ID Q45KZ0_TOXGO Unreviewed; 1186 AA.
AC Q45KZ0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 22-FEB-2023, entry version 79.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC2 {ECO:0000313|EMBL:AAZ57431.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000313|EMBL:AAZ57431.1};
RN [1] {ECO:0000313|EMBL:AAZ57431.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ME49 {ECO:0000313|EMBL:AAZ57431.1};
RX PubMed=16600400; DOI=10.1016/j.molbiopara.2006.02.008;
RA Sauvage V., Millot J.M., Aubert D., Visneux V., Marle-Plistat M.,
RA Pinon J.M., Villena I.;
RT "Identification and expression analysis of ABC protein-encoding genes in
RT Toxoplasma gondii. Toxoplasma gondii ATP-binding cassette superfamily.";
RL Mol. Biochem. Parasitol. 147:177-192(2006).
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; DQ125486; AAZ57431.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45KZ0; -.
DR SMR; Q45KZ0; -.
DR VEuPathDB; ToxoDB:TGARI_297800A; -.
DR VEuPathDB; ToxoDB:TGARI_297800B; -.
DR VEuPathDB; ToxoDB:TGARI_297800C; -.
DR VEuPathDB; ToxoDB:TGARI_297800D; -.
DR VEuPathDB; ToxoDB:TGCAST_297800A; -.
DR VEuPathDB; ToxoDB:TGCAST_297800B; -.
DR VEuPathDB; ToxoDB:TGCOUG_394400; -.
DR VEuPathDB; ToxoDB:TGCOUG_394410; -.
DR VEuPathDB; ToxoDB:TGDOM2_297800A; -.
DR VEuPathDB; ToxoDB:TGDOM2_297800B; -.
DR VEuPathDB; ToxoDB:TGDOM2_297800C; -.
DR VEuPathDB; ToxoDB:TGFOU_288700A; -.
DR VEuPathDB; ToxoDB:TGFOU_297800A; -.
DR VEuPathDB; ToxoDB:TGFOU_297800B; -.
DR VEuPathDB; ToxoDB:TGGT1_297800; -.
DR VEuPathDB; ToxoDB:TGMAS_297800; -.
DR VEuPathDB; ToxoDB:TGMAS_416870; -.
DR VEuPathDB; ToxoDB:TGME49_297800; -.
DR VEuPathDB; ToxoDB:TGP89_297800A; -.
DR VEuPathDB; ToxoDB:TGP89_297800B; -.
DR VEuPathDB; ToxoDB:TGP89_297800C; -.
DR VEuPathDB; ToxoDB:TGPRC2_362560; -.
DR VEuPathDB; ToxoDB:TGPRC2_426920; -.
DR VEuPathDB; ToxoDB:TGRH88_002580; -.
DR VEuPathDB; ToxoDB:TGRUB_431460; -.
DR VEuPathDB; ToxoDB:TGRUB_431470; -.
DR VEuPathDB; ToxoDB:TGRUB_431480; -.
DR VEuPathDB; ToxoDB:TGVAND_297800A; -.
DR VEuPathDB; ToxoDB:TGVEG_297800; -.
DR HOGENOM; CLU_001042_9_0_1; -.
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; 1.10.287.1490; -; 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 539..670
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 737..965
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 997..1039
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1186 AA; 135202 MW; FAB7C1D93648D143 CRC64;
MASSDGAATL RRSAFARAFF AEKMYIEAIV LEGFKSYSNR VYVGPLHPQF NAVTGLNGTG
KSNILDSICF VLGITNHALV RATKLDDLVY KQGQAGVTKA TVTLKFRNDP HQQNNPLPFP
YREMPEITIT RQIVIGGRDR YLLNSRNAQL KEVRDFFHCC QMNINSPHFM IQQGKITKVI
NMKPKEVLGL IEEVSGTRMY ELKRGNAVKL MQKKEQKLQE ISVVLREEIE PTIERLRKEK
QEYFNFVSMK EEMQRFQRFD VAYRFYSAKQ LLQQGTSDFD ELTQKKAEIE AQIAECDRET
AAAQKQLEDR EKLDGPLQRV RQKKEEVEKL LAKRHSEEKT ARRDLKLFSD ALEDLKKEEQ
KLAKKLAEKR ASRLSETSHA EAAEEEVKRV KEALENAEKK LEGLSTGGAE AGGGASLREK
LKQAKTKAAQ LEAEEEDLKT ELKHVDEELR QVRAKLNKSG ESAAQMTTQR DAAAARVAAL
EKQLAAEAVD EEKLASLREE MKLCRREIDA AKHEAQESQH ELNSWSKIAV RLPRGMHPHK
LHGQVFELVE LKNDYLDFAK ALQLLVGGKL EYVVVEDKDA SKAIFKENNF ASSRRRVTLL
PIQDCQVGKI CDTATLFQNR RLVGLSQDDP RVLRCLDVID FDANRHEKVA LYTFGGSLIC
ATAEMAEKIT YQPNKRQAFP TVTVEGDVFQ TGGVMAGGGS GHVKETLLLW KNFKRCSQMS
QELEERARQI DFYLQPMEQT VQRRTRVTRE LRLAQNELHN IEQLMATSSA GSEMARAQQL
EERRRDCTKR KEEVEAEKGK VLAEVQQLEA DVYELEHNRD KLEASLKKEV KVLRQRLKSL
EASVNTLQKE IGSFRQELMT LEKDLQSVQE DIEKRTQGLA DLQKAIEEKS KLKAKVEDVR
KEIELCLSEA AQSDKKLGEL TGKLKKLQKN KDHLLLTLKK HQHLMNDREK NIGAARQEME
ALQRANDWLH AEERKFNQPG SAYDFRQLRP ETARQRLQAL QVEVQRLQKS VNSAAATLLE
KTEKDLLALV ERKTQVENDK AKIEAVISEL DIKKRQSLET TWLQVNENFT GIFEQLLPNA
QAKLAQVNPR DLMDGLEMRI AFNKRWKESL AELSGGQRSL LALSLILALL KVKPAPVYIL
DEVDAALDLS HTQNIGSMIK TQFPTSQFII VSLKEGMFSH ADVLFR
//