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Database: UniProt
Entry: A0A4W3JNW3_CALMI
LinkDB: A0A4W3JNW3_CALMI
Original site: A0A4W3JNW3_CALMI 
ID   A0A4W3JNW3_CALMI        Unreviewed;       981 AA.
AC   A0A4W3JNW3;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 {ECO:0000313|Ensembl:ENSCMIP00000039753.1};
GN   Name=SMARCA5 {ECO:0000313|Ensembl:ENSCMIP00000039753.1};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000039753.1, ECO:0000313|Proteomes:UP000314986};
RN   [1] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17185593; DOI=10.1126/science.1130708;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Ancient noncoding elements conserved in the human genome.";
RL   Science 314:1892-1892(2006).
RN   [2] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17407382;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Survey sequencing and comparative analysis of the elephant shark
RT   (Callorhinchus milii) genome.";
RL   PLoS Biol. 5:E101-E101(2007).
RN   [3] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
RN   [4] {ECO:0000313|Ensembl:ENSCMIP00000039753.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   AlphaFoldDB; A0A4W3JNW3; -.
DR   Ensembl; ENSCMIT00000040324.1; ENSCMIP00000039753.1; ENSCMIG00000016087.1.
DR   GeneTree; ENSGT00940000156733; -.
DR   Proteomes; UP000314986; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   CDD; cd00167; SANT; 2.
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; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-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:UP000314986}.
FT   DOMAIN          120..285
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          415..566
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          768..820
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          40..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          944..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..974
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   981 AA;  114762 MW;  2C1C940CB1FDBC74 CRC64;
     MHKFINSVYP FYKTDRANRF DYLLQQTELF AHFIQPAAQK TPTSPLKMKP GRPRMKKDEK
     QNLLSAGDNR HRRTEQEEDE ELLSENSKTT NVCTRFEESP SYVKNGKLRD YQIRGLNWLI
     SLYENGINGI LADEMGLGKT LQTIALLGYM KCYRGIPGPH MVLVPKSTLY NWMAEFKRWV
     PSLRAICLIG DKEQRAAFIR DVLLPGEWDV CVTSYEMLIR EKSVFKKFNW RYLVIDEAHR
     IKNEKSKLSE IVREFKTTNR LLLTGTPLQN NLHELWALLN FLLPDVFNSA DDFDSWFDTN
     NCFGDQQLVE RLHLVLRPFL LRRIKTEVEK SLPPKKEVKI YVGLSKMQRE WYTRILMKDI
     DILNSSGKMD KMRLLNILMQ LRKCCNHPYL FDGAEPGPPY TTDIHLAVNS GKMVVLDKLL
     PKVKEQGSRV LVFSQMTRVL DILEDYCMWK NYEYCRLDGQ TPHEERQESI CSFNAPGSTK
     FLFMLSTRAG GLGINLATAD VVILYDSDWN PQVDLQAMDR AHRIGQTKQV RVFRFITDNT
     VEERIVERAE MKLRLDSIVI QQGRLVDQNL NKLGKDEMLQ MIRHGATHVF ASKDSEITDE
     DIDGILERGE KKTAEMNEKL SNMGEGLLRN FTMDTEVSVY NFEGEDYREK QKLALTEWIE
     PPKRERKANY AVDAYFREAL RVSEPKAPKA PRPPKQPSIQ DFQFFPPRLF ELLEKEILYY
     RKTIGYKVPR NPDLSNAAQV QKAEQGKIDE AEPLNDDEIE EKEKLLTQGF TSWTKRDFNQ
     FIKANEKWGR DDIENIAREV EGKSPEEVIE YSAVFWERCN ELQDIEKIMA QIERGEARIQ
     RRISIKKALD TKIGRYKAPF HQLRIAYGTN KGKNYTEEED RFLICMLHKL GFDKENVYDE
     LRQCIRNSPQ FRFDWFLKSR TAMELQRRCN TLITLIEREN LELEEKEKAE RKKRGPKTSS
     AQKRKADGTP DGRGRKKKLK L
//
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