位置:首页 > 蛋白库 > SMC_SYNY3
SMC_SYNY3
ID   SMC_SYNY3               Reviewed;        1200 AA.
AC   P73340;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=sll1120;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Required for chromosome condensation and partitioning.
CC       {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC       near the middle of the molecule. These domains are separated by coiled-
CC       coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01894}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA17371.1; -; Genomic_DNA.
DR   PIR; S77524; S77524.
DR   AlphaFoldDB; P73340; -.
DR   SMR; P73340; -.
DR   IntAct; P73340; 1.
DR   STRING; 1148.1652449; -.
DR   PaxDb; P73340; -.
DR   PRIDE; P73340; -.
DR   EnsemblBacteria; BAA17371; BAA17371; BAA17371.
DR   KEGG; syn:sll1120; -.
DR   eggNOG; COG1196; Bacteria.
DR   InParanoid; P73340; -.
DR   OMA; HNKIAME; -.
DR   PhylomeDB; P73340; -.
DR   Proteomes; UP000001425; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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   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; SSF52540; 2.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 1.
DR   TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1200
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409282"
FT   DOMAIN          542..656
FT                   /note="SMC hinge"
FT   REGION          90..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          202..528
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          692..1046
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1200 AA;  136136 MW;  E4FE00EBE6BBDF21 CRC64;
     MVYVKRIELS HFKSFGGTTA IPFLPGFTVV SGPNGSGKSN ILDALLFCLG LATSKGMRAE
     RLPDLVNNTF KGNRGSSEAS VSVTFELHDG ENLSEPGANH NGNGNGAKIS KEWTVTRRLK
     VTKGGNYSSN YYINGETATV TELHEQLNEL RIYPEGYNIV LQGDVTRIIT MNSKERREII
     DELAGVAEFD RKIVKTKETL TEVQDREERC QIIATELERT LERLAADRQK AEKYQALRQQ
     VQEKQGWAKV IQYKAVEQQR QKLWGQLERD REQSQQIQQA LDQRSQAIQT QQTELEKLNA
     QVKALGEEEQ LAVAAQLATQ KAQRDQLQQR YNDGDRQITN HQQQVGQIQA EISQSQQQFL
     HIQQEKSFHN TQTLPQLEAA VQTSQQQLEQ LRHQAQAIAS ASEAWVQEQT QLSRTVNQLQ
     DELIPQRSQL AQLEERQQQL LTNLAELTPL LTKVSVELEE KQFAQGQFNF QGEALTSQIQ
     TLASDLAQLE QERSLLQETQ TRLLKEQQEK QRQLDKLEAA SQAQQEVQGT YATKVILQSD
     LPGVCGLVAQ LGQVEPQYQL ALEIAAGGRL GFLVVEDDGV AAAGIEILKQ AKAGRATFLP
     LNKIRPPKGQ NPNLSYAHGY IDLAVNLIDG DRRYADIFAF IFGNTIVFDT LVNARNHLGK
     HRIVTLEGDL LEASGAMSGG SRNQRSGLRF GTMVSEDTAE VKQLRQRLQD IQQVQGRNEE
     LLLERTVRSR QLTQQLMEMR QQQREAQLHG EQTERDIARL SQQQTQINQQ QINQQQKLAE
     LQQNLALLQQ SLPPLEQQLA SAQQQLTALE TSQTHQQWQT IQIQIRTVEA EYQRQLQALR
     QGEDHLKDLQ NSSQRLEEKI AQAQEKIAQH QAQDLTLAQE QEQLKIALAE MNGAIQTTEA
     QLAKLSEKLG STKQERDRLE TQLNQLRSQQ QEQQWQWEKL QTNQQEYQEN LTQLQTQLEA
     LEQDLPDPWP EIPLLQDRDE ANLDFANILE ELERSIRNGQ KRLEAMEPVN MLALQEYEKT
     EARLGELSEK LQTIAGERTE LLLRIENFTT LRRRSFQDAF DAVNKNFQII FAELSDGDGY
     LQLDDAEDPF NGGLNLVAHP KGKPVRRLSS MSGGEKSLTA LSFIFALQRY RPSPFYGFDE
     VDMFLDGANV EKLSKMVRKQ AQQAQFIVVS LRRPMIEAAE RTIGVTQARG AHTQVLGIKL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024