ID W7A967_9APIC Unreviewed; 1511 AA.
AC W7A967;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=C922_01233 {ECO:0000313|EMBL:EUD68215.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD68215.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD68215.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD68215.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) 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; KI965463; EUD68215.1; -; Genomic_DNA.
DR RefSeq; XP_008815063.1; XM_008816841.1.
DR EnsemblProtists; EUD68215; EUD68215; C922_01233.
DR GeneID; 20036507; -.
DR VEuPathDB; PlasmoDB:C922_01233; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000030640; 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 636..758
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 162..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 377..411
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 463..497
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 834..940
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 991..1060
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1491
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 174156 MW; D954CECA4D82BEAE CRC64;
MRDAISAVEA KELLVEEDAA NTQTLSLMNG GIPDLLAVDR LEVDRSASAA ERDINGALNP
HTLSIENKKN SRIIIDRLIL ENFKSYSGVK VIGPFYKKFS CIVGPNGSGK SNIIDAMLFV
FGRRAKKIRQ NKLCDLIHSS KYSMHNEYTK VSIQFRTISE GGEQCNDPSQ QEGRAKWEGS
EQWDGQEQWD RPAEWQPPPL ESPQHFTISR EATADNQSRY RINDKVVTQK EVFDLLLQKG
IDLRNNRFLI LQGEVEQISQ MSPKGNKNEE GLLEYLEDII GTNSYIEGIN NSLEELERSE
EVYHDKVNRL KHVYNELKEL AGPKKEAKYY VQLQKFTYKL NILIVKKDKF ELAKRISIKE
EELAKYVKEK EQHNVVYATL LKERKEMNII LSSLENEESE IIRRKNKVDN EFKVLTTQDE
NVKKELLIVV EKIQNLYVKR EQLREKDIPL YKSIIESKQK ILNVLKRENI PKLERQLEKC
EEEMEKYNEE IKTDTDRINT IYSNEEKKLA PLQNSYDDLV RVTSEYSNRS NLIEKKQREF
LAHQENLKYL QTKLLNEMKE IDVQLKHMSK VESEKRKALH AKEELVTRID NETEQVTNKL
VNLTVKYETM KKELNTDRSL SKLHELIYHL KKTKIKGIHG VLGDLGSIDP KHEKAFLIAG
NNCTDFVVVD KPHDAVLLFE QMRKHNLGRV NVLSLSILEA NLLPVMKKHD ENYTPLLPNV
HRLIDFIRFK DEKYRVCFYY AVKETLVANT LEEAHVIGYS HKRRVVTVGG ELIENDGRIC
GGGLLNKQGK GAGWGGRTSV RKSCGNAGTE EQGSHCSSSF FRAEAPSQYD QNDVAKTEGD
IKEANKTMED LKLRKGNLLS EIKEITTLIE DNECKLEIAK KRIENCKKQL KDIDGQLQNS
DVPELTPEEK KELEHIKEMI EQKNDERNKV EILLKAQESK VKMYYEQLQN VGGEKKKTLK
NKFMYAERQL NITRDEIAKH SSEEVNALAN LQKGEKDILK FTDEIEEYEK NEKELESELK
DLETKGCMVY EEIEKMEKEV AKVQAQMEEN QKKKQQIDEN ISKKDLENVD LVYKTENLQK
EIEQLRLRGI AYEGKIDEYT RLIEQADRVV VENKPCRASG GASADQSTDE ESSQESGEES
GEEGSKEDLE DGLDDHDDGA VGGKRKRSSE GAAQSRKRKR GSAEESGDGS GDGSGDTRGG
DRESDAEGGD PRQRDEDQEE ELKALEDMAC DNEEWSDLES EYDYANVTDE QLQCMNRKEV
ENKLESKLRL LQKKAPNLKV FQDYNVKLYD YIKRRKDVYK SRKKKDKLKK HYDNLCNKRR
KEFLLAFNII AAKLKEMYQM IAIGGDAELE IIDSSEIFNE GILFSVRPPK KSWKHIQNLS
GGEKTLSSLA LVFALHYFKP NPIYFMDEID AALDFKNVSI ISHYIKTKTS DAQFIVISLR
NQMFELCDRM IGIYKTNDIT KCITLNPRRF QGDQPEEEAQ ELGEEEVSTE EEAEKVNQLE
DQANPYVTVP M
//
