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Database: UniProt
Entry: A0A1X7A7U9_9RHOB
LinkDB: A0A1X7A7U9_9RHOB
Original site: A0A1X7A7U9_9RHOB 
ID   A0A1X7A7U9_9RHOB        Unreviewed;      1151 AA.
AC   A0A1X7A7U9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:SLN72838.1};
GN   ORFNames=ROA7450_04066 {ECO:0000313|EMBL:SLN72838.1};
OS   Roseovarius albus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN72838.1, ECO:0000313|Proteomes:UP000193061};
RN   [1] {ECO:0000313|EMBL:SLN72838.1, ECO:0000313|Proteomes:UP000193061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN72838.1,
RC   ECO:0000313|Proteomes:UP000193061};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-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. {ECO:0000256|HAMAP-
CC       Rule:MF_01894}.
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DR   EMBL; FWFX01000020; SLN72838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7A7U9; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000193061; 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   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; 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; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
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:UP000193061}.
FT   DOMAIN          4..1136
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   REGION          406..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          184..218
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          289..334
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          936..991
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        713..742
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..819
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..888
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   1151 AA;  126632 MW;  383A7E234584501C CRC64;
     MHFSKLRLTG FKSFVDPTDL IITDGLTGVV GPNGCGKSNL LEALRWVMGE NRPSIMRGGG
     MEDVIFAGAA SRPARNFAEV VCHMDNSDRL APAGFNDADH LEVIRRITRD VGSAYKVNGK
     DARAKDVQML FADASTGAHS QALVSQGKIT DLINAKPKAR RKILEEAAGI SGLYQRRHEA
     ELKLKGAETN LARVDDVIEQ LATQLVQLAR QARQAQRYRA IGEDLRRSEG LLLYRRWKEA
     DLARAAADEE LRERITGAAR MEAAAREAAK LRVQAEDALP ALREEEAIAA AVLQRLQVQR
     DTLNEQEQNA RTRIETLTSR IEQLSRDIER EASLNRDAGE TIERLEWEAR ELGKAGEGHD
     ERLEIASEEA HEAAAVLQQR ETDLGQLTED VARLAARHHS AQRLLDDSRK MLGKSETEST
     RAREAAQGAK EAEARAAQEF EIAQQAEEEA QHIAEEAELA LNAAEEARME TQDREVTARA
     ERSEAEGELN ALSAEVTALA KLLERDTAEG GQILDRLQVT SGYEKALGAA LADDLRAPEV
     SADGPSGWAL LPGYSNAQTL PAGVNALSSY VNVPEVLARR IGQIGLVSGD DGPRLQAELN
     PGQRLVSREG DLWRWDGYRA WAEDAPSAAA LRLEQLNRLE ELKQELAHAT ARAEGAQQAH
     EALSLMLARQ TEEDRAAREA RRAADAQVTQ ASRTLSRAEA DRNLAASKHE SLGLAVTRHE
     EEAMEARKQL SEAEKGQTDL GDLDEARAQV DDVKMTVEAA RITMMSRRSA HDEIRREGES
     RTKRSQEVAK EVSGWRHRLE TAEKRSSELA ERKYTTEEEL VEASAAPEEI AAKREELGEQ
     IDKSGARRAE AADALSVAES AAREAVAGER DAERNASDAR EARARSEARM EAARETVAVA
     AERITEELEL APEALLEQLD VNPDEMPASD QIEADVNRLK RQRDALGAVN LRAEEDAREV
     EEEHTTLVNE KNDLEEAIRT LRSGIASLNK EGRERLLTAF EQVNSNFQML YKHLFGGGEA
     NLVMVESDDP LDAGLEIMCQ PPGKKLSVLS LLSGGEQTLT VAALIFGVFL ANPAPICVLD
     EVDAPLDDAN VGRFCDLLDE MCRRTETRFL IITHHAVTMS RMDRLFGVTM AEKGVSQLVS
     VDLKKAEQMV A
//
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