ID A0A090XY61_PAEMA Unreviewed; 1190 AA.
AC A0A090XY61;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:KFM90507.1};
GN ORFNames=DJ90_6372 {ECO:0000313|EMBL:KFM90507.1}, GNQ08_15605
GN {ECO:0000313|EMBL:MUG23816.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFM90507.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFM90507.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFM90507.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MUG23816.1, ECO:0000313|Proteomes:UP000442469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CT49 {ECO:0000313|EMBL:MUG23816.1,
RC ECO:0000313|Proteomes:UP000442469};
RA Olajide A.M., Chen S., Lapointe G.;
RT "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL Submitted (NOV-2019) 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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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:KFM90507.1}.
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DR EMBL; JMQA01000058; KFM90507.1; -; Genomic_DNA.
DR EMBL; WNZZ01000011; MUG23816.1; -; Genomic_DNA.
DR RefSeq; WP_036622175.1; NZ_WNZZ01000011.1.
DR AlphaFoldDB; A0A090XY61; -.
DR STRING; 44252.DJ90_6372; -.
DR GeneID; 77006678; -.
DR PATRIC; fig|44252.3.peg.6367; -.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000029278; Unassembled WGS sequence.
DR Proteomes; UP000442469; 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 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; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
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:UP000029278}.
FT DOMAIN 521..640
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..462
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 682..723
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 759..884
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 920..947
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1190 AA; 135582 MW; 0DF4D7471E07E141 CRC64;
MFLKRIELAG FKSFADKTEM EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
MEDIIFAGSD ARKAVNYGEV SLTLDNGDQA LPLDFSEVTV TRRVHRSGES EYYINKQACR
LKDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKRDARRK
LDDTEQNLLR IHDLISELED QVGPLKEQSE KALKYKELRE QLKNKEISLY VHQIEQIHES
WSEANAKLTK LQEEQLALST VVSAHDAKLE SDRLALRQVE DRIEQLQAQL LEYSESYEKS
EGYGEVLKER AKNLAQNREQ LRQSLAVSEE RYAQRSQELE QLTAKFAAAE QQLQELRREL
ADEEAKLIGV TGGISQAQEE GLKGQLLEIM NQMAQARNEI HYAEQQKESV KRRMDRAEEE
GVKWTEEQQR LKARKSELEA ALEKLGKEIS DLRSKYIQES ERHQSLQKLV EESQGGIRKW
EQKREGLVSR RDTMKEMEED YDGFMLGVKE VLKAAKKSML PGVHGAVAEL IRVPEKLEIA
VETALGGAMQ HIVMENEAVS RQAIAFLKQR QLGRATFLPL DVIRPRQISP ADKRLMEDAE
GFVGIGAELV GYEPRYADIV GSLLGNVVFA TDLEKANKMA ARCQYRFRIV TLEGDVVNAG
GSMTGGSQHR KNSNLLGRKR QLDQLAADIR ESEEMLDKLR KGLADVRSQV AKSESDLNRL
REAGDAKRAE EQAVAGDLKQ AQHEWRHVSE QFELYGQEKG HYQKELEELE ATKKAAEERL
AELEKEEQSV QQSIRAAEFA RKASESAKEE LQDLLTGLKV REGKLDQECS SLREQLRRAE
EEYKIQQREL EQNRTILQSI EADLQQNEEQ SVRQREELND FKLKKERAGE QLEMERASRT
VLVKKLEEGE SETKEQRIGL KAVEEQLRQT EIQANRLDVE LDNILRKLSE DYELSYELAK
QRYAVPEDVP QTQAEVKELK RQITLLGEVN LGAIEEYNRV NERYQFLTEQ KDDLVEAKTT
LYQVIREMDE EMSKRFKVTF DAIRREFVIV FSKLFGGGRA DLVLLDPDNL LETGIDVVAQ
PPGKKLQNLQ LLSGGERALT AMALLFAILQ VKPVPFCVLD EVEAALDEAN VSRFAQYLRE
FSEQTQFIVV THRKGTMEEA DVLYGVTMEE GGVSKLVSVK LDDEDTMEIA
//
