ID A0A0A7KKL3_9DEIO Unreviewed; 1108 AA.
AC A0A0A7KKL3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=QR90_08180 {ECO:0000313|EMBL:AIZ45098.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ45098.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; CP010028; AIZ45098.1; -; Genomic_DNA.
DR RefSeq; WP_039683752.1; NZ_CP010028.1.
DR AlphaFoldDB; A0A0A7KKL3; -.
DR STRING; 1182571.QR90_08180; -.
DR KEGG; dsw:QR90_08180; -.
DR HOGENOM; CLU_001042_2_2_0; -.
DR Proteomes; UP000030634; 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 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; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 3.
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|HAMAP-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|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000030634}.
FT DOMAIN 480..593
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 328..432
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 677..711
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 880..938
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1108 AA; 118385 MW; 4D62D25679C5EF5B CRC64;
MLRSITLQGF KSFAERTRLE FGPGVSAVIG PNGSGKSNVV EGLRWVTHGA RARELRAGRG
SELIFHGSGG KAPHGLAEVQ LELQTPEGRV NLSRRIYRDG AGEQDLNGKP VRARDVQAAL
RGTGLGPGGL AVIGQGEVSG VVGAEGRTLL GHVQEAAGLS RAVSARQETE ARLKDADSHL
AQLRLLLGER EAAVSRLERA ATQARRWREL TLRTLTLEDA LKRERQAALH REIAGARAET
AQLDIQSASL AAEVQTAAAV VEGAREAAQD ARARRDAHAG ALDALRAARD AHAQAERYRA
HLRGEAEGLQ SELASLPTSP PAQPAPDLAA LEAASARIRS DAENAERRAR TLDAELTRAR
TLAARAAEGL ARTEASRETL RAELERAEGN LEAAAEGLEA ATERLTTARH TREDAEAQYA
AVAAEREAAV SQERHLTNEL ARVNASVAPL RRERERLQTA LNSYARYGEG ARNALRLDHP
GIVGSVADLL TVPAEYETAI GAALGRRLEQ VVVNRADDAR DIIEELKRSG GRATFLPLDL
LRARPRRDAQ FLHELGVVGN LADLCPSDPP LVGQAILADT LVVQDLRAAN RIARSHSNRP
RLVTLDGELV EPGGAITGGR LRDSGAGVLG DQRRFQELEA ELEEADALGT RFSAELERLR
LTLGGGDERH DGLLAARERA AREERDAERR VTELTAQIRS LGENRDRLLA RLGPEQEVTS
VLDLPDVAAL ETELTAARHT AETGRATERE AAEALALARE LSAAWRAYES AQIRAADLRA
RLNANAGAAA TQDAHLSAAA AELARREAAL GELDEAEFPH AEAAREAAAA AYANLIGTQN
KVRARLDDLR VLIARREGSL EPLPAGCTPP GTPREWTAEL ARARAELETL GTVNARAEAD
HAAELAELSA QRAEAEDAES ATAELRAHLG ELQDAEGKAT RAAFSRVNAA FREYSAELLG
GEGELEGESD DSGRLTGLRL AVQPKGKRTR NLNLLSAGER TMAGLGFLFA LNHAGGDGSG
LQEGAGGLPL AVLDEVDAPL DEANIRRFTA FLERFSARGA QFLLVTHQKA TMEVATALWG
VTTDGSGASR VLSIRQTEDG ARRVPVEG
//
