ID A0A1H3IUL1_9EURY Unreviewed; 1198 AA.
AC A0A1H3IUL1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05216564_104243 {ECO:0000313|EMBL:SDY30584.1};
OS Halopenitus persicus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1048396 {ECO:0000313|EMBL:SDY30584.1, ECO:0000313|Proteomes:UP000199079};
RN [1] {ECO:0000313|EMBL:SDY30584.1, ECO:0000313|Proteomes:UP000199079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC30,IBRC 10041,KCTC 4046 {ECO:0000313|Proteomes:UP000199079};
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; FNPC01000004; SDY30584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3IUL1; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000199079; 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; -; 3.
DR Gene3D; 1.20.1060.20; -; 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; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 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}.
FT DOMAIN 542..656
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 726..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..520
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 1198 AA; 134869 MW; DD035B0A41091727 CRC64;
MHITEVVLDD FKSFGRTTRI PFYEDFTVIT GPNGSGKSNI IDGILFALGL ARTRGIRAEK
LTDLIYNPGH DGAESGDGPD EAAVTVVLDN ADGTLDRGQV VSAAGSENVG DVEEITVKRR
VKRTDDNYYS YYYLNGRSVN LSDIQDLLAQ AGVTPEGYNV VMQGDVTEII NMTAYQRRGI
IDEIAGVAEF DEKKEAAFEE LEAVEDRIGE ADLRIEEKED RLDRLADERE TALEYQSYRE
EKEEYRGYRK AAELEEKREA HESVQAEIEE TEAELAERQE KLDTRQGRVT RLEAELAELN
DEIERTGEDE QLAIKAEIEE IKGDISRIEG RIENAESRLE EAEAERRDAF VQIDRKQETI
EELEADAKEI KVEKASVKAD IADKRTELAE IEAEIDGIDT QYDELKADLA EHKDRLEEIK
AEKNDVQREK DRLLDEARRR SNEISEAQSD LEAAHERIPD LKARISELHG ELDTAETNRD
AIEETIADLF AEKAERQERL DAIEDDLREK QSEYASLEAD AKRRGDASWP RAVTTVRNAG
IEGVHGPVGE LASVDPTYAE ACETAAGGRL ANVVVDDDGV GETCIEHLKS RNAGRATFLP
ITELDDRGLP NAPTMPGVVD FARNLVEYDA RYDPVFSYVL GSTLVVEDMG TARDLMGEYR
MVTLEGDLVE TSGAMTGGSG GGSRFAFSTA GGGKLQRLAE EIEELEDERQ SLESEVDELD
AEIDDARERK ADAEERVRSV ESDIDRAETE LEEQHDRIEE LESTLETLRD EREEVDERMT
ELDAEIDELA DDQAAVEDRI EELEAELADS RIPELTSRAD EVREEIDDLE SRMDDLDGRL
NEVQLETEYA EDAVEDLHDR IEAAQNKKAE AEEAIADHED EIADKRELLA EKREAIEDLE
EELAELKAER SDLRETLSAA TEERDEQRRR VSEVESTLSD LRDRADRLEW EIDELESQVG
EYDPEAIPDH EEVERRIEEL EAEMEALEPV NMRAIDEYDE VESDLDRLQE RRDVLVSERD
GIEERIEEYE SQKKRTFMDA FESINDHFED IFERLSAGTG ELVLENPEDP FEEGLTMKAQ
PADKPVQRLD AMSGGEKSLT ALAFIFAIQR HNPAPFYALD EVDAFLDAVN AERVGEMVHD
LAGEAQFVVV SHRSALLERS ERAIGVTMQE DNVSAVTGMQ FGGDSEEADG DGEVPADD
//
