ID A0A1I6GCN5_9EURY Unreviewed; 1198 AA.
AC A0A1I6GCN5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN04487947_0927 {ECO:0000313|EMBL:SFR39949.1};
OS Halogeometricum rufum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=553469 {ECO:0000313|EMBL:SFR39949.1, ECO:0000313|Proteomes:UP000198531};
RN [1] {ECO:0000313|EMBL:SFR39949.1, ECO:0000313|Proteomes:UP000198531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7736 {ECO:0000313|EMBL:SFR39949.1,
RC ECO:0000313|Proteomes:UP000198531};
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; FOYT01000001; SFR39949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6GCN5; -.
DR STRING; 553469.SAMN04487947_0927; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000198531; 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; 3.30.70.1620; -; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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; SSF90257; Myosin rod fragments; 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}.
FT DOMAIN 544..658
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 418..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 993..1034
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; 134820 MW; 0946068873C78423 CRC64;
MHIKELVLDG FKSFGRKTRI PFYEDFTVVT GPNGSGKSNI IDGVLFALGL ARTRGIRAEK
LTDLIYNPGH AGDDAGRGGG TKEASVTVVL DNSDGKLDRS QVVNAAGSDD VGDVSEIRVK
RRVKETDDNY YSYYYLNGRS CNLSDIQDLL AQAGITPEGY NVVMQGDVTE IINMTPYQRR
GIVDEIAGVA EFDAKKEDAF GELEAVEERI DEADLRIEEK QSRLDQLEDE RETALKYQSL
REEREEYEGY LKAAELEDKR ADLEQTESKA EAKETKLESL REELDTRQGR VSRLESELEE
LSKEIERKGE DEQLRIKSEI ESVKGEIDRL ENAIEAAEDR IDEAETERRK AFVELDRKQE
KIDDVEDDIR GVKVEKASVK SEIKSKETEL AEVEAEIASV DTEFDELKEE LAERKSRLEE
LKTEKNDLQR EKDRLLDDTR RRSSEISETQ EKIAEVREEL PELKAKLSDL HSELDKAEKN
KAKIDGVIED LREDRSALKS DLDEVEEDLR SKQSEYAELE ARAGENGDTS WPRAVTTILN
SGQSGVHGTV GQLGSVPGEY ATACETAAGG RLAHVVVDDD GVGSSCIDYL KSRNAGRATF
LPITKMDDRG LPSKPNRPGV VDFARNIVEY DAEYEPIFSY VLGSTLVVED METARSLMGD
YRMVTLDGDL VERSGAMTGG SGGGSRYSFS KSGSGRLERL AVEISDLEDD RRDLEQEIRE
VESTLDDARE KASDAADRVR SVEADIERAE ESVEEREDEI TRLEDRIEEL RQKRAEVDEE
MQSLDEDIDA VDADIADVQS DIDELEAELA DSEIPELTAR ADEIRADIEE REDRMDELDG
RLNELQLEQE YAEDAIEDLN ETVESAQERK ADARDRIGEA EAAIEEKEAV LEEKREAVSD
LEAELKELKA ERSDLREDVR EAKSERDEQR DAVDRVESRV ESLRESAERL AWEIDELESQ
VGDYDPEEIP DHDEVQENIE RLTGKMESLE PVNMLAIDEY DEVQESLDDM QERRDVLAEE
RQGIQERIEQ FEAQKKATFM EAFDAINENF TDIFERLSDG TGELHLENPE DPFEEGLTMK
AQPGDKPIQR LDAMSGGEKS LTALAFIFAI QRHNPAPFYA LDEVDAFLDA ANAERVGEMV
DDLAGRAQFV VVSHRSALLE RSERVIGVTM QGDNVSAVTG IQLSDDEDEE ATEATADD
//