLA PRLERAQHTW YELSRLAERV
RGTVSLADAR VTSATARPVE ERRGRDPEEL EREAARVREQ EAELTAALEA ADRALEDTVA
HRAELEQALA VEERRLRDAA RAIADRREGL ARLSGQAGAA RSRAAAAQAE IDRLTAARDE
ARERAAVAHE EYEALRAEVD GLDAGDADLA AAHEAATREL ADAEAALTTT REALTSAERR
RAATQARHEA LSLGLRRKDG TGALLDAAGR LTGLLGPAAE LLTVAPGHEV PIVAALGAAA
DALAVTGPAT AAEAIRLLRK EDAGRAALLV AGATEPPPPP GPGVWEPSPV AGPDVREPAP
LSGPGAQEPL SAGPDGRAAR QPPSAAPSAA VPPRAAAPAV DAARPGLPGG ALPAAGLVSG
PDELMPALRR LLRDVVVVGT LEEAEALVYA RPALTAVTAD GDLLGAHFAQ GGSAGAPSLL
EVQASVDEAA ADLAELAVRC RELAAAQEEA AGRRRACADR VEELGERRRA ADREKSAVAQ
RLGGLAGQAR GAAGEAERAD AAVARAQEAV ERATEEAEEL AERLLVAQEA PTEDEPDTSV
RDRLAADGAN ARQTEMEARL QARTHEERVK ALAGRADSLD RAARAEREAR ARAERERARL
RHEAEVAAAV ASGARQLLAH VEVSLVRAEA ERSAAEEGRA VRERELAAAR ARGRELKAEL
DKLTDSVHRG EVLGAEKRLR IEQLETRALE ELGVDPAVLV AEYGPDQPVP AAPPAPGEQR
PAPGEDASAA HRREPAAAED ASAAHRREPA PGGDRPDDPG RAGDALRPFV RAEQEKRLKA
AERAYQQLGK VNPLALEEFA ALEERHRFLS EQLEDLKRTR ADLLQVVKEV DERVQQVFAE
AFRDTAREFE GVFSRLFPGG EGRLVLTDPG DLLGTGVEVE ARPPGKKVKR LSLLSGGERS
LTAVAMLVAI FKARPSPFYV MDEVEAALDD TNLQRLIRIM RELQESSQLI VITHQKRTME
VADALYGVSM QGDGVSKVVS QRLR
//