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Database: UniProt
Entry: G1SFT5_RABIT
LinkDB: G1SFT5_RABIT
Original site: G1SFT5_RABIT 
ID   G1SFT5_RABIT            Unreviewed;       515 AA.
AC   G1SFT5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Chromo domain-containing protein {ECO:0000259|PROSITE:PS50013};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001399.4, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000001399.4, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000001399.4}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001399.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G1SFT5; -.
DR   SMR; G1SFT5; -.
DR   STRING; 9986.ENSOCUP00000001399; -.
DR   Ensembl; ENSOCUT00000001632.4; ENSOCUP00000001399.4; ENSOCUG00000001628.4.
DR   eggNOG; KOG0384; Eukaryota.
DR   GeneTree; ENSGT00940000155888; -.
DR   HOGENOM; CLU_000315_8_1_1; -.
DR   InParanoid; G1SFT5; -.
DR   TreeFam; TF300674; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000001628; Expressed in autopod skin and 16 other cell types or tissues.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   PANTHER; PTHR45623:SF19; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   PROSITE; PS00598; CHROMO_1; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          274..366
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          391..469
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          32..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..213
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..264
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  58497 MW;  FC31774D42D2AF99 CRC64;
     MAQKRRGGSL SLPPCVFTWY RTFSQLAFDG DKLSHSASEE ASGSDSGSQS ESEQGSDPGS
     RHGSESNSSS ESSESPSESE SESAGSKSQP VLPEAKEKPA SKKERIADVK KMWEEYPDVY
     GVRRSNRSRQ EPSRFNIKEE ASSGSESGSP KRRGQRQLKK QEKWKREPSE DEREQGTSAE
     SEAEQKKVKA RRPVPRRTVP KPRVKKQTKT QRGKRKKQDS SDDDDEDDEA PKRQTRRRAA
     KNVSYKEDDD FETDSDDLIE MTGEGVDEQQ DNSETIEKVL DSRLGKKGAT GASTTVYAVE
     ANGDPGGDFD TEKDEGEVQY LIKWKGWSYI HSTWESEESL QQQRVKGLKK LENFKKKEDE
     IQQWLGKVSP EDVEYFNCQQ ELASELNKQY QVVERVIAVK TSKSTLGQTD FPAHSRKPAP
     SNEPEYLCKW MGLPYSECSW EDEALIGEKF QSCIDSFHSR NNSKTIPARE CKALKQRPRF
     VALKKQPAYL GGENLELRDY QLEGLNWLAH SWCKW
//
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