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Database: UniProt
Entry: A4H486_LEIBR
LinkDB: A4H486_LEIBR
Original site: A4H486_LEIBR 
ID   A4H486_LEIBR            Unreviewed;      1208 AA.
AC   A4H486;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   22-FEB-2023, entry version 88.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=LBRM_05_0410 {ECO:0000313|EMBL:CAM36875.1};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM36875.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM36875.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM36875.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM36875.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM36875.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
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DR   EMBL; FR798979; CAM36875.1; -; Genomic_DNA.
DR   RefSeq; XP_001561855.1; XM_001561805.1.
DR   AlphaFoldDB; A4H486; -.
DR   STRING; 5660.A4H486; -.
DR   GeneID; 5412743; -.
DR   KEGG; lbz:LBRM_05_0410; -.
DR   VEuPathDB; TriTrypDB:LbrM.05.0410; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_050009100; -.
DR   InParanoid; A4H486; -.
DR   OMA; HNKIAME; -.
DR   Proteomes; UP000007258; Chromosome 5.
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: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; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 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   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT   DOMAIN          518..649
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1175..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          180..232
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          297..345
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          463..501
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          697..940
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1181..1195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1208 AA;  136497 MW;  9764E0EA365BA5C8 CRC64;
     MRVKSIVIDG FKSYAHRKEL ADLSPHFNAI TGLNGSGKSN IFDAICFVMG ITNLKRVRAE
     DPRELIFRAG TTGVHAARVT IEFVNDDPAS APPGYSCEEY PLITIGRQIK LGGRQQFFFN
     NTVSLQSKVK RFFESISLNV DNPHFMILQG TVHKLIGMRS QDILSLIEEA VGTKAFDHRR
     RTAETLIRNK ERKMEEIDTN IEAQIRPLLD TMRADQEEYN AFMQNREKTE EKKRFRIALD
     YHTHHTEHTE VEARVEARKV DVQNAKSQLQ ALPRQEEEAT RRLVQLQGSL HAPSEAAISL
     HEEEDELKKA HSRLESELDN CTRLLRQLET QLKTLRREQE KQSNNQVTFA ARRQQHEQML
     AQIKEGKEAC AKLKRGLKLL QSGVQAGTSG VSLAEERQQV DLKLIEQQSR VHRATERFEE
     LVKQQQRIEA HQAEESSRVR HLEHEHAKAA ASLEKTKVVY APLALKQERK EALEAEISSL
     KREYQAEYEN FQRQVSTAAA RNYDLDYNRY ACPPDTEDNV LGRVGQLITP IDLQHALGLM
     VGAQNQLLRV VVTDDRVAEA IIHSGLRQRT AFFALDKLQR PPTHLFIDDA KLQAARLIAE
     QQGGWVHRAR DLVTVQEASS HQQQLNALAD FVFGTFFVCS SLRLAQDLAY NPSIKVKAVT
     IEGEVAEPNG LMTGGSTHHL RDVFADLKAY AAQKEPLQAL QQRTRTLETE YAALRNTLRQ
     HQHDIQAYKA AEAAAELSKQ RYIVAASSAQ SGAAELAEEM EREHATMTEA QEKVAVLQAR
     QCELAAQAQT TDLNVVRTEI ENQLAAAEAH VARLMADEER GAAEFERLEA DMEQQTADLS
     RKAQDMEEEL AQQQSQKLKL TAQVEELKQQ LVAVQARCKH NEERRQQLEK EIDDTQEELT
     RLAERKVTLD NLAKNGEVEL REQSRCLESL RRHIHEAEQR HSWLLEVRET FNQPGGPYDF
     SDAARTAATL QELREIEARA AAMSNKLSQK SAILYEERRR EYEELVKQRT ALGEDKEAIQ
     RCITEIESKK WGALDRMVGI VSSIFGRLFA ACLPGATAQL LEERDATNHL TGLGVRVSFN
     EKPRESLSEL SGGQRSLLAL CLMLAILRVR PAPLYILDEV DAALDPSHTQ NIGRMLQLYF
     PHSQFLLVSL KDGMFNNANV LYHIRNTQGY SEVARIEHKP PSQPTSASSD TRAASSGADR
     EGAVATSA
//
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