ID A0A316TUW8_9BACT Unreviewed; 1176 AA.
AC A0A316TUW8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:PWN06152.1};
GN ORFNames=DDZ15_09920 {ECO:0000313|EMBL:PWN06152.1};
OS Rhodohalobacter mucosus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2079485 {ECO:0000313|EMBL:PWN06152.1, ECO:0000313|Proteomes:UP000245533};
RN [1] {ECO:0000313|EMBL:PWN06152.1, ECO:0000313|Proteomes:UP000245533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8A47 {ECO:0000313|EMBL:PWN06152.1,
RC ECO:0000313|Proteomes:UP000245533};
RA Liu Z.-W.;
RT "Rhodohalobacter halophilus gen. nov., sp. nov., a moderately halophilic
RT member of the family Balneolaceae.";
RL Submitted (MAY-2018) 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:PWN06152.1}.
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DR EMBL; QGGB01000007; PWN06152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TUW8; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000245533; 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; 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; 2.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000245533}.
FT DOMAIN 521..628
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 824..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..208
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 234..352
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 381..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 982..1019
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 1176 AA; 134887 MW; B95093A697839C1B CRC64;
MYISDLQLHG FKSFAHKTHV KFDSGITAIV GPNGCGKSNI VDALRWVLGE QRPTLLRSSA
MSNVIFNGTA KKKALGMADV SLTFVNDKGI LPVEYSELTI TRRLYRSGDS EYLINNTPCR
LKDIMDLFMD TGMSSDAYSV IELKMVEEIL NDRNNDRRRL FEEAAGVTRY KEKRRQTIRK
LDDTLKDLQR LEDILIEVRK KTRSLELQAE KAGKAKKYKT ELEHLDKAYT LHELSTIREE
LEPLQTRISN AEKEKKEIGS RVEELEESEE KARTLLIEKE RHQAEAQRRV SQLHSSIREM
ETNLKITREK IVNEEGVIRQ HQSDIEQGGK DLAELEQLRE QSISKLENFS DERERSALSL
KESKEKFADV QQQFTKVRHE LYELEIEISD LSRKLSGLQS DRIKIESRLE NTEDDQLRID
GDIRDLKDEI ENAKGELSLT REKLDSIDSE LKSEEKRLEE SSRIRQNLEE KRETLRDEIR
SLKSRKDAVE SEISLLGNLA ESGAGLPSSI SFLQKEHGDQ FALLSTVGDL LNTKEELASA
LETALGESIH FVIVKNMGDA LKASRILKEN GKGKATFIPL SELKKSYSVH EKSIARHVGS
DSSYAPVVQL LLGSTLLVDD LENAVSILEK DEATSAVTRD GDLLTASRFL KSGSNHKQAG
IRLALKDKVE KLNTESNRYE KSITQRENEL QKLNEEIDSH NLDSIRASIR QIQQRSREAE
QQSSRYQSSI QVYEKNIQEL NSRKVRLLSN QDTAREELDT LHPRQKELQQ KITELSGLQE
EKKEILRKLE EERAIAQNRY NDAQLKHQDV KNKADNLEKD LERAENGISS MKTRLASRKE
LQSESRNKIE TFKEVIEQTE KQLEGSRSQK SEADQKLAEA EEASSRQRGA INEIEKELKE
LRRRKEVNLE LVHHLSMARE KFELQAQSHS DHIWETYGIL MDQVTEQLPD ETTPEEAKAR
IGWLRQKLNK IGDVNPLAID EFREEKERLS FYEEQIDDLQ KAEAEMRETI DEINSTATER
FNETFEKIRN NFKTVFNTLF HEDDFCDLMI RDEGEDQDPL EAKIDIRANP KGKRPSSINQ
LSGGEKTLTA IALLFAIYLV KPSPFCVLDE VDAPLDDANI ERFAAMIRKF SEDTQFIIIT
HNKKTMSKAE MMYGVTMPET GVSRLVGVKL DEVAEA
//
