ID A0A1E2WEM7_9NOSO Unreviewed; 1222 AA.
AC A0A1E2WEM7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=A4S05_16700 {ECO:0000313|EMBL:ODG96878.1};
OS Nostoc sp. KVJ20.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=457944 {ECO:0000313|EMBL:ODG96878.1, ECO:0000313|Proteomes:UP000094607};
RN [1] {ECO:0000313|EMBL:ODG96878.1, ECO:0000313|Proteomes:UP000094607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KVJ20 {ECO:0000313|EMBL:ODG96878.1,
RC ECO:0000313|Proteomes:UP000094607};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODG96878.1}.
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DR EMBL; LSSA01000400; ODG96878.1; -; Genomic_DNA.
DR RefSeq; WP_069070919.1; NZ_KV757622.1.
DR AlphaFoldDB; A0A1E2WEM7; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000094607; 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 CDD; cd03278; ABC_SMC_barmotin; 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 PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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}.
FT DOMAIN 567..684
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 97..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 307..391
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 741..1059
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1222 AA; 138038 MW; 6CE4A74DDA077163 CRC64;
MVHIKRVELT NFKSFGGTTS VPLLPGCTVI SGPNGSGKSN ILDALLFCLG LSSSKGMRAD
RLPDLVNNTQ TSKGRASIEA SVTVTFDLSD EISHKDAKVQ SEKVGEAEEA EEAGEVGEVG
EAGEENPKSK IQNPKSAEWS VTRRLRVTHQ GTYTSNYYIN GVPCTLTELH GELSNLRVYP
EGYNVVLQGD VTSIISMNAR ERREIIDELA GVAAFDRKII QAKSTLDEVK EKEDSCRIIE
TELTAQRDRL SQDRAKAERY QKLRTEFLAK QSWEAVLSWR SLQAQQEKLV HEIQTGDRNS
TELTTQLTNL NSEIVQKTAE LEELNAHVKA LGEEELLAVQ STLATQEAER KQLQRQLTEL
QTATQETAKR LTQTQQEIQK HRHSLEEIAE TQIVETRFIA SSQHQRNEAH QALETSREAA
AEIASASEAW VQQQTAFNRQ IEALLHTLEP QRTEQAQLRE RNNQLQQLIS EQTQLIERDE
PLLAEKQTEC NQVETEFNAS SEPIQNLAQN LSATEQELQI QQETQKRLLF EQREKQRQLD
KIEAQTQAQQ EVQGTQASKV ILQSGMPGLC GLVVQLGKVE PRHQLALEMA AGGRLGHIVV
EDDSVAAAGI ELLKQKRAGR ATFLPLNKIH APKFTQDATL RFASGFVNYA VNLVDCDRRY
KDVFSYVFGN TVVFSSLEAA RKNLGLYRIV TLDGELLETS GAMTGGSNSN RSALRFGTGE
AAESDEAIAL KTRLVDIERV LERCTEAIAT LSARTKKLTQ ELTEARQARR EQQLQLEQLQ
KDIKNLTAQL QGTRSQLAQN SQKLTTAQSR LEILERELPG QENKLQQLRH ALAELEASQT
PSEWQQIQAT IKIQEQQLQQ RETTLREAEQ RLKNLENQQQ RLQEKIQEAE TRITEYETQQ
TSCRDAIHRV LSQITTIDDQ ITQTRANLSV MEQNLGEEKQ KRDTTELEVR SHLLRQQQLQ
WEIEKLKETQ EKRREELIAL QSQLRDVGAE LPNPLPEVPD KVDLEELQKE LRSLTKRLQA
MEPVNMLALE EYERTQNRLQ ELTQKLETLE GERTELLLRI ENFTTLRQLA FKEAFDAVNE
NFQSIFAILS DGDGFLQLEN PEDPFSSGLN LVAHPKGKPV QRLASMSGGE KSLTALSFIF
ALQRYRPSPF YAFDEVDMFL DGANVERLAR MIKQQSQQAQ FIVVSLRRPM IESAERTIGV
TQARGAYTQV LGIKLQSSNT PA
//