ID   A0A1X7RMH9_ZYMTR        Unreviewed;      1211 AA.
AC   A0A1X7RMH9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=ZT3D7_G3763 {ECO:0000313|EMBL:SMQ48613.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ48613.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ48613.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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DR   EMBL; LT853694; SMQ48613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RMH9; -.
DR   STRING; 1276538.A0A1X7RMH9; -.
DR   Proteomes; UP000215127; Chromosome 3.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   CDD; cd03272; ABC_SMC3_euk; 1.
DR   Gene3D; 1.10.287.1490; -; 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; IPR041741; SMC3_ABC_euk.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
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   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215127}.
FT   DOMAIN          522..634
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          370..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          186..220
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          413..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          694..746
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          780..807
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          860..922
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          978..1005
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1211 AA;  137687 MW;  0AF8DDCFE84C2D51 CRC64;
     MYIKQIIIQG FKSYKDQTVI EPFSPKHNVI VGRNGSGKSN FFAAIRFVLS DKYTQLGRED
     RQGLLHEGAG SAVMSAYVEL IFDNTDERFP TNTPEVILRR TIGQKKDEYS LNRKNTTKQE
     VLNILESAGF SRSNPYYIVP QGRVTAITNM KDNERLNMLK TVAGTEVYES RRSESRKIMD
     ETHHKREKID DLLEHIRGRL NELEEEKEEL REYQDKDRER KCLEYTIHHH DQEMLQDHLD
     RIDGDREEGA EQNDEHREAL EAGEKQLEKI DVQIAGLQQQ IKLLTEEKAQ YKEDRTETAR
     AKAKAESDVL GMQENQNAAQ QAQSDRANQL RDVQALIKQH ETTLAQLLPE FNAKRAEAKD
     LKEQVQEAES TRQRLYSKQG RQNQFKTKKE RDEWLRKEVS EIHNILATRK ANSMQITEDI
     AELESQIGQL EEDIAELRNR IENRGDEQHN VSAEIQQAAE EKARLQDQRK ELWREEAKLD
     SVIANARLEL EKAERFLGQM MDASTARGLA SVRRIVEQDG IEGVYGPLGE LFDCRDSYKT
     AAEVTAGASL FHYVVEDDEV AETLIKRLQA EKGGRVTFTP LNRVKVRPVE MPKASDAVAL
     LSKLRYDGKY EKAMQQVFGK TIVCPNLQVA AQYARSHAVS AITPEGDRSD KKGALTGGFH
     DARNSRIDGL RRMKAARLEY DGTRSRKDEI GNELKQIDQK VSKAMSSLEK VQQKRDQMDG
     GYGPMREELR RKELDLRNRR EEVSGKQNQH DGISSLLSDL GNQLSGFEAE LASEFKKSLS
     NQEERQLEQL NSQLPDLKKQ YTTLYNELAD LEGTKRNTED TLSVNLRPRR DELLAADLDN
     DATRSGAGDS TKLKERKSEV KRATKRLDGI DAKLKEIDDA IDEAQNQLGA SEASRATKRG
     EVDRIEKAMQ NHQKNVERGA QRRAGHAARL AEVQNQIRNL GIVPDAAYKP QYKNMTVNTA
     TQKLHKVQES LKKYGHVNKK AFEQYQQFEK QRADLEERRK GLDSSDSSIR ELIDVLDMRK
     DEAIERTFKQ VSKAFAEIFV KLVPAGKGRL IIQRRSDKNA NGGAAPDDSD EDEDEETVRA
     RTGVENYIGV GISVSFNSKH DEQQRIQQLS GGQKSLCALA LVFAIQRSDP APFYLFDEID
     ANLDAQYRTA VAQLLEESAE TGQFICTTFR PEMLLVAEKC YGVSYLNKAS SIDVVSTEQA
     LDFVEGQISG K
//