ID A0A316V3S4_9BASI Unreviewed; 1437 AA.
AC A0A316V3S4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE RecName: Full=Condensin complex subunit 1 {ECO:0000256|PIRNR:PIRNR017127};
GN ORFNames=FA14DRAFT_82463 {ECO:0000313|EMBL:PWN31904.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN31904.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN31904.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN31904.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- FUNCTION: Regulatory subunit of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases.
CC {ECO:0000256|PIRNR:PIRNR017127}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000256|ARBA:ARBA00009606, ECO:0000256|PIRNR:PIRNR017127}.
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DR EMBL; KZ819606; PWN31904.1; -; Genomic_DNA.
DR STRING; 1280837.A0A316V3S4; -.
DR InParanoid; A0A316V3S4; -.
DR OrthoDB; 5480287at2759; -.
DR Proteomes; UP000245771; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR007673; Condensin_cplx_su1.
DR InterPro; IPR024324; Condensin_cplx_su1_N.
DR PANTHER; PTHR14222; CONDENSIN; 1.
DR PANTHER; PTHR14222:SF2; CONDENSIN COMPLEX SUBUNIT 1; 1.
DR Pfam; PF12717; Cnd1; 1.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR017127};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|PIRNR:PIRNR017127}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067,
KW ECO:0000256|PIRNR:PIRNR017127};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|PIRNR:PIRNR017127};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245771}.
FT DOMAIN 85..253
FT /note="Condensin complex subunit 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12922"
FT DOMAIN 1112..1273
FT /note="Condensin complex subunit 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12717"
FT REGION 145..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 158971 MW; 84AB4A50FF4B74A9 CRC64;
MSSSQSDGGN AIASEEGRFS LADELVAHRD ENYTITNELE ASSLGDHLDT LVDTLSLSPS
SIDTEEIFDH IKSFLQHFAI LKGPQRSKLL DSLSSAYVVQ LDAATRDLES EGIERYKEHS
ETLEKYAFAM QWFIHAAEKA FNSREERAAA SAGGANTEAR GKGANKNKNT SSSWDWQRSV
PAVLATLTKS LRLSTSILFP LSASRDAFVS GCVLRPALLL QENEAHLKIP LIKMSIFKVI
CNSVKNHGQA FAVQTSIMQA LAYYEHLPEP MAELLTYLRT EFDYERLGDE VLREVASREF
GGLDTKGPRC FARFLVRMAE LSPRSVLRVM VVLKKHLDSD SYPMRNAMLE VLGILIKDLT
MTDDAIPQPS EGDGADDSGA NGNNLSSQDD EDDENRREKG DARKKQIEQF WGLICERFLD
VNSYVRCKCI AVCAKLCELD AKFPSQRTIL TTQSIQSLSD KSSTVRKNAI NLLTRLILTH
PFGMHGGDLD KEEWEKRLAT IDNQLKEYDG VLDVPNEPED RTIQDEEMES VEGEDKSDSM
DTEEDGDASQ ETATAGDQDG DQTTTAGKGE ASSESRKKPR ASIDLETLAS QLSPADAEKV
IRLRLTRRYH TDALAFIDQL SLAVPTLSQL LVSTSKAEVL ESMEFFRVAH EYQVPGARIG
VRKMIHLIWT KDNNTLVMED GKELKGIKSR LIEVYRSLYF DPLPSKSNTD NINRIARNLV
ERTFDVTLAE LTSLEELLST MCGEGMIDER VIDKLWSVYS SPKAIPRAQR RGAIIILSML
AVARKEIVAD HIDTLLGTGL GGLGAKDVVL AKYTCVALSR VGGSVKKVKG ALSDNQLRFP
MNHPMFARLR AAIQWPSTSG QWFSLAEHAI QTIYLLGEQP DALCSEMIKQ MTVRVFGSSG
PKMSMADSAS VPPTPNSHLG ESTPAPSTSA NRTSAFGLAQ LLFVVGHVAL KQIVYLELVE
REFKRRKAEA DKEKVLANKD ANKPDENSAE QQETTKGAKK GKGSQRGKKK AEAPAEEDAD
ELDQVAGNAE DDIGDVVGEV REKELLYGPR SLLSLFGPVV VHICSNPTAY KNDFLRKAAV
LSMCKFMCVS SQFCEAQLPL VLSVLSTSQD PVVRSNIVIA LGDCAISFGS LIDENSEKLY
AGLGDSDLGV KKHTLMVLTH LILNGQVKAK GQLGEMAKCL EDEDERIADL AKLFFTELAT
KDNAVYNNLP DIISHLSIGE HAVDEETFGR VMRFVFTFVD KERQAENVVE KLCQRFRISP
EERQWRDIAF CLSLLPFKSD RSMKRLIEGL PFYQDKLYDP TVFKRFTEIL TKARTNRSNN
PGGATSSAYE TELQEFEQIL ESARAHGAQD AELESATQAK LARARRRQGG KGALPLTSDS
TNVSPVKPTS KASEPAAAKS KAKKPSATAA ATNARSTRRT TRRTRQVIED EDEDFDE
//
