ID D2RFP2_ARCPA Unreviewed; 1135 AA.
AC D2RFP2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Arcpr_0040 {ECO:0000313|EMBL:ADB57117.1};
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB57117.1, ECO:0000313|Proteomes:UP000001901};
RN [1] {ECO:0000313|EMBL:ADB57117.1, ECO:0000313|Proteomes:UP000001901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC {ECO:0000313|Proteomes:UP000001901};
RX PubMed=21304717;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001857; ADB57117.1; -; Genomic_DNA.
DR RefSeq; WP_012939453.1; NC_013741.1.
DR AlphaFoldDB; D2RFP2; -.
DR STRING; 572546.Arcpr_0040; -.
DR PaxDb; 572546-Arcpr_0040; -.
DR GeneID; 8738685; -.
DR KEGG; apo:Arcpr_0040; -.
DR eggNOG; arCOG00187; Archaea.
DR eggNOG; arCOG00368; Archaea.
DR eggNOG; arCOG00373; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR Proteomes; UP000001901; Chromosome.
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; 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; 2.
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:UP000001901}.
FT DOMAIN 501..617
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 151..192
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 218..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 653..916
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 945..989
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1135 AA; 132298 MW; 8E220144416AFBC1 CRC64;
MFIRKIKLRN FKSFKKAEIE FRDNFTVITG PNGSGKSNII DSILFCFGIS SSKTLRADKL
TDLIKHGQKE AEVTIELDGY IVRRRVKKTD KGYYSYYYIN GKSVSYSDIE RLIEKLGLNT
EYNIVMQGDV TRVAEMTPIQ RRKIIEDIAG ISEFEEKKEK ALEELEEVKR NIEKVEITIK
EVDDRLSQLK VEREEAIKYK NLVEERELLL NYKRIHEYLR LVNTANSLRK RLEELNEERD
QILKAITDIN SRLVNLNEEV KEIVDRIESF KDSRLKRINE EINVVSNEIS GLKKLISLFS
SEVEDLNREK EKTLISLQRA EEEIKRINEE LRDIDVKMES LENILNEKIS YLNALKIKYD
EITSRFRAQR EELESKLNLL NELKEKRTSL LKEREKILEG LRRIGMEIDD MELSREKIDL
SRIFDEIAED ERNLAILKNE MDKLKLKLFE IDGEIFKLRD EIAKIDKEIR EKEIELAKVS
AIQKPRAVEV VLKAKEEGKL EGIYGTVSQL CSVDEKYALA LEIAGGNALN FIVVEDEDKA
IRAVKYLKDV DGGRASFIPL NRINISLNLD KSVLSVEGVI DYAVNLIECD RKFRKVFELV
YKDALVVEDI DTAKKFMNKF RVVTLDGDLI EKSGVITGGS IKKKATLGLF DRERRLREDI
ENLKRSRSEL ESKLSEVELE RKDLEKRIEK LNEDITSLKS KISTSGAKVD EFSKLLKDIE
EKLKEKRREA EILNSKALEV EEEINKIEEN IRCIEREVKE LESKLKDDRI VKLNTKIEEI
RGEIERLKDL KSVLSSKQSS LVAKREQLIK AIEEYKSSLN DLEKKITERL NGIEDAKAKI
LELERRLESL REEERRINKE VGDLREKRDE LLKEIDKLEK EKSQKTLAEK LLEERIKDLK
EKLADVEKTL ESYDIEIPKD LPSLEYVERK LLQVEEELKS FGEINMKAIQ EYEDVKKRLD
ELIEKKKTLE RERKEIIEKI KRIEKMKKEA FLSTFNSINE KFKEIVKELA DGEGEIYLDK
DDPFQSGLHI RFKPFGKPIQ RLEAMSGGEK SLLTLAFIFA IQRYKPAPFY AFDEVDMFLD
GVNVGRLAKM IKKLSKDAQF IVVSLRKPML QEADHVIGVT RGGEEESIVT AIQLR
//
