ID A0A0G3UP64_9ACTN Unreviewed; 1265 AA.
AC A0A0G3UP64;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=M444_24645 {ECO:0000313|EMBL:AKL68079.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL68079.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL68079.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL68079.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
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; CP011664; AKL68079.1; -; Genomic_DNA.
DR RefSeq; WP_047960708.1; NZ_CP011664.1.
DR AlphaFoldDB; A0A0G3UP64; -.
DR KEGG; strm:M444_24645; -.
DR PATRIC; fig|465541.12.peg.5212; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000035653; Chromosome.
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; 3.40.50.300; 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:UP000035653}.
FT DOMAIN 510..704
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 308..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1051
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 735..769
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 819..846
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 892..954
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1080..1114
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 315..332
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 1265 AA; 135170 MW; 2BCA9E2E6F120614 CRC64;
MHLKSLTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNSDGV LPIDYAEVTI TRIMFRGGSS EYQINGDTCR
LLDIQELLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
LDAMRANLAR VQDLTEELRR QLKPLGRQAA VARRAAVIQA DLRDARLRLL ADDLVTLRGA
LDAEIADEAA LKERKESAEA ELAAALRREA ELEASVRELA PRLARAQQTW YELSQLAERV
RGTESLAQAR VKSASAPVED ERRGRDPQDM EREAARIREQ EAELTAALEA ASRALEDTVE
HRAELERSLA EEERRLRDAA RAIADRREGL ARLTGRLGAA RSRAGSAQAE IDRLVAARDE
ARSRAAAAQT EYEALAEEVG GLDDASAEAE YEAARVALAE AETELLAARD GLAETERSRA
AVAARRDALA LGLRRKDGTG AVLAARGRLE GLLGPAAERV SVAAGYEVAV AAALGAAADA
VAVATVSGAA AAIRHLRTTD AGRATFLITP PPLPNQPATP AASPLPGQGA GPMDPAIPGQ
AASAADSVLP RQGADLPDAS FPGPGPGGRV GPGHQAPSAI EARGFGGGAP DGGAAGVATA
VATGGGGVAA GELVGGEDGA VRALRAVLRD FVVVRDLDEA QALVAARPDA VAVTAEGDVL
GAHLAHGGSA GAPSLIEVRA AVDEAAAELA RLDARRETAV ARRQAAQARR EEAGTLVEDL
GRRRRAAEQA RAGVAQQLGR LAGQAKGAAG EAERGASAAA KAQDALEQAL AEVEECAERL
AIAEEMPVEE EPDTAARDRL AADGANARQT EMEARLQLRT HEERVKGLAG RADGLDRAAR
AEREARQRAE RRRVRLRHEA EVARAVADGA RQLLAHIEVS LRRAERERSA AEHAKGLRER
ELDGARGRGR DLKGELDKLT DSVHRGEVLG AEKRLRIEQI EGRALEEFGV EAAALAAEYG
PDQPVPPSPP AEGERLPEDP EHPRNLPGPF VRGEQEKRLR AAERAYQQLG KVNPLALEEF
AALEERHQFL SEQLDDLRRT RADLLQVVKE VDQRVEQVFT EAYRDTAREF EGVFSRLFPG
GEGRLVLTDP DDMLATGVDV EARPPGKKVK RLSLLSGGER SLTAVALLVS IFKARPSPFY
VMDEVEAALD DTNLQRLIRI MEELQESSQL IVITHQKRTM EVADALYGVS MQGDGVSKVI
SQRLR
//
