ID A0A401KNV8_ASPAW Unreviewed; 1200 AA.
AC A0A401KNV8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Condensin complex subunit 1 {ECO:0000256|PIRNR:PIRNR017127};
GN ORFNames=AAWM_03868 {ECO:0000313|EMBL:GCB20983.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB20983.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB20983.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB20983.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB20983.1}.
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DR EMBL; BDHI01000007; GCB20983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KNV8; -.
DR STRING; 105351.A0A401KNV8; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:TreeGrafter.
DR GO; GO:0000796; C:condensin complex; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:TreeGrafter.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:InterPro.
DR FunFam; 1.25.10.10:FF:000272; Condensin complex subunit 1; 1.
DR FunFam; 1.25.10.10:FF:000920; Condensin complex subunit 1; 1.
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 Pfam; PF20168; PDS5; 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:UP000286921}.
FT DOMAIN 101..263
FT /note="Condensin complex subunit 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12922"
FT DOMAIN 1015..1175
FT /note="Condensin complex subunit 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12717"
FT REGION 836..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 134013 MW; A1E3C5BA577ADB55 CRC64;
MEDRIQFDIN ESLKHYLSDP ASVPTPDADP ELLDCETDPD QLSSALIDNV LNPIVDAVAE
NPEGLARSSS FDSLQFLLKC ALPPDMSSRP QKESIVTNLS LSKLLDLIVS GLSVEADIIH
GELESDEQDG IQHHKQLLEM YGFLLQWALS AVEVKAAEKP AEPVPARRGA GKSARSKANA
KDGNWDWTAQ IQISMETMCK VMKLKLSRIF LTTSDRDTFI NLFTRSIYLI LESEQRVKSM
SIRMHAFKVL CIAVKHHGHA FGAQTSIVQS LTYFEHLSEP MAEFLHILAE QYDYPQLSDE
ILKELGNKEF NSNDTRGPKS VSAFIVKLSE LAPRLIIKQM TLLAKQLDSE SYTLRCAVIE
VCGNLIADLS RQEERSDNYK TQINAFFDVL EERFLDINPY CRCRAIQVYM RICDLEQKFP
KRRQAVAELA ARSLEDKSSN VRRNAIRLLA KLVSTHPFSV MHGGQLSHKE WSARLDTVDA
ELNALRPPET PGFDGADASH VDSALLDDAT QLPEDSPSKA SGLSEEEKAT AIKKAAEQAA
TSELLARLQL TRKYYNEAIR FIEVLQSSSG LVAQLLSSRN KSEAIEAMDF FVVLDAYKVE
TSRSGIRRML RLIWTKGNSD EGKGVQTHLI DCYKGLFFEA PDSFSPNDAA NYIARNMISL
TFGSTPAELT CLEQLLSTMM RAGHISDAVI AKLWQVYGVQ KKEISRTQRR GAIIVLGMLA
LADPEVVIKE IETMLRIGLG SLGRSDLVLA KYTCIALRRM VPGRQAKSKD VGIPKLGNDH
AVLTKLGAIV ETISDSKEWY GVAEQAIGAI YALSKHPDVL CSDILKRKTR FVFQPQIQRS
PSEVSDDGEE QRPETASTDG QGAKQETSST SLSQLLFVVG HIAIKQIVHL ELCELDFKRR
KAEQEKNKTT NTSNQKNDNA EDDELDLIGG TTEDDFQDAM AHIRERELLY GENSLLSNFG
PLVTEICANS NIYADRNLQA AATLCMAKLM CVSADYCEKN LPLLITIMER SEDPTVRSNA
VIALGDMAVC FNHLIDENTD FLYRRLNDDE ASVKRTCLMT LTFLILAGQV KVKGQLGEMA
KCLEDEDKRI ADLARMFFTE LAGKDNAVYN HFVDMFSLLS AERNLEEASL RRIVKFLIGF
VEKEKHARQL AEKLAARLPR CETERQWNDV AYALSLLPHK NEEITKTITA GFNKVVTANA
//