CND3_SCHPO
ID CND3_SCHPO Reviewed; 875 AA.
AC Q10429;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Condensin complex subunit 3;
DE AltName: Full=CAPG homolog;
DE AltName: Full=p100;
GN Name=cnd3; ORFNames=SPCC188.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 453-466 AND 727-760,
RP FUNCTION, AND IDENTIFICATION IN A CONDENSIN COMPLEX WITH CUT3; CUT14; CND1
RP AND CND2.
RX PubMed=10485849; DOI=10.1101/gad.13.17.2271;
RA Sutani T., Yuasa T., Tomonaga T., Dohmae N., Takio K., Yanagida M.;
RT "Fission yeast condensin complex: essential roles of non-SMC subunits for
RT condensation and Cdc2 phosphorylation of Cut3/SMC4.";
RL Genes Dev. 13:2271-2283(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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. The condensin complex probably
CC also plays a role during interphase. {ECO:0000269|PubMed:10485849}.
CC -!- SUBUNIT: Component of the condensin complex, which contains the
CC cut14/smc2 and cut3/smc2 heterodimer, and three non SMC subunits that
CC probably regulate the complex: cnd1, cnd2 and cnd3.
CC {ECO:0000269|PubMed:10485849}.
CC -!- INTERACTION:
CC Q10429; Q9Y7R3: cnd2; NbExp=2; IntAct=EBI-1149700, EBI-1149594;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found in the
CC cytoplasm, while a minority of the complex is associated with
CC chromatin. A subpopulation of the complex however remains associated
CC with chromosome foci in interphase cells. During mitosis, most of the
CC condensin complex is associated with the chromatin. At the onset of
CC prophase, condensin associates with chromosome arms and to chromosome
CC condensation. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC {ECO:0000305}.
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DR EMBL; AB030214; BAA82626.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB41223.1; -; Genomic_DNA.
DR PIR; T43522; T43522.
DR RefSeq; NP_588207.1; NM_001023197.2.
DR PDB; 5OQR; X-ray; 2.61 A; A/B=1-823.
DR PDBsum; 5OQR; -.
DR AlphaFoldDB; Q10429; -.
DR SMR; Q10429; -.
DR BioGRID; 275693; 22.
DR IntAct; Q10429; 1.
DR STRING; 4896.SPCC188.03.1; -.
DR iPTMnet; Q10429; -.
DR MaxQB; Q10429; -.
DR PaxDb; Q10429; -.
DR PRIDE; Q10429; -.
DR EnsemblFungi; SPCC188.03.1; SPCC188.03.1:pep; SPCC188.03.
DR GeneID; 2539121; -.
DR KEGG; spo:SPCC188.03; -.
DR PomBase; SPCC188.03; cnd3.
DR VEuPathDB; FungiDB:SPCC188.03; -.
DR eggNOG; KOG2025; Eukaryota.
DR HOGENOM; CLU_004446_1_0_1; -.
DR InParanoid; Q10429; -.
DR OMA; NHQKNFV; -.
DR PhylomeDB; Q10429; -.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q10429; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..875
FT /note="Condensin complex subunit 3"
FT /id="PRO_0000095045"
FT REPEAT 55..76
FT /note="HEAT 1"
FT REPEAT 77..113
FT /note="HEAT 2"
FT REPEAT 117..154
FT /note="HEAT 3"
FT REPEAT 157..192
FT /note="HEAT 4"
FT REPEAT 222..259
FT /note="HEAT 5"
FT REPEAT 379..418
FT /note="HEAT 6"
FT REPEAT 516..554
FT /note="HEAT 7"
FT REPEAT 556..591
FT /note="HEAT 8"
FT REPEAT 740..778
FT /note="HEAT 9"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..875
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5OQR"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 211..215
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 267..273
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 308..324
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 336..348
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 356..372
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 378..394
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 399..412
FT /evidence="ECO:0007829|PDB:5OQR"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 416..434
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 492..506
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 535..549
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 553..569
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 572..589
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 598..609
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 615..632
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 636..648
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 656..670
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 674..696
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 704..717
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 720..722
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 741..752
FT /evidence="ECO:0007829|PDB:5OQR"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 760..771
FT /evidence="ECO:0007829|PDB:5OQR"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 780..794
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 802..820
FT /evidence="ECO:0007829|PDB:5OQR"
SQ SEQUENCE 875 AA; 100491 MW; 38A67C9A1A61A0CE CRC64;
MSCIQIISSS QTSIAGHRKL CNKLFTLRTQ EGFETDILRA LNIILTVKKG NSNADRVLRF
LVTFVNYLQQ KDPEIDIVQP ILKHILRGLD AKDKTVRYRC CQIIARVVNC VKEIDDDLYN
TLKEKLLSRV LDRESIVRLE AVVALSRLQE DTGDEENDVR NILLFLLQND PSSEVRRSVL
LNIEVSNSTL PFILERARDV DAANRKCVYA RVLPKIGDFR YLSIKKRVRI LKWGLNDRDE
SVEKAAADML AYQWIENADN NLLELLERLD VSNNSDVAVL AIKKFFDVRV DSLSQLEFPE
QFWLELTAES SLLARTFNEI CIEKNYTDLL DKMPEVVQLT YYIERQYVSL RDKSSYDESC
FIIEQLLYIG LSQDMVDEIG RRKLLKSLTN SLSTMALPDS LISLHIELLR KLCSSENDFC
SLLVEIITEV FEQGHSQNQT EEQGNSNAPE LNKNDYEGEE ITVSQKSPSP SLPPNELNEP
EPDDMDGYKE AFNELRCLSY VQCLFENITS SLNENLYMVD MLKTLIIPAV RSHDLPIREK
GLECLSLVCL LNADLAFENV PLYLHCYEKG SVVLKCTAIR TLTDMLIQHG KAKFTEYEDA
ISSILFEALG EFENAELQTL GAEAIAKLLV ILHYRDELFL KPLIIQYFEP NTVDNHALRQ
VLGYFFPVYA FGAHENQWRI ATIFCDALLS LLEIYRDLDE DDVQLSIGHI AQQMLDWTDN
EKLYERKTQT GDDYIALNHN VHLHLANMIF ESLPNASEGK ERKFMISLLG KLKIPTDLPS
SDYQRTKRKL ETYESHGFTM DSTSLSILAK FERMLLQNEE ARSKFEETEE ERLMENAEEN
EHAGAEAISG EIIPDTVEAN MEDEEEVYVK QEEDL
