ID A0A091ICB6_CALAN Unreviewed; 962 AA.
AC A0A091ICB6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JUN-2023, entry version 42.
DE SubName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 {ECO:0000313|EMBL:KFP06254.1};
DE Flags: Fragment;
GN ORFNames=N300_03048 {ECO:0000313|EMBL:KFP06254.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP06254.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP06254.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP06254.1};
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. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KL218525; KFP06254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ICB6; -.
DR STRING; 9244.A0A091ICB6; -.
DR Proteomes; UP000054308; 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; cd18064; DEXHc_SMARCA5; 1.
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:UP000054308}.
FT DOMAIN 113..278
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 408..559
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 761..813
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP06254.1"
FT NON_TER 962
FT /evidence="ECO:0000313|EMBL:KFP06254.1"
SQ SEQUENCE 962 AA; 112889 MW; FF4A56B00D4459EC CRC64;
FSHQQQTDRA NRFEYLLKQT ELFAHFIQPA AQKTPTSPLK MKPGRPRIKK DEKQNLLSVG
DYRHRRTEQE EDEELLTESS KTTNVCTRFE ESPSYVKSGK LRDYQVRGLN WLISLYENGI
NGILADEMGL GKTLQTISLL GYMKHYRNIP GPHMVLVPKS TLHNWVNEFK RWVPTLRAVC
LIGDKDQRAA FVRDVLLPGE WDVCVTSYEM LIKEKSVFKK FNWRYLVIDE AHRIKNEKSK
LSEIVREFKT TNRLLLTGTP LQNNLHELWA LLNFLLPDVF NSSEDFDSWF DTNNCLGDQK
LVERLHMVLR PFLLRRIKAD VEKSLPPKKE VKIYVGLSKM QREWYTRILM KDIDILNSAG
KLDKMRLLNI LMQLRKCCNH PYLFDGAEPG PPYTTDMHLV TNSGKMVVLD KLLPKLKEQG
SRVLIFSQMT RVLDILEDYC MWRNYEYCRL DGQTPHDERQ ASINAYNEPG SSKFVFMLST
RAGGLGINLA TADVVILYDS DWNPQVDLQA MDRAHRIGQT KTVRVFRFIT DNTVEERIVE
RAEMKLRLDS IVIQQGKLVD QNLNKLGKDE MLQMIRHGAT HVFASKESEI TDEDIDHILE
RGAKKTAEMN EKLSKMGESS LRNFTMDTES SVYNFEGEDY REKQKMAFTE WIEPPKRERK
ANYAVDAYFR EALRVSEPKA PKAPRPPKQP NVQDFQFFPP RLFELLEKEI LYYRKTIGYK
VPRNPDLPNA AQAQKEEQLK IDEAEPLNDE ELEEKEKLLT QGFTNWNKRD FNQFIKANEK
WGRDDIENIA REVEGKTPEE VIEYSAVFWE RCNELQDIEK IMAQIERGEA RIQRRISIKK
ALDTKVSSLY KAPFHQLRIS YGTNKGKNYT EEEDRFLICM LHKLGFDKEN VYDELRQCIR
NSPQFRFDWF LKSRTAMELQ RRCNTLITLI ERENMELEEK EKAEKKKRGP KPSSVRFREA
FL
//