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Database: UniProt
Entry: A0A1E2WEM7_9NOSO
LinkDB: A0A1E2WEM7_9NOSO
Original site: A0A1E2WEM7_9NOSO 
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
//
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