ID A0A0D9QPK1_PLAFR Unreviewed; 1469 AA.
AC A0A0D9QPK1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=AK88_01548 {ECO:0000313|EMBL:KJP88858.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP88858.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP88858.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) 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; KQ001657; KJP88858.1; -; Genomic_DNA.
DR RefSeq; XP_012334606.1; XM_012479183.1.
DR EnsemblProtists; KJP88858; KJP88858; AK88_01548.
DR GeneID; 24266862; -.
DR VEuPathDB; PlasmoDB:AK88_01548; -.
DR OMA; CPALDNM; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000054561; 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; 1.20.1060.20; -; 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}.
FT DOMAIN 606..728
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 753..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..290
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 319..353
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 433..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 538..569
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 966..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 769..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 168251 MW; A09EC0A00CF4CD6A CRC64;
MRDVVSVVEA KELLAEDDAA NEQTLSIMNE GEAERSAEYH LSSAAEKDVT GGLRRHTLST
EKRKGSRIII DRLILENFKS YSGVKVIGPF YKKFSCIVGP NGSGKSNIID AMLFVFGRRA
KKIRQNKLCD LIHSSKYSMH NEYTKVSIQF RTIAEEGGGE KWQETAHPST ALPDSFTISR
EATADNQSRY RINDKVVTQK EVFDLLLHHG IDLRNNRFLI LQGEVEQISQ MSPKGTKNEE
GLLEYLEEII GTNCYIEGIN KSLEELERCE EVYQEKVNRL KHVYNELKEL AGPKKEAKYY
VQLQKFTYKL HILIVKKDKH ELAKKILIKE EELAKYMKEK KQHNIVYAEL LKERKEMNTV
LGVLEHEESE IVKSKNKVDN EFKLLTTQHE NVKKEIVIVV QKIQNLYVKR EQLREKDIPL
YKSIIEDKQN ILNGLKREAI PKLERQLEKC EEEMERYNEE IKMDTDKINT IYSNEEKKLA
PLQKTYDDMV KVTSEYNNRC NLIEKKQKEF LAHEEKLKYV QGKVLNEMKE LDVQLKHMNK
VELEKKKILH EKERLLTEVD NETEQVTNKL VNLTVMYETM KKDFSTDKSM NKLHELIYHL
KKTKIKGIHG MLGDLGSIDP KYEKAFLIAG NNCTDFVVVD KPHDAVLLFE QMRKHNSGRV
NVLSLSILEN NLLPVMKKQE ENYTPLLPNV HRLIDFIRFK EDKYKICFYY AVKDTLVANT
LEEAHVIGYS HKRRVVTVGG ELIENDGRIC GGGVMNKQGK ESSGESGRRS SARKSCGSGG
TTEGSEETEA TNTFFRAEAA PSQYDQKDVD KTERDIKEAN KHMDQLKMRK ANLLNEIKEV
KTLIEDNECK VEIAKKRIEN CKKQLKDIEG QLQNSNVPEL TPEEKRELES IKEMIEEKNN
EKNKIEILLK AQESKVKMYY EQLQNVGGEK KKTLKSKFLH AERQLNITRD EIAKHSSEEV
NALANLQKGE KDILKFTDEI EEYEKNEKEL ENELKDLEAK GSIVYEQIEQ MEKELNKVQA
QMEQNQKKKQ QIDENVSKKD LENVDLVYKT EHLQKEIEQL RLRGVAYEGK IEEYTRLIEQ
ADRVVVENRR CRASSGEEDS QHGSGGGSDG GSGGGSDGGS GGGSDGGSGG GSDGGSDGGS
DGGSDGGSDG GSDDGSEDGS GDGRDHERDD GSRDARERDQ DQDEELKALE DLACDHEDWT
DLETEYNYAD VTETQLQDMN RKEMEHKLNS KLLLLQKKAP NLKVFKDYNV KLYDYMKRKK
DVHKSRKKKD KLKKHYDNLC NKRRKEFLLA FNIISAKLKE MYQMIAVGGD AELEIIDSSE
IFNEGILFSV RPPKKSWKHI QNLSGGEKTL SSLALVFALH YFKPNPIYFM DEIDAALDFK
NVSIISHYIK TKTSDAQFIV ISLRNQMFEL CDRMIGIYKT NDITKCITLN PGRFQGDQHG
GQQGAAGGEQ QDAEEKIHEQ ANPYVAVTM
//
