ID A0A0F7IF16_9EURY Unreviewed; 1165 AA.
AC A0A0F7IF16;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=GAH_01058 {ECO:0000313|EMBL:AKG91622.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91622.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG91622.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG91622.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) 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; CP011267; AKG91622.1; -; Genomic_DNA.
DR RefSeq; WP_048095125.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7IF16; -.
DR STRING; 113653.GAH_01058; -.
DR GeneID; 24803632; -.
DR KEGG; gah:GAH_01058; -.
DR PATRIC; fig|113653.22.peg.1053; -.
DR HOGENOM; CLU_001042_2_2_2; -.
DR InParanoid; A0A0F7IF16; -.
DR OrthoDB; 9143at2157; -.
DR Proteomes; UP000034723; 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; -; 1.
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; 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:UP000034723}.
FT DOMAIN 521..640
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 163..503
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 701..791
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 818..922
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 1165 AA; 134907 MW; B7FDAAB68FCAC16B CRC64;
MHIKKITIKN FKSFGKKVEI PLERGFTVIS GPNGSGKSNI IDSIIFCLGL HSSSKVLRAE
KLTDLIYSGN GRRLGTAEVE IVFEPDNGEE LRISRKVRVT EKNYYSNYYI NGKPASHGEV
VRVLEKAGIY SDAYNIVMQG DVTRIVEMTP MQRRKIIDDI AGISEFEEKK ARAIEELEAV
RQNIEKISAI LSEVELRLKE LERDREEALR YRELLEKKER LENELKAIRR KELSLKLERL
RKEVERLQRQ KDSAMVRISE IKVEKESIRK ELEDVSRRIA ETADERYREI QERIADIQAE
IEGLRKEEEI LKAEIERLNE ERMKALLDIT KINERLESLR KELENLLLQK VSVEESVDSI
KAQIEGVREQ IEKLSGEEKE LRDEIVSLSE KAEELREGKS ELLRERDRIY EGLRRVSIEI
EELEGELNRI RNEYSGVKDE IELRRREIER IESQLAREIT NKNAIDRKIF DLRNEISAID
EEIKGKELEL AKVKAELSAY EATFGRAVEL ILEAKEKKAL PGIFGIVAQL AEVEERYALA
LEIAAGNALN FIVVENEDDA IRAINYLKQI RGGRATFLPL NKIRKNFEKI NLDRKVLSEK
GVIDYAVNLV KCEPKFRPVF NFVFRDTLVV DNVENAKRIM DGRRIVTLDG ELIEKSGAIT
GGSVDRKKGL LISKELLERE KKISEEITVL NSKKAFLVGE LRKVEDSWRE AQSRVKELEE
SLRNAENDVK VLQARLEGIA AREKEILERI EDRERERREL GQKIGDVEQA VKEVDSELSK
IEGRLEELNR KMKGSALPKL TEELERLKSQ FSVAREGLIK IESEIEKKEL EIGQAERELE
DKERRVGEID GKVSEYGEKI EHGRKKAMEL REEMERLREE EETLGEAIKE LRRERDALFS
KLKDLENEES RLEYDLVGFD EKIRARKEAM GEIEAEIQGL PEMEPSMSRD EAVSELERVE
SELSKFGEVN MKAIQDYEEV KARWEELYSR KVTLEKEREE ILERIERYDR MKKEKFFEVF
NAINENFKEV IAKLANGEGE LYLDNHDDPF NSGLHMKVKP YGKPVQRLEQ MSGGEKSLVA
LAFIFAIQRY KPAPFYAFDE VDMFLDGVNV ARLARMIKEM SSRAQFIVVS LRKPMLEQAD
AIVGVTMGRD NSSQVTGIRR ASMIQ
//