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Database: UniProt
Entry: K8GN89_9CYAN
LinkDB: K8GN89_9CYAN
Original site: K8GN89_9CYAN 
ID   K8GN89_9CYAN            Unreviewed;      1235 AA.
AC   K8GN89;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=OsccyDRAFT_0300 {ECO:0000313|EMBL:EKQ70040.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ70040.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ70040.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ70040.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-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       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:EKQ70040.1}.
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DR   EMBL; AJUB01000005; EKQ70040.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GN89; -.
DR   STRING; 864702.OsccyDRAFT_0300; -.
DR   PATRIC; fig|864702.5.peg.322; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_3; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000001332; 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   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.
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:UP000001332}.
FT   DOMAIN          580..697
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          119..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          224..432
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          468..565
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          740..919
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          1017..1079
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        119..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1235 AA;  141050 MW;  51EA00F02CA93215 CRC64;
     MYVKRLELTN FKSFGGKTVI PLLPGFTVIS GPNGSGKSNL IDAILFCLGL AGSKGMRAER
     LPDLVNHTQS TRNRSTIEAS VTVTFDLTDE PISIDDEIEQ AVSGNRADSN LETMMSENGK
     AKSANGSNGN GHIEHRLNSK NNDSHNGLRE WSVTRKLRVT QQGTYTSNYY MNGEPCTLTE
     LHEALGRLRI YPEGYNVVLQ GDVTRIISMN PRERREIIDE LAGVAAFDRK ISQAKDKLDA
     VKDREDKYHI VEQELIAQRD RLAQDRIKAE KYKKLRQELQ TKEQWEAVIQ RRQVVRQIEQ
     LQQQITADDK AIADFTEQIA TLATEIQRST VELEQLNARV KALGEEELLA LQATLATQEA
     ELRQLQRQES DLQAARKELE ANLTRTQQEL LENQQQLNTL NQEQQRLESQ ELSSLQTARD
     QALQQLEQSR EAATASAASA EAWVQEQTSL RHRIDTLLET LEPQRSEQAR LRERTLQLER
     QIQEQTQTLR SLEQQLAKKQ EQQATTTIQQ TESQQQIQVL AAKLAAAEQE LQIQQETRTR
     LLNEQRENQR RLDKLEAQTQ AMQEAQGTHA TQLILQMNLP GVCGLVAQLG WVEPRYQLAL
     ETAAGARLGN LVVEDDGVAA AAIELLKQRK AGRATFLPLN KLQPGRFPSR GMLRSLPGCI
     GFAVDLIKFD SQYRDVFAYV FGTTLVFETL SEARRYLGEH RMVTIDGELL EASGAITGGS
     INTRQALHFG TMDSGESDEV KALRDRLQEI ERILTHCENA IFRATNLVKE RTQELTELRQ
     QHREHQLKAE QFTNELKSLS TQQASLSTQL DQYTQELQTC QTHLQRLDTE IPAHEEELHQ
     YRQALSELEQ SHTHSEWQQI QATLRSQEAD LSQKELALRT AEQRIRDLDN QQQRLQEKVQ
     QQQQRLQELR TQQATQLNQE SAVGSQQSEL EQQITDTRSA QVMLEQRLGT EKTQRDRVER
     QLRDQQIQQQ QREWDRQKVQ ETQQSRRENL IALQEQLQAQ QLDLPELLPE VPENIGLEQL
     QQELRSLQKR LQAMEPVNML ALEEYDRTQA RLNELTEKLR TLEEERTELL LRIENFTTLR
     QRAFMEAFDA VNENFQSIFA TLSDGDGRLQ LDDPQAPFNG GLNLIAHPKG KPVQRLASMS
     GGEKSLTALS FIFALQRYRP SPFYAFDEVD MFLDGANVER LARMIKQQAE QAQFIVVSLR
     RPMIESAQRQ IGVTQARGAF TQVLGIDLTP QRASL
//
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