ID A0A0D2J0D3_9EURO Unreviewed; 1226 AA.
AC A0A0D2J0D3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Condensin complex subunit 1 {ECO:0000256|PIRNR:PIRNR017127};
GN ORFNames=Z520_01282 {ECO:0000313|EMBL:KIY02817.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY02817.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY02817.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY02817.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN848063; KIY02817.1; -; Genomic_DNA.
DR RefSeq; XP_016636939.1; XM_016771800.1.
DR AlphaFoldDB; A0A0D2J0D3; -.
DR STRING; 1442371.A0A0D2J0D3; -.
DR GeneID; 27707028; -.
DR VEuPathDB; FungiDB:Z520_01282; -.
DR OrthoDB; 5480287at2759; -.
DR Proteomes; UP000053411; 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; 1.
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:UP000053411}.
FT DOMAIN 87..249
FT /note="Condensin complex subunit 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12922"
FT DOMAIN 1037..1202
FT /note="Condensin complex subunit 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12717"
FT REGION 147..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 137191 MW; AE9572B2DC9AF8B3 CRC64;
MEDQVDFDIN ESLKLYLSDV MTIATPEASP ELIDCENDPD SLSPGSVDSA LDSVIDLITE
NPEALLRSST FDTLQFLLKH SSVLSTQSLG KVLTLIVSGL STTADIANQD IENDEQETLP
QHKRLLEMYA FLLQWAVSAV EAKAQEKSSA APARRGGKGA KSKSAAKDNS WDSSDQIQSA
MDVMCRVMKL KLNRIFQTTS DRDTFINLFT RSIYLIMESE TRVKITAVRM FCFKVLCVAV
KHHGHALGAQ TSIVQNLTYF EHLSEPMAEF LHILSEQYDY PQLSAEILRE LAAKEFSQND
NKGPKSVSAF IIKLSELEPR LVIKEMGLLA KFLDSEAHTL RCAVIEVCGN LLADLSRQEE
KTETTKIQIN AFFDTLEQRF LDTAPFCRVR AMQVLTKICD LEQKFPKRRQ NASELAMQSL
QDKSSNVRRN AIKLLRKLVS SHPFSLMHGG QLSHKEWTER LEAVESQLDA LKPPPESPGM
ARTAAGEEQV DQDLLDDATQ AEEEPQEMTE EEKIAAVKKA QEEAATSEVI GKLQLTRKYY
LEALKFIETI HDASEIAVQL LSSPNKSEVI DVMDFFVTID AFKVETARKG IRRMMRLIWT
KGNSDEGKGV QAHLIDNYKS LFFDAPDMFS TNDAANFVAR NMISLTFGAT PAELTSLEQL
LSTMFKAGHI SELVIAKLWQ VYGVNKEISR AQRRGAIIVL GMIALASPEV VVKEIDTMLR
VGLGQLGRTD FVLAKFTCVA LRRMIPTTKK VQEKTASAGL SKMSNNHEVL RMLASILLTT
SASKDWYGMA EQAISAIYVL SDHPDVLCSE VLRQKTRLVF QQTKDLSSLS RTPSPEPDAM
DIDGEEQVTN PEAEPHEPVP TETKQEKPSI ALSQLLFAVG HIAVKQIVHL ELCELDFKRR
KQDQEKNKPV ANSSPDKSSA PTPAQRKRTA AEEVLAEKQK EEEKDELDLI GGTTEDDFTE
AIVHIREREL LYGSHSLLAN FGPLVTEICA NNTAYKDRNL QAQATLCLAK LMCVSSEYCE
KNLPLLITIL ERSTDPIVRS NAVIALGDMA VCFNHLIDEN TDFLYRRLND ADESVKRTCL
MTLTFLILAG QVKVKGQLGE MAKCLEDADK KIADLARMFF TELATKDNAV YNQFVDMFSV
LTQEGPLEGG VMEEEAVKRI LKFLCGFIEK DKHAKNLAEK LAARLNRCAN KRQWDDTAYA
LSLLQHKNED ITRKIQEGYR VVETEA
//
