ID E9AKE6_LEIMU Unreviewed; 1212 AA.
AC E9AKE6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 22-FEB-2023, entry version 53.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=LMXM_05_0400 {ECO:0000313|EMBL:CBZ23397.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ23397.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
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; FR799558; CBZ23397.1; -; Genomic_DNA.
DR RefSeq; XP_003871930.1; XM_003871881.1.
DR AlphaFoldDB; E9AKE6; -.
DR GeneID; 13453050; -.
DR KEGG; lmi:LMXM_05_0400; -.
DR VEuPathDB; TriTrypDB:LmxM.05.0400; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 231904at2759; -.
DR PhylomeDB; E9AKE6; -.
DR Proteomes; UP000007259; 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; 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}.
FT DOMAIN 518..653
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1180..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 311..345
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 404..501
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 757..916
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1212 AA; 136555 MW; EC54D42CCDA7CDFC CRC64;
MRVKSIVIDG FKSYAHRKEL ADLSPHFNAI TGLNGSGKSN IFDAICFVMG ITNLKRVRAE
DPRELIFRAG TTGVHAARVT IEFVNDDPAS APPGYSCEEY PLITIGRQIK LGGRQQFFFN
NTVSLQSKVK RFFESISLNV DNPHFMILQG TVHKLIGMRS QDILSLIEEA VGTKAFDHRR
RTAETLIRNK ERKMEEIDTN IEAQIRPLLE TMRADQEEYN TFLHKRETME EKVRFRVALD
YHTHRTKHTE AEAAMEARKA DVRNAKAQLQ ALPRQEEEAA RRLLQVQDSL SAPSEAAITL
HEEEDELKKA HSRLEGQLAS CTKSLKQLEA QLKSLRKEQE RQSTSQAAFA ARQQQHEQLL
AQIKEGKEAC AKLRKGLKLL QSGVQASTSG VSLAEERQQV DLQLIEQQSR VRRATERVEE
LVKQQRRVEA HQAEESGRVR HLEHEYAKAT ASLEKAKAVY TPLALKQERK EALEAEISSL
KREYQAEYEN FQRQVSTATA RSYDLDYNRY ACPPDTEDKV LGRVGQLITP TDPQHALGLM
VGAQNQLLRV VVTDDRVAEA IIRSGLRQRT AFFALDKLQR QPTHFSIDGA KLQAARLIAE
QQGGWVHRAR DLVTVQEASS HQQQQQQQLN ALADFVFGNF LVCSSLRLAQ ELAYNPSIKA
KAVTVEGEVA EPNGLMTGGS TRQLRDVFAD LKTYTAQKQP LKALQQRTRA LEVEYAALRD
TLRQRQHDIQ VYKAAEEAAE LSRQRYIVAA NSAQSGAAEL TEQMEREQTA LAEAREKIEA
LQARQRELAT QAQTTDLNAV RREMEDQLAA AEAHVARLMA DEERGAAEFE RLEADMEQQA
ADLSRKTQDT EEDMVQQQSQ KLKLAAQVEE VMQQLAAVQT RSKQNEERRQ RLETDIDDAQ
EELTRLAERK VTLDNLVENG EVELREQGRC LESLRRHVHE AEQRHSWLLE ARDTFDQPGG
PYDFSDAART AAILQELRDV EARAAVMSSK LSQKSAILYE ERRREYEELV KQRTALGEDK
EAIQRCITEI ESKKWGALDR MVGVVSSIFG KLFAACLPGA TAQLLEERDA ANHLSGLGVR
VSFNGKPRES LAELSGGQRS LLALCLILAI LRVRPAPLYI LDEVDAALDP SHTQNIGRML
QLYFPHSQFL LVSLKDGMFN NANVLYHIRN TQGYSEVARI EHKPPSQQTA PDSDTPNVAS
GAERKGAVAS PA
//
