ID   A0A0S4JMS1_BODSA        Unreviewed;      1340 AA.
AC   A0A0S4JMS1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=BSAL_32135 {ECO:0000313|EMBL:CUG91447.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG91447.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   EMBL; CYKH01001926; CUG91447.1; -; Genomic_DNA.
DR   VEuPathDB; TriTrypDB:BSAL_32135; -.
DR   OMA; CPALDNM; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0051276; P:chromosome organization; 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   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   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT   DOMAIN          553..670
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          994..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          729..836
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1091..1161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        946..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1023..1050
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1340 AA;  152097 MW;  2FFB22DFB49FAE94 CRC64;
     MSNVSRAISS SIGEHHSHSA TQNNPPTRFV IRDIDVENFK SYAGTHRIGP FHKTFTCVIG
     PNGSGKSNVI DAMLFVFGKA AKKIRLEKLS ELIHSSAAFP QLSYAAVTVN FIEVRETKED
     ADDPTQRLEI PGTELSIKRE VHRNNQSQYF INNIRSTQKE VVATLTEKGV DLDHNRFLIL
     QGEVEQISLM KPKAEKEGEE GLLEYLDDLI GTNQYVDSIT QAAAAFDHVQ EERLGILDDL
     RRALADRNAL EAAKLSTLNY VTKDNHLQRT LIVLCQLKTE DMEKQLVGPR KRLEALVQEL
     QAIDAKSKET RDAVGELSKE EDAKKKIVKA ATVELEAIRS RKLALEEDYE KEKASAEEQE
     KQRKKEMDKI KKASEEIKAH QLQAQNAELD VSLKEQRFQE VKDDLAAEEP RYAAAKDALV
     TKEKPIRVEL EKARKSLLPY TRKLQEAEEV RSTAVERLRR EEDKIHRAEK DLDAARQDVF
     KQQQIARDVT EMLTKAENDT TAQSIQAIQS NLKQCVAQKL QINQSIEDTK RNFKEGSAND
     RIANYLLSQR DIKKYFGTLR QLGRIDPAFD VAAGVASNQW GFHVVEDEET ATLVLERLKS
     SNMGRATLIV LDKVGKRLAD KIDRKFQAPS QSDRLFDMIQ PINEKFRPAF YSAVQDTLVC
     EDLQTARRIG FGAGGGARHR VVTRSGELVE PNGTILAGGQ PRPAELNAAR APQDQQAVKD
     VLMKLQHELQ DAVARENGVR EQLVQLEQQN SSISPDQIRR MKSQLTAANA AVTAAERRIA
     EMERQLAQLR DNAAQQEFRA NLKQRINEAS DAVRTCEEEQ SEFQNTVKEL ERQLANIGGA
     EFLELEKSVL SMRTRLDVDE KALREAKKVL QKSAATKERK EKDLLEAQAR LEALRDENAE
     QLKEQLSRLQ QLVDTAEKER LRQQKVVADA ETAVENVKSQ ITVLEEQLRE HNKERDRTEE
     TRQQEEATIS KELATLGKLT EKLQRAEEHI RDNIRSYGAD TYEPQNGVKG EEYPDLSDDD
     SDENSKNETR ARKRALSTDG SDDDDADAAP RPSHLSTTEG DEPKQTPQLT EAQISAIVFT
     VPVEKLVNYD YQHSSHLARE LSEEIKRLEA TIDFTAVGRW REKDVIYRRI KDSYDTVRTR
     LDNAELQLNT LKDRRKKEFL ECFHIIQRNV KEMYQMLTHG GDAEVELVDT QDPFEGVNFL
     VRPPKKSWKQ VSNLSGGEKT LSSLALVFAL HHVRPTPVYV MDEIDAALDF KNVSIVANYV
     LRQATGAQFI IISLRNNMFE LAHQLVGICK IRDVTRSLTL NPHAMQHMIH ETLIRQQQAR
     RQKRARDEGA ALISDHARVD
//