ID E6N382_CALS0 Unreviewed; 548 AA.
AC E6N382;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Structural maintenance of chromosomes protein 5 {ECO:0000256|ARBA:ARBA00018687};
GN ORFNames=HGMM_F22F09C38 {ECO:0000313|EMBL:BAJ46788.1};
OS Caldiarchaeum subterraneum.
OC Archaea; Nitrososphaerota; Candidatus Caldarchaeales;
OC Candidatus Caldarchaeaceae; Candidatus Caldarchaeum.
OX NCBI_TaxID=311458 {ECO:0000313|EMBL:BAJ46788.1, ECO:0000313|Proteomes:UP000008120};
RN [1] {ECO:0000313|EMBL:BAJ46788.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAJ46788.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21169198; DOI=10.1093/nar/gkq1228;
RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H.,
RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.;
RT "Insights into the evolution of Archaea and eukaryotic protein modifier
RT systems revealed by the genome of a novel archaeal group.";
RL Nucleic Acids Res. 39:3204-3223(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010171}.
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DR EMBL; AP011708; BAJ46788.1; -; Genomic_DNA.
DR AlphaFoldDB; E6N382; -.
DR Proteomes; UP000008120; Chromosome.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR PANTHER; PTHR45916:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008120}.
FT DOMAIN 1..522
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 138..239
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 350..377
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 548 AA; 62141 MW; 924123FAE9698F28 CRC64;
MIVGPNGAGK SSILLAISVA LGQTYTERGQ RLADLIRRGY ESARVAVVFD NRPVDGVRPI
PSINSDTVTI TRFLKKTGEY WHYVNNRFKT KAEVGNLLSR IGINPDNVLI IMHQNMIEQF
VSRDSREKLA LIEEAVGAAG LRERIRDTEA KLSALLAEEA VLRKTLDEAR SAVEFWREEY
EKLTILRRLE ERRKLLELEY LWSLVREAEK SRERLEEKIE SIRRETESLE AKITEARNTV
STYYQSLVKG LREGWSERVL METVDGIVAA AESLGRFLER REIREDELRQ LRYEVTALDK
EIIRRRGEAE AKGPRTDTGR KPAEVSEEIK AVGLQIAALG TPNPQAEEMY LIAESKYREA
ELKAQQLSEN AKKTMAEVEY RKQKWAEFVR ELVNSVEPEY QHILSLVGGA GKIELRNLHD
IDKASIEIYV GFRGVEPTLL DTHTQSGGER IVATMAFLLA VQKHIKSPFR AVDEFDVHLD
PLNRERIIHI LTSSAKNDPN TQYIVITPGR VPFTEEMNVI IVQSVKGKSA VLVPAQTEVV
SGDERQGG
//
