ID   K8ERG1_9CHLO            Unreviewed;      1227 AA.
AC   K8ERG1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   OrderedLocusNames=Bathy18g00760 {ECO:0000313|EMBL:CCO20636.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO20636.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO20636.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO20636.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) 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. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
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DR   EMBL; FO082261; CCO20636.1; -; Genomic_DNA.
DR   RefSeq; XP_007508145.1; XM_007508083.1.
DR   AlphaFoldDB; K8ERG1; -.
DR   STRING; 41875.K8ERG1; -.
DR   GeneID; 19010743; -.
DR   KEGG; bpg:Bathy18g00760; -.
DR   eggNOG; KOG0933; Eukaryota.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000198341; Chromosome_18.
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   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT   DOMAIN          523..643
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          319..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          239..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          428..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          684..912
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          959..1015
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        319..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  138634 MW;  752F6D219DA96F99 CRC64;
     MYVEEVCIDG FKSYAQRTIV PQFDQYFNAI TGLNGSGKSN ILDSICFVLG ITNLSQVRCS
     SLQELVYKQG QAGITKASVS ITFNNSEKSR SPVGYEHCDQ VTVTRQIVIG GKNKYMINGS
     VAQPTRVQNL FHSVQLNVNN PHFLIMQGRI TKVLNMKPIE ILGMLEEAAG TRMYESKKEA
     ATKTLTKKEL KVTEIDQLLE EEILPTIEKL RKERGEYMKW ASANDTLERL RRFCVAVEFC
     EAEEEMTKAE EESEKLKETV EMHLSKAMEA KAMSQEMDKD IAVKIENREK ACGDQLNASK
     QRVEEKSKEL VKKTSAFEHV SKEMKSEESS LKKLEKSKSD AISADEKRKE KVKDLELEAQ
     REEENLRSAE AEAEKSERKL MNVQTGAGDT SENKSLQTQL MEAIGKVAEC DAKAKSEALR
     QKHIEKEMRE AEKLKACKAK ESAKMQNEMS EAVKMVEKAQ LELASFETEF DDIQDKCAQL
     EEKKASLESA LEDARDSCDQ LEGKLAGLDF KFKNPDVKFD RAKKVKGTIA KLFDVMDEST
     MTALEVIAGG KLYQVVVDSA DTGKALLERG ELQKRVTIVP LDKVDGRKAH DEQVKAAEKV
     SNNEAKLAVS LVTAKDQSVQ SVMNYVFGRA FVCQTQETAK RVAFDKNVLL NCVTVEGDLL
     NPTGLLTGGS RNKGSSVLKK LKAFSEAEMK ASELRDDIER CDRDIEKAKI ERKKYTELET
     KLDQCEHKLN LLKEKNSESE AFQLEEKRMK LTNELEECER NVREMARVKE ETLALQKKLD
     AEIKNFAKER QNLLKDAEKK VKETKKLVND IKERIKKKET IVLDARVEKE AAMKAIASLE
     EDIEHAKGGI ETLSKKVIEF EREMINAQQA FDEESKALEI IQTKLRETDD EIASLRKQKS
     KLEQKHMDES VEAKKLNFKI DQFAKAASDA QSRFHLLEKE HPWATEHERQ LFGKEGTEYD
     FSKRDVKKAQ KQLQEAEETQ KQLGKRVNKK VIAMFDKAEQ EFKQLQEKRR IVLNDRSKIE
     KVIHELDEKK RETLELVWQK VTKDFGSIFS TLLPGTRAKL EPVEGTTFLD GLEVKVAFGE
     VWKESLSELS GGQKSLLALS LILALLLFKP APIYILDEVD AALDLSHTQN IGRMIRTHFP
     FSQFIVVSLK EGMFNNANVI FRTKFVDGLS TVSRTAPALK DKVTEEDKKD GGALGAAAQK
     RADKSTTTTT KAAAKKGHVA KENAAPL
//