ID A0A0C2LRC7_9CYAN Unreviewed; 1223 AA.
AC A0A0C2LRC7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SD81_11375 {ECO:0000313|EMBL:KIJ77321.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ77321.1};
RN [1] {ECO:0000313|EMBL:KIJ77321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ77321.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-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 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:KIJ77321.1}.
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DR EMBL; JXCB01000007; KIJ77321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2LRC7; -.
DR OrthoDB; 9808768at2; -.
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; 1.10.287.1490; -; 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 PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
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 568..685
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 108..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 308..420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 452..479
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 505..553
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 749..1067
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1223 AA; 138474 MW; CDB5D6D02968BCAD CRC64;
MVYVKRVELT NFKSFGGTTS VPLLSGFTVI SGPNGSGKSN ILDSLLFCLG LASSKGMRAD
RLPDLVNTTQ TSKSRSAVEA SVTVTFDLSD HQLEDELETL PVVSVVEDEE VGEVEEAPKE
ESEDEKNRQE KIRAKPGSEW SVTRRLRVTP QGTYTSNYYI NGISCTLTEL HEELENLRIY
PEGYNVVLQG DVTSIISMNA RERREIIDEL AGVAGFDRKI NQAKETLDEV KDKEDSCRIV
ETELIAQRDR LSQDRAKAEK YQRLRTEFQE KQSWEAVLSW RSLQAQQEKL VASIQAGSST
SAELTNQLTT LNTEIAQKTV ELEQLNAHVK ALGEEELLAV QSTLATQEAE RKQLQRQQKE
LETASQETVK RLQQTQTEIQ QHQQTIEQLA QQQIVELSNA TSLQTERDQA QQALDISREA
AAQIASASEA WVQQQTALNR QIEAVLQTVE PQRTEQAQLR ERNNQLQQLI QEQTELIQTL
EPEIADKQSQ IINVELSGAT SLQQVEQLAE TVSGTEQELQ IQQETQKRLL QEQREKQRQL
DKLEAQQAAQ QEVQGTQASK VILQSGMPGI CGLVVQLGRV EPRHQLALEI AAGARLGHIV
VEDDSIAAAG IELLKQKRGG RATFLPLNKI HAPKFTQDFT LRYANGFVNY AVNLIECDRR
YKDVFTYVFG NTVVFETINQ ARQHLGLYRI VTLDGELLET SGAMTGGSTN QRSSLRFAGV
EAAESEEVSS LKTRLADIEK ILERCGEAIS TLSTRTKRLT QELTEARQAR REQQLQLEQL
QKEIKSLTAQ LETTRSQLSQ NSERLATVRS RLEVLDRELP SQEQQLQQLR QALAELEQSQ
TPQEWQHIQA TIKIQEQQLQ QRDAALREGE QKLKNLENQQ QRLQEKIAVG EQRIQEYHQD
QINQQTQLTA LGTQYSALNS QIAETRAALS QMEQNLGEEK QQRDATEQEL RSHTMRQQHL
EWELQKLQET QQTKAEELTA LQTQMQTMAA ELPNPLPEVP DKVNLEELQK ELRSLAKRLQ
AMEPVNMLAL EQYERTQKRL EELTQKLQTL EAERTELLLR IENFTTLRQR AFKEAFDAVN
ENFQSIFATL SEGDGYLQLD NPEDPFNSGL NLVAHPKGKP VQRLASMSGG EKSLTALSFI
FALQRYRPSP FYAFDEVDMF LDGANVERLA KMIKQQAQQA QFIVVSLRRP MIESAERTIG
VTQARGAYTQ VLGIKLQSNH NSA
//
