ID A0A1H6HXR0_9EURY Unreviewed; 1198 AA.
AC A0A1H6HXR0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05192561_101562 {ECO:0000313|EMBL:SEH39884.1};
OS Halopenitus malekzadehii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1267564 {ECO:0000313|EMBL:SEH39884.1, ECO:0000313|Proteomes:UP000199215};
RN [1] {ECO:0000313|EMBL:SEH39884.1, ECO:0000313|Proteomes:UP000199215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10418 {ECO:0000313|EMBL:SEH39884.1,
RC ECO:0000313|Proteomes:UP000199215};
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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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DR EMBL; FNWU01000001; SEH39884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6HXR0; -.
DR STRING; 1267564.SAMN05192561_101562; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000199215; 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; 1.10.287.1490; -; 2.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.340; -; 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; TIGR02169; SMC_prok_A; 1.
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; SSF46579; Prefoldin; 1.
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:UP000199215}.
FT DOMAIN 542..656
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 910..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..520
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 910..931
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 1198 AA; 134510 MW; 1DAD9D8BF7737E11 CRC64;
MHITEVVLDD FKSFGRTTRI PFYEDFTVIT GPNGSGKSNI IDGILFALGL ARTRGIRAEK
LTDLIYNPGH DGAESGDGPD EAAVTVVLDN SDGTLDRGQV VSAAGSENVG DVEEITVKRR
VKRTDDNYYS YYYLNGRSVN LSDIQDLLAQ AGVTPEGYNV VMQGDVTEII NMTAYQRRGI
IDEIAGVAEF DEKKEAAFEE LEAVEDRIGE ADLRIGEKED RLDRLADERE TALEYQSYRE
EQEEYRGYRK AAELEEKRET REEVFAEIEE TEAELADRRA ELDTRQGRVT RLESELSELN
DEIERTGEDE QLAIKAEIEE IKGDISRLEG QIENAESRLE EAETDRRDAF VQIDRKQETI
DDLEADAKEI KVEKASVKAD VADKRSELAE IEAEIDGIDT QYDELKADLA ENKERLEELK
ADKNDVQREK DRLLDEARRR SNEISEAQSD LEEAHERIPD LKARISELHG ELDTAETNRD
AIEETIADLF AEKTERQERL DALEDDLREK QSEYATLEAD AKNRGDTSWP RAVTTIRNAG
IDGVHGPVGE LASVDPTYAE ACETAAGGRL ANVVVDDDGV GETCIDHLKS RNAGRATFLP
ITELDDRGLP NAPTMPGVVD FARNLVEYDA RYDPVFSYVL GSTLVVEDMA TARDLMGDYR
MVTLEGDLVE TSGAMTGGSG GGSRYSFSTA GGGKLQRLAE EIEELEDERQ SLESEIDDLD
AEIDDARERK ADAEERVRSV EADIDRAETD LEDGHDRIEE LESTLETLHT EREEVDERMT
ELDAEIEELA SEQAAVEDRI AEIEAELADS RIPELTSRAD DVRDEIEDLE SRMDDLDGRL
NEVQLEKEYA EDAVEELHDR IEAAQNKKAE AEETIADHEA AIEEKRELLA EKRDEIEDLE
EELAELKAER SDLRETLSAA TEERDEQRQR VSTVESTLSD LCDRADRLEW EIDELESQVG
DYDPESIPDH DEVERRIEEL DAEMEALEPV NMRAIDEYDE VEAALDQLQE RRDVLVTERD
GIEERIAEYE SQKKRTFMDA FESINDHFED IFERLSAGTG ELVLENPEDP FEEGLTMKAQ
PADKPVQRLD AMSGGEKSLT ALAFIFAIQR HNPAPFYALD EVDAFLDAVN AERVGEMVHD
LAGEAQFVVV SHRSALLERS ERAIGVTMQE DNVSAVTGMQ FGADGEEADG DGEVPADD
//
