ID V9KBI0_CALMI Unreviewed; 950 AA.
AC V9KBI0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 {ECO:0000313|EMBL:AFO95149.1};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO95149.1};
RN [1] {ECO:0000313|EMBL:AFO95149.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:AFO95149.1};
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).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; JW862632; AFO95149.1; -; mRNA.
DR AlphaFoldDB; V9KBI0; -.
DR GO; GO:0070603; C:SWI/SNF superfamily-type complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF76; TRANSCRIPTION ACTIVATOR BRG1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 84..249
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 405..567
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 782..852
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 702..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..950
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO95149.1"
SQ SEQUENCE 950 AA; 109974 MW; 2B9BD89E5232DDD3 CRC64;
APEEKKKIQD PDSEDVSEMD ARQIIENAKQ DVDDEYSAAN SSIRGLQSYY AVAHAVTERV
DIQSTLLING LLKQYQVKGL EWLVSLYNNN LNGILADEMG LGKTIQTIAL ITYLMEHKRI
NGPFLIIVPL STLSNWAYEF DKWAPSVVRI SYKGSPAARR AFVPQLRSGK FNVLLTTYEY
IIKDKHVLAK IRWKYMIVDE GHRMKNHHCK LTQVLNTHYV APRRLLLTGT PLQNKLPELW
ALLNFLLPTI FKSCSTFEQW FNAPFAMTGE KLVQVDLNEE ETILIIRRLH KVLRPFLLRR
LKKEVEAQLP EKVEYVIKCD MSALQRVLYR HMQAKGVLLT DGSEKDKKGK GGTKTLMNTI
MQLRKICNHP YMFQHIEESF SEHLGFTGGI VQGADLYRAS GKFELLDRIL PKLRATNHKV
LLFCQMTSLM TIMEDYFAYR SFKYLRLDGT TKSEDRGMLL KTFNEPGSHY FIFLLSTRAG
GLGLNLQAAD TVVIFDSDWN PHQDLQAQDR AHRIGQLNEV RVLRLCTVNS VEEKILAAAK
YKLNVDQKVI QAGMFDQKSS SHERRAFLQA ILEHEEQDEC EVVSAEVKGS DGHTEEDEVP
DDETVNQMIA RSEEEFELFM RMDLDRRREE ARNPKRKPRL MEEDELPNWI LKDDAEVERL
TCEEEEEKMF GRGSRQRKEV DYSDSLTEKQ WLKVAIEEGN LEEIEEEVRQ KKARKRSKRD
VDPPVVMATT STRSSREKDD DEKKKKKRGR PPAEKLSPNP PHLTKKMKKT VDAVIKYKDS
NTGRQLSEVF IQLPSRKELP EYYELIRKPV DFRKIKERIR NHKYRCLNDL ERDVMLLCQN
AQTYNLEGSL IYEDSIVLQS VFTSVRQKIE KEEDSEEDSE EGEEEEEEGS ESESRSVKVK
IRLGRKEKGS DRVKARKRSS RISKSKPIVS DDDTEDEVDE DRSGSGTEED
//
