ID A0A091FNR4_CORBR Unreviewed; 1467 AA.
AC A0A091FNR4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative global transcription activator SNF2L2 {ECO:0000313|EMBL:KFO62950.1};
DE Flags: Fragment;
GN ORFNames=N302_11293 {ECO:0000313|EMBL:KFO62950.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO62950.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO62950.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO62950.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK719351; KFO62950.1; -; Genomic_DNA.
DR STRING; 85066.A0A091FNR4; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0070603; C:SWI/SNF superfamily-type complex; IEA:UniProt.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18063; DEXHc_SMARCA2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 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; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
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:SF541; GLOBAL TRANSCRIPTION ACTIVATOR SNF2L2-RELATED; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 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.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 3: Inferred from homology;
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};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976}.
FT DOMAIN 97..132
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 334..406
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 635..800
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 949..1111
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1296..1366
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1406
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO62950.1"
FT NON_TER 1467
FT /evidence="ECO:0000313|EMBL:KFO62950.1"
SQ SEQUENCE 1467 AA; 168027 MW; 8EDC4BF1758D27E3 CRC64;
QSVDGLHEKG MVEDVHCGSM KSMRPPHPGM GPPQSPMDQH SQGYMSPHPS PLGAPEHVSS
PMSGGGPTPP QMTPSQPGPI IAGDPQVMNQ PNRGPSPFSP AQLHQLRAQI LAYKMLARGQ
PLPENLQLAV QGKRTLPGIQ QQQPPSAFNR QSGIGLHAMS GAATGPGPAP GMPGHTAAIT
PKTWTEGQAP DMNVSNAQQK LPAPAPSGRP SPAPPATQPA AKQTLTAPTK KPQGLDPVEI
LQEREYRLQA RIAHRIQELE NLPGSLPPDL RTKATVELKA LRLLNFQRQL RQEVVACMRR
DTTLETALNS KAYKRSKRQT LREARMTEKL EKQQKIEQER KRRQKHQEYL NSILQHAKDF
KEYHRSVAGK IQKLSKAVAT WHANTEREQK KETERIEKER MRRLMAEDEE GYRKLIDQKK
DRRLAYLLQQ TDEYVANLTN LVWEHKQAQA AKEKKKRRRR KKATEENAEG MASGLGPDGE
PIDESSQMSD LPVKVTHTET GKVLLGPEAP KASQLDAWLE MNPGYEVAPR SDSEDESGSE
YEEEDEEEES SRLEADEKIL LDPNSEEVSE KDAKQIIETA KQDVDDEYSM QYSARGSQSY
YTVAHAITER VEKQSSLLIN GTLKHYQLQG LEWMVSLYNN NLNGILADEM GLGKTIQTIA
LITYLMEHKR LNGPYLIIVP LSTLSNWTYE FDKWAPSVVK ISYKGTPAMR RSLVPQLRSG
KFNVLLTTYE YIIKDKHILA KIRWKYMIVD EGHRMKNHHC KLTQVLNTHY VAPRRILLTG
TPLQNKLPEL WALLNFLLPT IFKSCSTFEQ WFNAPFAMTG ERVDLNEEET ILIIRRLHKV
LRPFLLRRLK KEVESQLPEK VEYVIKCDMS ALQKILYRHM QAKGILLTDG SEKDKGAKTL
MNTIMQLRKI CNHPYMFQHI EESFAEHLGY SNGVINGAEL YRASGKFELL DRILPKLRAT
NHRVLLFCQM TSLMTIMEDY FAFRNFLYLR LDGTTKSEDR AALLKKFNEP GSQYFIFLLS
TRAGGLGLNL QAADTVIIFD SDWNPHQDLQ AQDRAHRIGQ QNEVRVLRLC TVNSVEEKIL
AAAKYKLNVD QKVIQAGMFD QKSSSHERRA FLQAILEHEE ENEEEDEVPD DETLNQMIAR
REEEFDLFMR MDMDRRREDA RNPKRKPRLM EEDELPSWII KDDAEVERLT CEEEEEKIFG
RGSRQRRDVD YSDALTEKQW LRAIEDGNLE EMEEEVRLKK RKRRRNVDKD SGKEDGEKAK
KRRGRPPAEK LSPNPPKLTK QMNAIIDTVI NYKDSSGRQL SEVFIQLPSR KELPEYYELI
RKPVDFKKIK ERIRNHKYRS LGDLEKDVML LCHNAQTFNL EGSQIYEDSI VLQSVFKSAR
QKIAKEEESE DESNDDEEED EEEESESESK SVKVKIKLNK KDEKSREKGK GKKRQSRAKA
KPVVSDDDSD EDQDENDQSE ASGSDDE
//
