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Database: UniProt
Entry: A0A1B0AGG3_GLOPL
LinkDB: A0A1B0AGG3_GLOPL
Original site: A0A1B0AGG3_GLOPL 
ID   A0A1B0AGG3_GLOPL        Unreviewed;      1403 AA.
AC   A0A1B0AGG3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Condensin complex subunit 1 {ECO:0000256|PIRNR:PIRNR017127};
OS   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI044953-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI044953-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI044953-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   STRING; 7398.A0A1B0AGG3; -.
DR   EnsemblMetazoa; GPAI044953-RA; GPAI044953-PA; GPAI044953.
DR   VEuPathDB; VectorBase:GPAI044953; -.
DR   Proteomes; UP000092445; 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   Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT   DOMAIN          76..239
FT                   /note="Condensin complex subunit 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12922"
FT   DOMAIN          1074..1234
FT                   /note="Condensin complex subunit 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12717"
FT   REGION          1302..1403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          443..477
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1302..1322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1357..1371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1403 AA;  161645 MW;  AE62E205FFA8D0E4 CRC64;
     MDFQFNLPSS NTDLLNSSGD SYYVKHLYSS SEIPDKLKVC KQMLFQSDPF YIFDHFDTYY
     AVIENKSTDA AAMKNLFRAF DLMYITVDKL GSSLAPILAA TEPLAPQQRK GYLNLTKMCL
     FLLVNVVRKI DGNIVRLQQQ QQNSQQKRKS NKQLDTLEEY PDWDVKRGKF LVQLYNLMQC
     PLQKLWNPPV AEENFVNMLC EVCYRTLEVL HMRNDNRHVV DTIFQIFGIA IKRYNHAINF
     PVRILQILRS TEHAGRSIAY GINVLHEEFG ISTVFAVLIK EIIESLSMGS ADTLVSRYFS
     NFLTELATIA PKLMIPHLST LGDELLGCES HVLRNCILQI MGDAVVGELT SEELPEDMKE
     ARDEFLDNLL MHISDISAHV RAKVLQIWNH MKEEQAVPLS FQLKVLCAAV ERLEDKTCSV
     RKQAVQLIKA FLERNPFSAK LTLVELQKKY NEEVEKMEKL SALLAAERKQ AEELEEKWNL
     VIPKMLPFIE DIVKQTQDPP ETQETYEDLV QRINTMLLEE KYQEAVSLVR KADHVAGNSE
     LRLSLKEEEQ CAYYLALLKS YIFLANGCKD SNEEFGTQIK TVKFLQDSIE FSKAISKAMP
     KLQEMLLSKT NSDVFEAVDL FTTGYMFGIK GTENGMRQML YLVWSSDKEK RDAVSDAYKK
     VLFTTDQTGR THALHVVQNL SRFLESLEYG HYTAMECLIK EWVHNEDIDS IIIQVLFERF
     TLKLEGTTEN ESRLALQLLI MCSYAKSSIA SANISIIESI GLGLRGKQDP RIFSGCLEFL
     LNSIDQSSTT KYYKRYEADY SIVQKVTEMY SKFFFHPRIP DFDQVTMKTL QFYYRLCQTP
     DVISQTLVFE ILKQFKKVAV QLGEMTASQH AQALETPFSQ AIPGTQSHLT VAPQLKMPVF
     LLTRFIFMIG YMALKEMIFL DIDVYNNMKY RQELTECEQK KKKSAFTNCN GNRRKTANLN
     MSATESLKRL TGAAAEPQQE PDEDLVGATA EDNVAELINH ICEEILFHDE NALLPKLFPY
     ILEICKYPFK YSDSALQQSA SLALVRFMCV SSRICESYMP FLMNILSHTK NIKIKCNIVI
     GLSDLTFRFP NIIEPWTGHF YSTLHDENTE LRLTAVKMLS HLILHEMIRV KGQIADLAIC
     IVDDNDEIKN ITQQFFKEIA NKSNILYNVL PDIISKLSDS SSNLEEEKYR IIMRYILGLI
     HKDRQVETLV EKLCLRFPVT REERQWRDIA YCLSLLSYNE KTIKKLIDNL QHFKDKVQID
     EVYQSFKLII SNTSKLAKPE LKTLIGELET RINDCLKIRE PTNEDEERNS ENDKETGRKL
     RCLQKKSGKT STRSNNRRRR GKQDSSQSSS PHESSCSSSD FEDEPPKINK NKQQVRSKVI
     QETASSDEEE SQIPRRKRGR NNK
//
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