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Database: UniProt
Entry: R7L2A3_9BACT
LinkDB: R7L2A3_9BACT
Original site: R7L2A3_9BACT 
ID   R7L2A3_9BACT            Unreviewed;      1231 AA.
AC   R7L2A3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=BN601_00600 {ECO:0000313|EMBL:CDE82784.1};
OS   Coraliomargarita sp. CAG:312.
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC   Coraliomargaritaceae; Coraliomargarita.
OX   NCBI_TaxID=1262865 {ECO:0000313|EMBL:CDE82784.1, ECO:0000313|Proteomes:UP000017918};
RN   [1] {ECO:0000313|EMBL:CDE82784.1, ECO:0000313|Proteomes:UP000017918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:312 {ECO:0000313|Proteomes:UP000017918};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CDE82784.1}.
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DR   EMBL; CBJS010000012; CDE82784.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7L2A3; -.
DR   STRING; 1262865.BN601_00600; -.
DR   Proteomes; UP000017918; 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; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 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:UP000017918}.
FT   DOMAIN          2..1215
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   DOMAIN          527..629
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|Pfam:PF06470"
FT   COILED          165..206
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          246..490
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          682..842
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          875..919
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   1231 AA;  138614 MW;  9F89ABDCF009CCAC CRC64;
     MYLKQVTING FKSFADKTEL PLTPGITCIV GPNGCGKSNI VDAIRWVLGE QSAKALRGGK
     MQDVIFQGTE TRKPLQFCDV SLLFTDCEKQ LKFNEVEITR KVYRDGGSDY FINGKSARLK
     DIQNLFMDTG VGRVSYSFMV QGQIDQILSS NPGERRTIFE EAAGITKYKT QRREALNKLA
     LVEQNLARAT DRIEEISRQI GTLKRQASKA LRYKRLSYRL RHLDLALNSH NYAKQNALLK
     EDETVQKRLS SEILELSEKL AACEEDLSRM RASRAELLAQ LESLRQNASE VRSAKEQAER
     NSEFAEVRKR DLGERLEQIS KELESLKEQL SALEGKAQGD IEVKQMQLNL VSADDEVFRQ
     QSAELAEVEE SLRDAENRLS RAKQDSLMNE SAVTRLRSNC TTLEVDLKSY QVRHAALSDQ
     IFQLKEENSS LERRCEELSA AMENANERLG NAEADITEAV AKADELRAQY RNQQAEIQQM
     DRQLASKSAK LSLLNDLQSR MEGFSEGVKA IMKGRLGECL DPLNLKIVSQ NVEVADGWTS
     AFETMLGSAV DAVAIEDSSK LPQALALLRE RNLGNACFQI KDANLNAISD ADALPQGIWR
     GCDIVKPQDP DLSEYVRNMV AGCYFCEDIM QFANFALNNK NFKFMAAVAK DGSMLDARGI
     IYASSGEKRD TQSSFILRNS EIKRIKEEIE VDNDALTTLN ERAMQIQSQL ESAEAEIENR
     KNLSSEIKRE IASINAQSSS AKAAFSEKNS EIEKKTAAMA EMENSRFEAQ DRLNSAMKAL
     EDAEKSISES RNLISETEAQ IAELRETKDQ KYAVLSETRL ELAAKKSRLE SLERGLGAIR
     EQQAETRALI ERRTIESQSI ARQIENFDAE TLSERERAKN LAENLEAALG EIEAQRVKVA
     ESETSIAEYE NSLSAEREAH MRKTSEKNEC QIRIAKIRSK LDFISERILS EYDVEIANVD
     WKSELWKSDE EFEIKVKLDE LEDGEINAKP KRERGDPTQD DLDAMESTDF SPIEDEVREL
     RERINAMGAV NLVAIEEYAE LKERYDFLKT QTDDLWASKN ALVADIDEIN ATSQKLFSET
     FEQIRKNFAF TFQKIFGGGT ADLRLVESED VLDSGIEIVA RPAGTVLKSL SLLSGGQRTM
     TAVSLLFAIY MVKPSPFCVL DELDAPLDDA NIGRYTDMLK EFTRYSQFLV ISHNKRTMSA
     AQTLYGVTMQ ERGVTRLISM RFNGESTSSG E
//
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