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Database: UniProt
Entry: A0A091I8R0_CALAN
LinkDB: A0A091I8R0_CALAN
Original site: A0A091I8R0_CALAN 
ID   A0A091I8R0_CALAN        Unreviewed;      1918 AA.
AC   A0A091I8R0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   Flags: Fragment;
GN   ORFNames=N300_14149 {ECO:0000313|EMBL:KFP04984.1};
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:KFP04984.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFP04984.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP04984.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; KL218430; KFP04984.1; -; Genomic_DNA.
DR   STRING; 9244.A0A091I8R0; -.
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:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR   CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR   CDD; cd18056; DEXHc_CHD4; 1.
DR   CDD; cd15531; PHD1_CHD_II; 1.
DR   CDD; cd15532; PHD2_CHD_II; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR009462; CHD_II_SANT-like.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 1.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF06461; CHDII_SANT-like; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01146; DUF1086; 1.
DR   SMART; SM01147; DUF1087; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000313|EMBL:KFP04984.1};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KFP04984.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          371..418
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          450..497
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          530..587
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          623..658
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          739..923
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1055..1204
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1344..1401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1526..1673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..538
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1379..1400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1536..1561
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1566..1587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1614..1653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1918
FT                   /evidence="ECO:0000313|EMBL:KFP04984.1"
SQ   SEQUENCE   1918 AA;  218615 MW;  188D9BA8AF64DA24 CRC64;
     MASGIGSPSP CSGGSDDDEM EILLNNTIPQ HPEPEEEPEE ELLSEAEAPK IKKKKKPKKL
     KEPKVPKLSK RQKKEVNERM PKLGDSSGEG NEFVEEEEEV LRSDSEGSDY TPGKKKKKKL
     GPKKEKKNKT KRKEEEEEEE EDDDSKEPKS SAQLLEDWGM EDIDHIFTEE DYRTLTNYKA
     FSQFVRPLIA AKNPKIAVSK MMMVLGAKWR EFSTNNPFKG ISGASVAAAA AAAVAVVESM
     VTNVDAVLPQ PPVDVPLRKA KTKEGKGPNA RRKPKATPRI PDIKKPKTKK VAPLKIKLGG
     FGSKRKRSSS EDDDLDVESD FDDASINSYS VSDGSTSRSS RSRKKLKAGK KKKKGEEDST
     VAVDGYETDH QDYCEVCQQG GEIILCDTCP RAYHMVCLDP DMEKAPEGKW SCPHCEKEGI
     QWEAKEDNSE GEEIMEDVVG DAEEEDDHHM EFCRVCKDGG ELLCCDACPS SYHIHCLNPP
     LPEIPNGEWL CPRCTCPALK GKVQKILIWK WGQPPVGPPP PRPPDADPNA PPPKPLEGRP
     ERQFFVKWQG MSYWHCSWVS ELQLELHCQV MFRNYQRKND MDEPPSGDFG GEEEKSRKRK
     NKDPKYAEME ERFYRYGIKP EWMMIHRILN HSVDKKGNVH YLIKWRDLPY DQASWESEDV
     DIQDYDLFKQ SYWNHRELMR GEEGRPGKKL KKVKMRKLER PPETPTVDPT VKYDRQPEYL
     DVTGGTLHPY QLEGLNWLRF SWAQGTDTIL ADEMGLGKTV QTAVFLYSLY KEGHSKGPFL
     VSAPLSTIIN WEREFEMWAP DMYVVTYVGD KDSRAIIREN EFTFEDNAIR GGKKASRMKK
     EAAVKFHVLL TSYELITIDM AILGSIDWAC LIVDEAHRLK NNQSKFFRVL NGYSLQHKLL
     LTGTPLQNNL EELFHLLNFL TPERFHNLEG FLEEFADIAK EDQIKKLHDM LGPHMLRRLK
     ADVFKNMPSK TELIVRVELS PMQKKYYKYI LTRNFEALNA RGGGNQVSLL NVVMDLKKCC
     NHPYLFPVAA MEAPKMPNGM YDGSALIRAS GKLLLLQKML KNLKEGGHRV LIFSQMTKML
     DLLEDFLEHE GYKYERIDGG ITGNMRQEAI DRFNAPGAQQ FCFLLSTRAG GLGINLATAD
     TVIIYDSDWN PHNDIQAFSR AHRIGQNKKV MIYRFVTRAS VEERITQVAK KKMMLTHLVV
     RPGLGSKTGS MSKQELDDIL KFGTEELFKD EATEGGDNKE GEDSSVIHYD DKAIERLLDR
     NQDETEDTEL QGMNEYLSSF KVAQYVVREE EMGEEEEVER EIIKQEESVD PDYWEKLLRH
     HYEQQQEDLA RNLGKGKRIR KQVNYNDGSQ EDRDWQDDQS DNQSDYSVAS EEGDEDFDER
     SEAARRPSRK GLRNDKDKPL PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT
     TQWLVRDLRG KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS
     LIRKKVQEFE HVNGRWSMPE LAEIEENKKL SQPSSPSPKT PTPSTPGDTQ PNTPAPVPPP
     EEGVKAEEGA SAKEQGESSE PEKDLNASAA ETEVPMECAQ PVETPPQEAK SPVNPTEADE
     KKLEEPEVKE RPDEPMEVES KADVEKAEDR APIENPPEPP IITLDEKDEK KDDDKKDVVM
     LQNGEMLKES VDERHKKAVK QRFMFNIADG GFTELHSLWQ NEERAATVTK KTYEIWHRRH
     DYWLLAGIIN HGYARWQDIQ NDPRYAILNE PFKGEMNRGN FLEIKNKFLA RRFKLLEQAL
     VIEEQLRRAA YLNMSEDPSH PSMALNTRFA EVECLAESHQ HLSKESMAGN KPANAVLHKV
     LKQLEELLSD MKADVTRLPA TIARIPPVAV RLQMSERNIL SRLANRSSEP PPPPPPQQ
//
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