ID A0A238YQL0_9BACT Unreviewed; 1167 AA.
AC A0A238YQL0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN06265340_10465 {ECO:0000313|EMBL:SNR72729.1};
OS Desulfurobacterium atlanticum.
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=240169 {ECO:0000313|EMBL:SNR72729.1, ECO:0000313|Proteomes:UP000198405};
RN [1] {ECO:0000313|EMBL:SNR72729.1, ECO:0000313|Proteomes:UP000198405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15668 {ECO:0000313|EMBL:SNR72729.1,
RC ECO:0000313|Proteomes:UP000198405};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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}.
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DR EMBL; FZOB01000004; SNR72729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238YQL0; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000198405; 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; 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; 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 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 2..1155
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 521..621
FT /note="SMC hinge"
FT /evidence="ECO:0000259|Pfam:PF06470"
FT COILED 170..498
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 658..790
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 826..930
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 1167 AA; 133922 MW; C418E30F84E3D17C CRC64;
MHIKSLTLKG FKSFADETEI RFSKGINCIV GPNGCGKSNV VDALKWVTGD TSSRGMRASN
MKDMVFKGAV GRRAARTAEV SITLSRDELL PIKENEVVIT RKIKANGDSE FLINNRKVRL
KDIQELFLSI GLGHKDYVFF EQGQIDRVLK LKPEERRVLI DDAAGVAPFK EKKEETLKKL
AEAETNLENV RKVIDEVSKN LKTLKNQAEK AKKFQSLKEK ELELEKKLYG CEIRNLKLTK
ELKERELEIL REDRNSLEKE ASSIQVSVEE LRDESEKLAK EIKELTAELY ELEKTKKEAS
VKRDFYLKEK ERIKEELKEI DGEELKKIER IKNVEQEIQF LIEEKEKLVE SILGLEKEIE
RLNTQFNSLK KEKEDVETSL SDIKRQISDA VGRYRKIEVE KIREEEKVVS YKRQIEKFPA
EIDSLKRELS YYEEQKKILQ TKLEEILSSI EKTEEERKAI SVVRENREEK VEELKRKIQE
KEKEIVSISS KIESMEKLLQ NIDFGKLENS IVESGKKGKV KGYIGLLSNL IKVDEGWEKI
VEAFLSLFGA GIVLKTFDDI NWVRERIKGN GRVMLLSAEV VPLKGRYIEE ATPLISHVKP
VDVRVKELVS VIFSNVFYTS SDASRLAKMY PDAVFIDKDL NIYSGKGSYI GKFKGKGIFE
IEKEIETLKL RRETLEKELE SLKLSLKPLI DALSEVDDEL FSLQEKANGL KGERIEVEGK
IREAERRIKE ITKNVESLTE KLQLAREFVE GFSKRDNLYS EKLKELVERK KDLEDKLRDK
EKRFSEILTE VDKVRGLISE KKSSISVLKE KLSHVSEKLG IKEKTVSAIK RELSHLNDKR
EKLKRKYEEA ENGIHSAEDI LSGIDEAIED AKVELETLER RRAEIVSLIK EREEGLKQKE
KELKEIQKKI KEIEIELARI NVKEEEIVEK ILAIDSTVEE AVNAAATVES EDEIKKELIA
VKEKISKIGA VNLLAIKEYD KVKDRYEFIV EQEKDLIKSI KDLKEAIEKI DEEIKKRFFA
TFKSVNKVFR NTFKKVFGGG SARLVLTSED PAEAGIEIEA KPPGKKHSNI NLLSGGERTL
VVISLLYALY SIHPAPFLVL DEIDAALDEI NILRFTELLK SISEKTQVIV ITHKKVTMEV
ADVLYGVTME VPGISKVVGV SFALSEI
//
