ID   Q802S1_TAKRU            Unreviewed;      1200 AA.
AC   Q802S1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   22-FEB-2023, entry version 115.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=smc2 {ECO:0000313|EMBL:CAD58848.2};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|EMBL:CAD58848.2};
RN   [1] {ECO:0000313|EMBL:CAD58848.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14660695; DOI=10.1093/molbev/msh023;
RA   Cobbe N., Heck M.M.;
RT   "The evolution of SMC proteins: phylogenetic analysis and structural
RT   implications.";
RL   Mol. Biol. Evol. 21:332-347(2004).
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
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DR   EMBL; AJ534333; CAD58848.2; -; mRNA.
DR   RefSeq; NP_001027796.1; NM_001032624.1.
DR   AlphaFoldDB; Q802S1; -.
DR   GeneID; 445959; -.
DR   KEGG; tru:445959; -.
DR   CTD; 10592; -.
DR   OrthoDB; 231904at2759; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   CDD; cd03273; ABC_SMC2_euk; 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   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR027120; Smc2_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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   2: Evidence at transcript level;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
FT   DOMAIN          520..640
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          946..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          260..344
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          409..502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          678..930
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        946..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1200 AA;  135736 MW;  524394FD948321EF CRC64;
     MHIKSIILEG FKSYAQRTEI NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSHVRAS
     NLQDLVYKNG QGGITKATVS ITFDNSNKGE SPLGFETHDE ITVTRQVVIG GRNKYLINGV
     NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILAMIEEAAG TRMYECKKIS
     AQKTIEKKEA KLKEIQTILD EEITPTMQKL QEERSSYLEY QKLMREIQHL TRLHVAWLFV
     CAEETKLKSA DNLKVMQDNI KKMQVSLVEN ESKVQELSAQ IQELQKKKDQ EVNGVLKSLE
     EALADVQRAD AKVQSGLDMK KQNIQDETKK RKELVKNMEE DKKMLIVKER EVSKVMEQLL
     AMQEEGQKEN AALEVAEKHF RAVSAGLSTN EDGEEATLAG QMMTCKNDIS KADTEAKQAQ
     MALKHAQAEL KTKQTEMKKM DSGYKKDQDA LRAVRSSREK LQAELDTLGY EDGKEERLLD
     KRRQLSREVT ELGEKYERLV SRFPNLRFDY KDPERGWDRS KVKGLLANLI TIQEVSYATA
     LEVVAGGRLY NIVVDTEVTG KKLLERGELQ RRYTIIPLNK ISARTLDDRV VNTAKSLVGR
     ANVHTALSLV GYEADLRKAM QYVFGSTLVC DTLDNAKKVA FDKHVMTKTV TLGGDIFDPQ
     GTLSGGARSQ AASVLSSLQE LKDVRDELNS KESQLQDVEG QLTGLRATAD KYRQLKQQCE
     LKVEEEQILQ AKLQQSSFHQ QQEELERLRA TIADSEETLR ITEEVHKRAE EKYQVLEKKM
     KNAEAEREQE LKAAQQKLTA AKTKADAFNK GLKQKQQESD AVALELEELR REQAGYEQQI
     QAVDEAMKAI QEQIDSMACT VSQNKEAVRK AQEELTKQKE VIMAQDKELK VKSSEANHLR
     EQNNEVQLKI KELEHNINKH RKDTQDAADK VSRMLEEHDW IHSARQSCGQ PNTSYDFKTN
     NPKEAGQRLK RLEETKDKLE RNVNRRAMNM LSEAEERYND LMKKKRIVES DKTKILQTIE
     ELDQKKNEAL NVAWQKVNKD FGSIFSTLLP GATAKLAPPQ GCGVLEGLEF KVALGTTWKE
     NLSELSGGQR SLVALSLILA MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRAHFRHSQF
     VVVSLKDGMF ANANVLFKTK FVDGMSTVTR TALSQSDASV PQKAPEKSRH RDRKNRQLLG
//