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Database: UniProt
Entry: G1T4M2_RABIT
LinkDB: G1T4M2_RABIT
Original site: G1T4M2_RABIT 
ID   G1T4M2_RABIT            Unreviewed;      1051 AA.
AC   G1T4M2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 {ECO:0000313|Ensembl:ENSOCUP00000011238.4};
GN   Name=SMARCA5 {ECO:0000313|Ensembl:ENSOCUP00000011238.4};
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:ENSOCUP00000011238.4, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000011238.4, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000011238.4,
RC   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:ENSOCUP00000011238.4}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000011238.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   EMBL; AAGW02045719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02045720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02045721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02045722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002716976.1; XM_002716930.3.
DR   AlphaFoldDB; G1T4M2; -.
DR   SMR; G1T4M2; -.
DR   STRING; 9986.ENSOCUP00000011238; -.
DR   PaxDb; 9986-ENSOCUP00000011238; -.
DR   Ensembl; ENSOCUT00000013053.4; ENSOCUP00000011238.4; ENSOCUG00000013042.4.
DR   GeneID; 100344339; -.
DR   KEGG; ocu:100344339; -.
DR   CTD; 8467; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   GeneTree; ENSGT00940000156733; -.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   InParanoid; G1T4M2; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000001811; Chromosome 15.
DR   Bgee; ENSOCUG00000013042; Expressed in ovary and 16 other cell types or tissues.
DR   GO; GO:0016590; C:ACF complex; IEA:Ensembl.
DR   GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR   GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0016589; C:NURF complex; IEA:Ensembl.
DR   GO; GO:0031213; C:RSF complex; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0090535; C:WICH complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR   GO; GO:0140751; F:histone octamer slider activity; IEA:Ensembl.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:Ensembl.
DR   GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR   CDD; cd18064; DEXHc_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          191..356
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          486..637
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          839..891
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  121709 MW;  12987184DDEBEB16 CRC64;
     MSAAEPPPPP PPESAPSKPA ASAASSGSNS GNKGGPEGVA AQAAASAASA GSADADMEEV
     FDEASPGKQK EIQEPDPTYE EKMQTDRANR FEYLLKQTEL FAHFIQPAAQ KTPTSPLKMK
     PGRPRIKKDE KQNLLSVGDY RHRRTEQEED EELLTESSKA TNVCTRFEDS PSYVKWGKLR
     DYQVRGLNWL ISLYENGING ILADEMGLGK TLQTISLLGY MKHYRNIPGP HMVLVPKSTL
     HNWMSEFKRW VPTLRSVCLI GDKEQRAAFV RDVLLPGEWD VCVTSYEMLI KEKSVFKKFN
     WRYLVIDEAH RIKNEKSKLS EIVREFKTTN RLLLTGTPLQ NNLHELWSLL NFLLPDVFNS
     ADDFDSWFDT NNCLGDQKLV ERLHMVLRPF LLRRIKADVE KSLPPKKEVK IYVGLSKMQR
     EWYTRILMKD IDILNSAGKM DKMRLLNILM QLRKCCNHPY LFDGAEPGPP YTTDMHLVTN
     SGKMVVLDKL LPKLKEQGSR VLIFSQMTRV LDILEDYCMW RNYEYCRLDG QTPHDERQDS
     INAYNEPNST KFVFMLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAMD RAHRIGQTKT
     VRVFRFITDN TVEERIVERA EMKLRLDSIV IQQGRLVDQN LNKIGKDEML QMIRHGATHV
     FASKESEITD EDIDGILERG AKKTAEMNEK LSKMGESSLR NFTMDTESSV YNFEGEDYRE
     KQKIAFTEWI EPPKRERKAN YAVDAYFREA LRVSEPKAPK APRPPKQPNV QDFQFFPPRL
     FELLEKEILY YRKTIGYKVP RSPDLPNAAQ AQKEEQLKID EAEPLNDEEL EEKEKLLTQG
     FTNWNKRDFN QFIKANEKWG RDDIENIARE VEGKTPEEVI EYSAVFWERC NELQDIEKIM
     AQIERGEARI QRRISIKKAL DTKIGRYKAP FHQLRISYGT NKGKNYTEEE DRFLICMLHK
     LGFDKENVYD ELRQCIRNSP QFRFDWFLKS RTAMELQRRC NTLITLIERE NMELEEKEKA
     EKKKRGPKPS TQKRKMDGAP DGRGRKKKLK L
//
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