ID A0A1I2YNB9_9RHOB Unreviewed; 1147 AA.
AC A0A1I2YNB9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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 ORFNames=SAMN04488021_1054 {ECO:0000313|EMBL:SFH26516.1};
OS Paracoccus aminovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH26516.1, ECO:0000313|Proteomes:UP000183635};
RN [1] {ECO:0000313|EMBL:SFH26516.1, ECO:0000313|Proteomes:UP000183635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH26516.1,
RC ECO:0000313|Proteomes:UP000183635};
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; FOPU01000005; SFH26516.1; -; Genomic_DNA.
DR RefSeq; WP_074966398.1; NZ_LN832559.1.
DR AlphaFoldDB; A0A1I2YNB9; -.
DR STRING; 34004.SAMN04488021_1054; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000183635; 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; 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; 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; 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:UP000183635}.
FT DOMAIN 4..1132
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 423..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..204
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 251..278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 769..824
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 946..987
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 441..462
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 1147 AA; 123257 MW; 6EF39393B6ED690D CRC64;
MRFDRLRLNG FKSFVDPTDL VIREGLTGVV GPNGCGKSNL LEALRWVMGE NRPTAMRGEG
MEDVIFAGTA RRSARAHAEV TLTIDNKDRL APAGMNDADS LDITRRITRD AGSAYRINGK
DVRARDVQML FADASTGAHS PALVRQGQIS ELINAKPKAR RRILEEAAGI SGLYQRRHEA
ELKLNGAEAN LTRVDDTLDQ LSTQAASLAR QARAAARYRE IGAALRRAEG VLLYRRWAEA
DQAKAATAEA LRAAIRAAAE AEAQARRAIA AREGAEATLP PLREEEQVAA AILSRATVER
EALDEAEARA AQTIQTLLAR IAQLDRDIER ESALNRDAGE VIARLDWERR ELDKAGQGHE
DRLALASETA DEAAEALREV EAKLAELTDE SARLAARHHS AERLAQDLRQ MLDRAGRAAQ
EAEAAAARAA DAGTQADAAR EAAEEAQEAA RDRVEQAEDT LAAAEESRAA LEAEESAARS
ARAEAEGEVS ALNAEMAALK RLVERGQGGG AILELVRVAR GHEAAFGAAL GDDLGVGLAG
DGSGWHLLPG YDAPQPLPAG AEPLAPHVEG PEALGRRLSQ VGLVADAATG AAMQAQLAPG
QRLVTRDGDL FRWDGMRVMA GEASSAAALH LQKVNQLAEL TGQAAAAQAR AAAAQAAHQA
LRDRHLAAAE AEKRARDARR DAERGLSEAV RAVTRAESDL SMAQSRAESA RAELARHRDD
AADARKRLAE AERALADLPD RGAAAAAVEH ARTGAEAARI ATLTRRGALD ELRREANART
KRLQEIAKEE SGWRLRLDQA GTRAAELAAR RDEAAADLEE AEAQPEILAE RRAVLTESEA
QAAARLARAR AALSAADQAL RIAAEAEREA ERAASDARET RAAREARAEA ATEAEAAARL
RIHEELEATP EALLDSLGEV EEIAPDALED RIARLRQQRD ALGAVNLRAD EDKRELEAER
DRLGAEKADL TEAIRKLRQG IGSLNREGRE RLLAAFDTVN ANFTTLFTHL FGGGEARLVL
VESDDPLEAG LEIMCQPPGK KLSTLSLLSG GEQTLTALAL IFAVFLANPA PICVLDEVDA
PLDDANVTRF CDLMDEMTRR TDTRFLVITH HAVTMARMDR LFGVTMVEQG VSQLVSVDLK
RAEALVA
//
