ID A0A202E8U0_9EURY Unreviewed; 1190 AA.
AC A0A202E8U0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-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=B2G88_09635 {ECO:0000313|EMBL:OVE84644.1};
OS Natronolimnobius baerhuensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnobius.
OX NCBI_TaxID=253108 {ECO:0000313|EMBL:OVE84644.1, ECO:0000313|Proteomes:UP000196084};
RN [1] {ECO:0000313|EMBL:OVE84644.1, ECO:0000313|Proteomes:UP000196084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3597 {ECO:0000313|EMBL:OVE84644.1,
RC ECO:0000313|Proteomes:UP000196084};
RA Zhao B.;
RT "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely
RT halophilic alkalithermophilic archaeon isolated from the athalassohaline
RT Wadi An Natrun, Egypt.";
RL Submitted (FEB-2017) 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}.
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:OVE84644.1}.
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DR EMBL; MWPH01000002; OVE84644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A202E8U0; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000196084; 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; 1.20.5.170; -; 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; 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:UP000196084}.
FT DOMAIN 542..656
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 409..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1032
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; 134496 MW; 722B242B96EA995E CRC64;
MYIKAVVLDN FKSFGRKTKI PFYEDFTVVT GPNGSGKSNI IDSILFALGL ARTRGIRAEK
LTDLIYNPGH EDDSDSGGPR EAIVEVILDN SDGTLDRSQV INAAGSEDVG DVDEIRIRRR
VKQTEDNYYS YYYLNDRSVN LSDIQDLLAQ AGVTPEGYNV VMQGDVTEII NMTPYARREI
IDEIAGVAEF DAKKEDAFGE LEIVEERIDE ATLRIEEKRD RLGQLEDERQ TALRYRRLRD
EKEEYEGYKK ASELEEKREE LAAAEDAVSD LETDLEDLQR ELDERQGTLV RLQEDLEDLN
AEIERKGEDE QLRIKSEIEE IKGDISRLED KIEASEDAID EAESKRREAF VQIDRKQETI
DELADEMREH KLEKASIKSE IQEREAEKAD LEAEIDAVDT EFDELKADLS DRKDDLEEAK
TAKNDLQREQ DRLLDEARRR SNEISEKEST IEQRREEIPD LENHKSDLER ELEKAQKNQA
SIADVVDDLK SEKRRLQSDV DELDDEIQAK QQEYAELEAN AGESGDSSFG RAVTTILNSG
IDGVHGAVAQ LGTVPGEYAV ACETAAGGRL ANVVVSDDVI GQQCIDHLKS RNAGRATFLP
MTDMHKRRLP NAPTDPGVVD FAYNLVDFDS QYDEVFSYVL GDTLVVEDIE TARSYMGDYR
MVTLDGDLVE KSGAMTGGSG GGSRYSFTGG GEGQLERVAK QITELQDERA SLRDDLRDVE
GRLDDARDRK TDAADEVRSI ESEIESLETK RDSIEDEIET LEDELEELED DRESVDDRMN
TISSEINEKT AVIEEIEADI DDLESELADS KIPELTAQIE DLQHEIDERD NKIDDLDGTL
NELELEKEYA EDAVDSLHDD IEDAQNKTAE HEDRIEECEA AIEDKEADLE DKREAVAELE
DELTELKADR SELREELEDA RTKRDQQQER VNAVESKLET KRERAQDLEW EIEGLESEVG
DYDPEDVPDH ETVLEMIDLL TADMEAMEPV NMLAIDEYDE VREDLEELEE GKATLVEEAE
GIRDRIEQYE TQKKQTFMDA YEEISSHFTE IFEKLSEGTG TLHLENEDDP FDGGLTMKAQ
PGDKPIQRLD AMSGGEKSLT ALAFIFGIQR HNPAPFYALD EVDAFLDAVN AERIGEMVEE
LAGQAQFVVV SHRSAMLDRS QRAIGVTMQQ DNVSAVTGID LSSEEVPADD
//
